| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The mammalian gene of acetylcholinesterase associated collagen . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Human endplate acetylcholinesterase deficiency caused by mutations in the collagen like tail subunit ( ColQ ) of the asymmetric enzyme . ^^^ In skeletal muscle , acetylcholinesterase ( AChE ) exists in homomeric globular forms of type T catalytic subunits ( ACHET ) and heteromeric asymmetric forms composed of 1 , 2 , or 3 tetrameric ACHET attached to a collagenic tail ( ColQ ) . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Mutation in the human acetylcholinesterase associated collagen gene , COLQ , is responsible for congenital myasthenic syndrome with end plate acetylcholinesterase deficiency ( Type Ic ) . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Acetylcholinesterase ( AChE ) occurs in both asymmetric forms , covalently associated with a collagenous subunit called Q ( ColQ ) , and globular forms that may be either soluble or membrane associated . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Congenital end plate acetylcholinesterase deficiency caused by a nonsense mutation and an A > G splice donor site mutation at position +3 of the collagenlike tail subunit gene ( COLQ ) : how does G at position +3 result in aberrant splicing . ^^^ Congenital end plate acetylcholinesterase ( AChE ) deficiency ( CEAD ) , the cause of a disabling myasthenic syndrome , arises from defects in the COLQ gene , which encodes the AChE triple helical collagenlike tail subunit that anchors catalytic subunits of AChE to the synaptic basal lamina . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The end plate species of acetylcholinesterase ( AChE ) is an asymmetric enzyme consisting of a collagenic tail subunit composed of three collagenic strands ( ColQ ) , each attached to a tetramer of the T isoform of the catalytic subunit ( AChE ( T ) ) via a proline rich attachment domain . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The asymmetric form of acetylcholinesterase comprises three catalytic tetramers attached to ColQ , a collagen like tail responsible for the anchorage of the enzyme to the synaptic basal lamina . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| A component of collagen tailed acetylcholinesterase ( asymmetric ; A AChE ) in muscle forms a metabolically stable pool which can be released from the cell surface only by collagenase , suggesting that part of the enzyme is covalently bound by its tail ( COLQ ) subunits . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The synaptic CMS are caused by mutations in the collagenic tail subunit ( ColQ ) of the endplate species of acetylcholinesterase that prevent ColQ from associating with catalytic subunits or from insertion into the synaptic basal lamina . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| A basal lamina CMS is caused by mutations in the collagenic tail subunit ( ColQ ) of the endplate species of acetylcholinesterase that prevent the tail subunit from associating with catalytic subunits or from becoming inserted into the synaptic basal lamina . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Two novel mutations in the COLQ gene cause endplate acetylcholinesterase deficiency . ^^^ To date , all reported cases are due to mutations within the gene encoding ColQ , a specific collagen that anchors acetylcholinesterase in the basal lamina at the neuromuscular junction . ^^^ In both cases , the absence of acetylcholinesterase was demonstrated by morphological and biochemical analyses , and heteroallelic mutations in the COLQ gene were found . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| In the collagen tailed forms of cholinesterases , each subunit of a specific triple helical collagen , ColQ , may be attached through a proline rich domain ( PRAD ) situated in its N terminal noncollagenous region , to tetramers of acetylcholinesterase ( AChE ) or butyrylcholinesterase ( BChE ) . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Two different heparin binding domains in the triple helical domain of ColQ , the collagen tail subunit of synaptic acetylcholinesterase . ^^^ ColQ , the collagen tail subunit of asymmetric acetylcholinesterase , is responsible for anchoring the enzyme at the vertebrate synaptic basal lamina by interacting with heparan sulfate proteoglycans . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| A synaptic CMS is caused by mutations in the collagenic tail subunit ( ColQ ) of the endplate species of acetylcholinesterase that prevent the tail subunit from associating with catalytic subunits or from becoming inserted into the synaptic basal lamina . