| Interacting proteins: P22303 and Q86XR5 |
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 Q86XR5 |
Pubmed |
SVM Score :0.0 |
| Regulation of PRiMA : membrane anchor of acetylcholinesterase ( AChE ) in neuron and muscle . ^^^ |
|
| Interacting proteins: P22303 and Q86XR5 |
Pubmed |
SVM Score :0.0 |
| PRiMA : the membrane anchor of acetylcholinesterase in the brain . ^^^ |
|
| Interacting proteins: P22303 and Q86XR5 |
Pubmed |
SVM Score :0.0 |
| Expression of PRiMA in the mouse brain : membrane anchoring and accumulation of ' tailed ' acetylcholinesterase . ^^^ We analysed the expression of PRiMA ( proline rich membrane anchor ) , the membrane anchor of acetylcholinesterase ( AChE ) , by in situ hybridization in the mouse brain . ^^^ |
|
| Interacting proteins: P22303 and Q86XR5 |
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 Q86XR5 |
Pubmed |
SVM Score :0.0 |
| Tetramers of the ' tailed ' variant ( AChE ( T ) ) , which are anchored in the cell membrane of neurons by the PRiMA ( Proline Rich Membrane Anchor ) protein , constitute the main form of AChE in the mammalian brain . ^^^ |
|
| Interacting proteins: P22303 and Q86XR5 |
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 Q86XR5 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P22303 and Q86XR5 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P22303 and Q86XR5 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q86XR5 and P22303 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q86XR5 and P22303 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q86XR5 and P22303 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q86XR5 and P22303 |
Pubmed |
SVM Score :0.0 |
| PRiMA : the membrane anchor of acetylcholinesterase in the brain . ^^^ We have now cloned the gene PRiMA ( proline rich membrane anchor ) encoding the AChE anchor in mammalian brain . ^^^ We show that PRiMA is able to organize AChE into tetramers and to anchor them at the surface of transfected cells . ^^^ Furthermore , we demonstrate that AChE is actually anchored in neural cell membranes through its interaction with PRiMA . ^^^ Finally , we propose that only PRiMA anchors AChE in mammalian brain and muscle cell membranes . . ^^^ |
|
| Interacting proteins: Q86XR5 and P22303 |
Pubmed |
SVM Score :0.0 |
| Expression of PRiMA in the mouse brain : membrane anchoring and accumulation of ' tailed ' acetylcholinesterase . ^^^ We analysed the expression of PRiMA ( proline rich membrane anchor ) , the membrane anchor of acetylcholinesterase ( AChE ) , by in situ hybridization in the mouse brain . ^^^ We compared the pattern of PRiMA transcripts with that of AChE transcripts , as well as those of choline acetyltransferase and M 1 muscarinic receptors which are considered pre and postsynaptic cholinergic markers . ^^^ The results suggest that PRiMA expression is predominantly or exclusively related to the cholinergic system and that anchoring of cholinesterases to cell membranes by PRiMA represents a limiting factor for production of the AChE tailed splice variant ( AChET ) PRiMA complex , which represents the major AChE component in the brain . ^^^ |
|
| Interacting proteins: Q86XR5 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: Q86XR5 and P22303 |
Pubmed |
SVM Score :0.0 |
| Tetramers of the ' tailed ' variant ( AChE ( T ) ) , which are anchored in the cell membrane of neurons by the PRiMA ( Proline Rich Membrane Anchor ) protein , constitute the main form of AChE in the mammalian brain . ^^^ |
|
| Interacting proteins: Q86XR5 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 . ^^^ |
|
| Interacting proteins: Q86XR5 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: Q86XR5 and P22303 |
Pubmed |
SVM Score :0.0 |
| Regulation of PRiMA : membrane anchor of acetylcholinesterase ( AChE ) in neuron and muscle . ^^^ |
|