| Interacting proteins: P08133 and P04271 |
Pubmed |
SVM Score :0.0 |
| Annexin 6 binds S100A1 and S100B and blocks the ability of S100A1 and S100B to inhibit desmin and GFAP assemblies into intermediate filaments . ^^^ Annexin 6 , a member of a family of Ca ( 2+ ) dependent phospholipid and membrane binding proteins , interacts with the Ca ( 2+ ) regulated EF hand proteins , S100A1 and S100B , and blocks the ability of these two proteins to inhibit the assembly of desmin and glial fibrillary acidic protein ( GFAP ) into intermediate filaments in a Ca ( 2+ ) and dose dependent manner . ^^^ S100A1 and S100B each possess one annexin 6 binding site , characterized by an affinity for annexin 6 in the submicromolar range . ^^^ As S100A1 and S100B exist in solution as homodimers in which the two monomers are related by a 2 fold symmetry axis , each of the above S 100 homodimers likely crosslinks two annexin 6 molecules , a situation that appears typical of all the annexin S 100 protein complexes described thus far . ^^^ However , whereas in the cases of other annexin S 100 complexes the C terminal extension of the S 100 molecule appears indispensable for annexin binding , the annexin 6 binding site can not be restricted to the S100A1 and S100B C terminal extension . ^^^ |
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| Interacting proteins: P08133 and P04271 |
Pubmed |
SVM Score :0.0 |
| Chromatographic procedures and amino acid sequence analysis were used in this study to identify seven calcium binding proteins , annexin 6 , cap g , annexin 5 , calmodulin , S100A11 , S100B and S100A6 , associated with uveal melanoma , the primary ocular tumor of adults . ^^^ |
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| Interacting proteins: P08133 and P04271 |
Pubmed |
SVM Score :0.0 |
| Previous work has shown that S100A1 and S100B bind annexin 6 in a Ca ( 2+ ) dependent manner and that annexin 6 , but not annexin 5 , blocks the inhibitory effect of S100A1 and S100B on intermediate filament assembly . ^^^ We show here that both halves of annexin 6 ( i . e . , the N terminal half or annexin 6 a and the C terminal half or annexin 6 b ) bind individual S100s on unique sites and that annexin 6 b , but not annexin 6 a , blocks the ability of S100A1 and S100B to inhibit intermediate filament assembly . ^^^ We also show that the C terminal extension of S100A1 ( and , by analogy , S100B ) , that was previously demonstrated to be critical for S100A1 and S100B binding to several target proteins including intermediate filament subunits , is not part of the S 100 surface implicated in the recognition of annexin 6 , annexin 6 a , or annexin 6 b . ^^^ |
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| Interacting proteins: P08133 and P04271 |
Pubmed |
SVM Score :0.0 |
| Annexin 5 , annexin 6 , S100A1 and S100B in developing and adult avian skeletal muscles . ^^^ In the present study , annexin 5 , annexin 6 ( or ANXA 5 and ANXA 6 , respectively , according to a novel nomenclature ) , S100A1 and S100B were analyzed for their subcellular localization in developing and adult avian skeletal muscles by confocal laser scanning microscopy , immunogold cytochemistry , and western blotting , and for their ability to form annexin S 100 heterocomplex in vivo by immunoprecipitation . ^^^ These four proteins displayed distinct expression patterns , ANXA 5 being the first to be expressed in myotubes ( i . e . at embryonic day 8 ) , followed by ANXA 6 ( at embryonic day 12 ) and S100A1 and S100B ( between embryonic day 12 and embryonic day 15 ) . ^^^ From our data we suggest that : ( 1 ) ANXA 5 and ANXA 6 , and S100A1 and S100B can be used as markers of skeletal muscle development ; ( 2 ) ANXA 6 and S100A1 and S100B appear strategically located close to or on skeletal muscle membrane organelles that are critically involved in the regulation of Ca2+ fluxes , thus supporting previous in vitro observations implicating S100A1 and ANXA 6 in the stimulation of Ca2+ induced Ca2+ release ; and ( 3 ) ANXA6 / S100A1 and ANXA6 / S100B complexes can form in vivo thereby regulating each other activities and / or acting in concert to regulate membrane associated activities . . ^^^ |
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