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The collagen tailed form of acetylcholinesterase ( A ( 12 ) AChE ) appears to be localized at the neuromuscular junction in association with the transmembrane dystroglycan complex through binding of its collagenic tail ( ColQ ) to the proteoglycan perlecan . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The C terminal t peptide ( 40 residues ) of vertebrate acetylcholinesterase ( AChE ) T subunits possesses a series of seven conserved aromatic residues and forms an amphiphilic alpha helix ; it allows the formation of homo oligomers ( monomers , dimers and tetramers ) and heteromeric associations with the anchoring proteins , ColQ and PRiMA , which contain a proline rich motif ( PRAD ) . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Transcriptional regulation of acetylcholinesterase associated collagen ColQ : differential expression in fast and slow twitch muscle fibers is driven by distinct promoters . ^^^ The presence of a collagenous protein ( ColQ ) characterizes the collagen tailed forms of acetylcholinesterase and butyrylcholinesterase at vertebrate neuromuscular junctions which is tethered in the synaptic basal lamina . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| At the neuromuscular junction , acetylcholinesterase ( AChE ) is mainly present as asymmetric forms in which tetramers of catalytic subunits are associated to a specific collagen , collagen Q ( ColQ ) . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Functional localization of acetylcholinesterase ( AChE ) in vertebrate muscle and brain depends on interaction of the tryptophan amphiphilic tetramerization ( WAT ) sequence , at the C terminus of its major splice variant ( T ) , with a proline rich attachment domain ( PRAD ) , of the anchoring proteins , collagenous ( ColQ ) and proline rich membrane anchor . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The expression of the synaptic asymmetric form of the enzyme acetylcholinesterase ( AChE ) depends of two different genes : the gene that encodes for the catalytic subunit and the gene that encodes for the collagenic tail , ColQ . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The authors describe two patients with congenital myasthenic syndrome ( CMS ) with end plate acetylcholinesterase ( AChE ) deficiency caused by mutations in the collagenic tail ( ColQ ) of AChE : a homozygous C terminal Y230S mutation in Patient 1 and Y430S and a C terminal splice site mutation in Patient 2 . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Two proteins , ColQ and PRiMA , organize tetramers of acetylcholinesterase ( AChE ) and of butyrylcholinesterase ( BChE ) through peptide interactions . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The blocking effect of tubocurarine on nerve evoked muscle twitches was determined in isolated diaphragm and EDL muscles , after inhibition of acetylcholinesterase by fasciculin 1 , butyrylcholinesterase by tetraisopropylpyro phosphoramide , or both acetylcholinesterase and butyrylcholinesterase by neostigmine , and in acetylcholinesterase deficient ColQ muscles . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| Transcriptional regulation of acetylcholinesterase associated collagen ColQ in fast and slow twitch muscle fibers . ^^^ The presence of a collagenous protein ( ColQ ) characterizes the collagen tailed forms of acetylcholinesterase ( AChE ) and butyrylcholinesterase at vertebrate neuromuscular junctions , which is tethered in the synaptic basal lamina . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| In neuromuscular junctions , the main form of acetylcholinesterase ( AChE ) is a hetero oligomer in which the catalytic subunits are associated to a specific collagen , ColQ . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The association of tetrameric acetylcholinesterase with ColQ tail : a block normal mode analysis . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The asymmetric A 12 acetylcholinesterase ( AChE ) molecular form , consisting of three tetrameric catalytic oligomers and three non catalytic subunits of collagen Q ( ColQ ) , is the functional AChE form in the neuromuscular junction . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| In the collagen tailed forms , AChE ( T ) subunits are associated with a specific collagen , ColQ , which is encoded by a single gene in mammals . ^^^ ColQ contains a short peptidic motif , the proline rich attachment domain ( PRAD ) , that triggers the formation of AChE ( T ) tetramers , from monomers and dimers . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| We have previously shown that collagen Q ( ColQ ) anchors AChE at the neuromuscular junction . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| BACKGROUND : The EP species AChE is an asymmetric enzyme consisting of a tail subunit composed of three collagenic strands ( ColQ ) , each attached to a tetramer of catalytic subunits . ^^^ Human EP AChE deficiency is caused by mutations in COLQ . ^^^ CONCLUSIONS : 1 ) After mutations in the AChR epsilon subunit , mutations in COLQ are emerging as second most common cause of congenital myasthenic syndromes . 2 ) A founder effect is likely for G240X in the Palestinian Arab families . 3 ) That mutations predicting total absence of AChE from the EP have variable phenotypic expressivity suggests that modifying genes or environmental factors can partially compensate for EP AChE deficiency . . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The association of AChE ( T ) or BChE subunits with ColQ produces collagen tailed molecules , which are inserted in the extracellular matrix , e . g . in the basal lamina of neuromuscular junctions . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| The splice to exon 5 produces the GPI anchored form of AChE found in the hematopoietic system , whereas the splice to exon 6 produces a sequence that binds to the structural subunits PRiMA and ColQ , producing AChE expression in brain and muscle . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| In these cells , a fraction of AChE subunits is associated with a triple helical collagen , ColQ , each strand of which can recruit a tetramer of AChE ( T ) . ^^^ Interaction of AChE ( T ) subunits with the complete collagen tail ColQ increased enzyme activity in cultured cells , as well as in muscle fibers in vivo . ^^^ Truncated ColQ subunits , presenting more or less extensive C terminal deletions , also increased AChE activity and secretion in C2C12 cells , although the triple helix could not form in the case of the larger deletion . ^^^ Coinjections of AChE ( T ) and ColQ resulted in the production and secretion of asymmetric forms , indicating that assembly , processing , and externalization of these molecules can occur outside the junctional region of muscle fibers and hence does not require the specialized junctional Golgi apparatus . . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| By coinjecting Xenopus oocytes with AChE ( T ) and ColQ mRNAs , we reproduced the muscle patterns of collagen tailed forms . ^^^ |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P22303 and Q9Y215 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The mammalian gene of acetylcholinesterase associated collagen . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Mutation in the human acetylcholinesterase associated collagen gene , COLQ , is responsible for congenital myasthenic syndrome with end plate acetylcholinesterase deficiency ( Type Ic ) . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Transcriptional regulation of acetylcholinesterase associated collagen ColQ in fast and slow twitch muscle fibers . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Human endplate acetylcholinesterase deficiency caused by mutations in the collagen like tail subunit ( ColQ ) of the asymmetric enzyme . ^^^ In skeletal muscle , acetylcholinesterase ( AChE ) exists in homomeric globular forms of type T catalytic subunits ( ACHET ) and heteromeric asymmetric forms composed of 1 , 2 , or 3 tetrameric ACHET attached to a collagenic tail ( ColQ ) . ^^^ Coexpression of each COLQ mutant with wild type ACHET in SV 40 transformed monkey kidney fibroblast ( COS ) cells reveals that a mutation proximal to the ColQ attachment domain for ACHET prevents association of ColQ with ACHET ; mutations distal to the attachment domain generate a mutant approximately 10 . 5S species of AChE composed of one ACHET tetramer and a truncated ColQ strand . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Acetylcholinesterase ( AChE ) occurs in both asymmetric forms , covalently associated with a collagenous subunit called Q ( ColQ ) , and globular forms that may be either soluble or membrane associated . ^^^ Acetylcholinesterase ( AChE ) occurs in both asymmetric forms , covalently associated with a collagenous subunit called Q ( ColQ ) , and globular forms that may be either soluble or membrane associated . ^^^ AChE has also been hypothesized to play developmental roles in the nervous system , and ColQ is also expressed in some AChE poor tissues . ^^^ To seek roles of ColQ and AChE at synapses and elsewhere , we generated ColQ deficient mutant mice . ^^^ ColQ / mice completely lacked asymmetric AChE in skeletal and cardiac muscles and brain ; they also lacked asymmetric forms of the AChE homologue , butyrylcholinesterase . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| In the collagen tailed forms , AChE ( T ) subunits are associated with a specific collagen , ColQ , which is encoded by a single gene in mammals . ^^^ ColQ contains a short peptidic motif , the proline rich attachment domain ( PRAD ) , that triggers the formation of AChE ( T ) tetramers , from monomers and dimers . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Congenital end plate acetylcholinesterase deficiency caused by a nonsense mutation and an A > G splice donor site mutation at position +3 of the collagenlike tail subunit gene ( COLQ ) : how does G at position +3 result in aberrant splicing . ^^^ Congenital end plate acetylcholinesterase ( AChE ) deficiency ( CEAD ) , the cause of a disabling myasthenic syndrome , arises from defects in the COLQ gene , which encodes the AChE triple helical collagenlike tail subunit that anchors catalytic subunits of AChE to the synaptic basal lamina . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| By coinjecting Xenopus oocytes with AChE ( T ) and ColQ mRNAs , we reproduced the muscle patterns of collagen tailed forms . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The end plate species of acetylcholinesterase ( AChE ) is an asymmetric enzyme consisting of a collagenic tail subunit composed of three collagenic strands ( ColQ ) , each attached to a tetramer of the T isoform of the catalytic subunit ( AChE ( T ) ) via a proline rich attachment domain . ^^^ Human end plate AChE deficiency was recently shown to be caused by mutations in COLQ . ^^^ We here report nine novel COLQ mutations in 7 patients with end plate AChE deficiency . ^^^ We examine the effects of the mutations on the assembly of asymmetric AChE by coexpressing each genetically engineered COLQ mutant with ACHE ( T ) in COS cells . ^^^ We classify the newly recognized and previously reported COLQ mutations into four classes according to their position in ColQ and their effect on AChE expression . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The asymmetric form of acetylcholinesterase comprises three catalytic tetramers attached to ColQ , a collagen like tail responsible for the anchorage of the enzyme to the synaptic basal lamina . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| A component of collagen tailed acetylcholinesterase ( asymmetric ; A AChE ) in muscle forms a metabolically stable pool which can be released from the cell surface only by collagenase , suggesting that part of the enzyme is covalently bound by its tail ( COLQ ) subunits . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| We have previously shown that collagen Q ( ColQ ) anchors AChE at the neuromuscular junction . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| BACKGROUND : The EP species AChE is an asymmetric enzyme consisting of a tail subunit composed of three collagenic strands ( ColQ ) , each attached to a tetramer of catalytic subunits . ^^^ Human EP AChE deficiency is caused by mutations in COLQ . ^^^ CONCLUSIONS : 1 ) After mutations in the AChR epsilon subunit , mutations in COLQ are emerging as second most common cause of congenital myasthenic syndromes . 2 ) A founder effect is likely for G240X in the Palestinian Arab families . 3 ) That mutations predicting total absence of AChE from the EP have variable phenotypic expressivity suggests that modifying genes or environmental factors can partially compensate for EP AChE deficiency . . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| In these cells , a fraction of AChE subunits is associated with a triple helical collagen , ColQ , each strand of which can recruit a tetramer of AChE ( T ) . ^^^ Interaction of AChE ( T ) subunits with the complete collagen tail ColQ increased enzyme activity in cultured cells , as well as in muscle fibers in vivo . ^^^ Truncated ColQ subunits , presenting more or less extensive C terminal deletions , also increased AChE activity and secretion in C2C12 cells , although the triple helix could not form in the case of the larger deletion . ^^^ Coinjections of AChE ( T ) and ColQ resulted in the production and secretion of asymmetric forms , indicating that assembly , processing , and externalization of these molecules can occur outside the junctional region of muscle fibers and hence does not require the specialized junctional Golgi apparatus . . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The synaptic CMS are caused by mutations in the collagenic tail subunit ( ColQ ) of the endplate species of acetylcholinesterase that prevent ColQ from associating with catalytic subunits or from insertion into the synaptic basal lamina . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The association of AChE ( T ) or BChE subunits with ColQ produces collagen tailed molecules , which are inserted in the extracellular matrix , e . g . in the basal lamina of neuromuscular junctions . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| A basal lamina CMS is caused by mutations in the collagenic tail subunit ( ColQ ) of the endplate species of acetylcholinesterase that prevent the tail subunit from associating with catalytic subunits or from becoming inserted into the synaptic basal lamina . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Two novel mutations in the COLQ gene cause endplate acetylcholinesterase deficiency . ^^^ To date , all reported cases are due to mutations within the gene encoding ColQ , a specific collagen that anchors acetylcholinesterase in the basal lamina at the neuromuscular junction . ^^^ In both cases , the absence of acetylcholinesterase was demonstrated by morphological and biochemical analyses , and heteroallelic mutations in the COLQ gene were found . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| In the collagen tailed forms of cholinesterases , each subunit of a specific triple helical collagen , ColQ , may be attached through a proline rich domain ( PRAD ) situated in its N terminal noncollagenous region , to tetramers of acetylcholinesterase ( AChE ) or butyrylcholinesterase ( BChE ) . ^^^ We further show that AChE subunits can associate with nonhelical collagen ColQ monomers , forming ColQ associated tetramers ( G 4 Q ) , which are secreted or are anchored at the cell surface when the C terminal domain of ColQ is replaced by a GPI addition signal . . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Two different heparin binding domains in the triple helical domain of ColQ , the collagen tail subunit of synaptic acetylcholinesterase . ^^^ ColQ , the collagen tail subunit of asymmetric acetylcholinesterase , is responsible for anchoring the enzyme at the vertebrate synaptic basal lamina by interacting with heparan sulfate proteoglycans . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| A synaptic CMS is caused by mutations in the collagenic tail subunit ( ColQ ) of the endplate species of acetylcholinesterase that prevent the tail subunit from associating with catalytic subunits or from becoming inserted into the synaptic basal lamina . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The collagen tailed form of acetylcholinesterase ( A ( 12 ) AChE ) appears to be localized at the neuromuscular junction in association with the transmembrane dystroglycan complex through binding of its collagenic tail ( ColQ ) to the proteoglycan perlecan . ^^^ Mutations in COLQ cause endplate AChE deficiency in humans . ^^^ Nine previously reported and three novel mutations are in CTD of ColQ , and most CTD mutations do not abrogate formation of A ( 12 ) AChE in transfected COS cells . ^^^ Patient endplates , however , are devoid of AChE , suggesting that CTD mutations affect anchoring of ColQ to the synaptic basal lamina . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Transcriptional regulation of acetylcholinesterase associated collagen ColQ : differential expression in fast and slow twitch muscle fibers is driven by distinct promoters . ^^^ The presence of a collagenous protein ( ColQ ) characterizes the collagen tailed forms of acetylcholinesterase and butyrylcholinesterase at vertebrate neuromuscular junctions which is tethered in the synaptic basal lamina . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| At the neuromuscular junction , acetylcholinesterase ( AChE ) is mainly present as asymmetric forms in which tetramers of catalytic subunits are associated to a specific collagen , collagen Q ( ColQ ) . ^^^ Together , our data suggest that a ternary complex containing ColQ , perlecan , and MuSK is required for AChE clustering and support the notion that MuSK dictates AChE synaptic localization at the neuromuscular junction . . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Functional localization of acetylcholinesterase ( AChE ) in vertebrate muscle and brain depends on interaction of the tryptophan amphiphilic tetramerization ( WAT ) sequence , at the C terminus of its major splice variant ( T ) , with a proline rich attachment domain ( PRAD ) , of the anchoring proteins , collagenous ( ColQ ) and proline rich membrane anchor . ^^^ Each WAT makes similar but unique interactions , consistent with an asymmetric pattern of disulfide linkages between the AChE tetramer subunits and ColQ . ^^^ The P59Q mutation in ColQ , which causes congenital endplate AChE deficiency , and is located within the PRAD , disrupts crucial WAT WAT and WAT PRAD interactions . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The expression of the synaptic asymmetric form of the enzyme acetylcholinesterase ( AChE ) depends of two different genes : the gene that encodes for the catalytic subunit and the gene that encodes for the collagenic tail , ColQ . ^^^ Recent evidence support this notion : first , the presence of two heparin binding domains in ColQ that interact with heparan sulfate proteoglycans ( HSPGs ) at the synaptic basal lamina ; and second , a knockout mouse for perlecan , a HSPG concentrated in nerve muscle contact , in which absence of asymmetric AChE at the NMJ is observed . ^^^ The physiological importance of collagen tailed AChE form in skeletal muscle has been illustrated by the identification of several mutations in the ColQ gene . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The authors describe two patients with congenital myasthenic syndrome ( CMS ) with end plate acetylcholinesterase ( AChE ) deficiency caused by mutations in the collagenic tail ( ColQ ) of AChE : a homozygous C terminal Y230S mutation in Patient 1 and Y430S and a C terminal splice site mutation in Patient 2 . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The C terminal t peptide ( 40 residues ) of vertebrate acetylcholinesterase ( AChE ) T subunits possesses a series of seven conserved aromatic residues and forms an amphiphilic alpha helix ; it allows the formation of homo oligomers ( monomers , dimers and tetramers ) and heteromeric associations with the anchoring proteins , ColQ and PRiMA , which contain a proline rich motif ( PRAD ) . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| Two proteins , ColQ and PRiMA , organize tetramers of acetylcholinesterase ( AChE ) and of butyrylcholinesterase ( BChE ) through peptide interactions . ^^^ A short proline rich sequence in the N terminal domain of ColQ or PRiMA associates four C terminal extension of AChE or BChE . ^^^ At the neuromuscular junction , ColQ / AChE represents the concentrated enzyme . ^^^ The clusterisation of AChE depends upon ColQ through three sites of interactions : two different heparin binding domains in the collagen domain interact with heparan sulfate proteoglycan particularly the perlecan and the C terminal non collagenic domain interacts with MuSK , the tyrosine kinase receptor organiser of the neuromuscular junction . ^^^ The absence of ColQ and AChE has revealed that the excess of Ach stimulates more nicotinic receptors but probably not until their desensitization . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The blocking effect of tubocurarine on nerve evoked muscle twitches was determined in isolated diaphragm and EDL muscles , after inhibition of acetylcholinesterase by fasciculin 1 , butyrylcholinesterase by tetraisopropylpyro phosphoramide , or both acetylcholinesterase and butyrylcholinesterase by neostigmine , and in acetylcholinesterase deficient ColQ muscles . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The splice to exon 5 produces the GPI anchored form of AChE found in the hematopoietic system , whereas the splice to exon 6 produces a sequence that binds to the structural subunits PRiMA and ColQ , producing AChE expression in brain and muscle . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| In neuromuscular junctions , the main form of acetylcholinesterase ( AChE ) is a hetero oligomer in which the catalytic subunits are associated to a specific collagen , ColQ . ^^^ Then , AChE clusters appear with the onset of contraction and correlate with a dramatic increase in AChE , ColQ 1 and ColQ1A mRNA levels in muscle cells . ^^^ AChE aggregates are organized by a ternary complex , which involves direct interactions between ColQ , perlecan and MuSK . . ^^^ |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The association of tetrameric acetylcholinesterase with ColQ tail : a block normal mode analysis . ^^^ In physiological conditions , AChE exists as tetramers associated with the proline rich attachment domain ( PRAD ) of either collagen like Q subunit ( ColQ ) or proline rich membrane anchoring protein . ^^^ Recently , the crystal structure of the tryptophan amphiphilic tetramerization ( WAT ) domain of AChE associated with PRAD ( [ WAT ] 4PRAD ) , which mimics the interface between ColQ and AChE tetramer , became available . ^^^ In this study we built a complete tetrameric mouse [ AChE ( T ) ] 4 ColQ atomic structure model , based on the crystal structure of the [ WAT ] 4PRAD complex . ^^^ This model can be used to study the implications of the association of AChE with ColQ . . ^^^ |
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| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| The asymmetric A 12 acetylcholinesterase ( AChE ) molecular form , consisting of three tetrameric catalytic oligomers and three non catalytic subunits of collagen Q ( ColQ ) , is the functional AChE form in the neuromuscular junction . ^^^ |
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| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q9Y215 and P22303 |
Pubmed |
SVM Score :0.0 |
| NA |
|