| Calcium-dependent and -independent hetero-oligomerization in the synaptotagmin family. | |
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MedLine Citation:
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PMID: 11011146 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Synaptotagmins constitute a family of membrane proteins that are characterized by one transmembrane region and two C2 domains. Recent genetic and biochemical studies have indicated that oligomerization of synaptotagmin (Syt) I is important for expression of function during exocytosis of synaptic vesicles. However, little is known about hetero-oligomerization in the synaptotagmin family. In this study, we showed that the synaptotagmin family is a type I membrane protein (N(lumen)/C(cytoplasm)) by introducing an artificial N-glycosylation site at the N-terminal domain, and systematically examined all the possible combinations of hetero-oligomerization among synaptotagmin family proteins (Syts I-XI). We classified the synaptotagmin family into four distinct groups based on differences in Ca(2+)-dependent and -independent oligomerization activity. Group A Syts (III, V, VI, and X) form strong homo- and hetero-oligomers by disulfide bonds at an N-terminal cysteine motif irrespective of the presence of Ca(2+) [Fukuda, M., Kanno, E., and Mikoshiba, K. (1999) J. Biol. Chem. 274, 31421-31427]. Group B Syts (I, II, VIII, and XI) show moderate homo-oligomerization irrespective of the presence of Ca(2+). Group C synaptotagmins are characterized by weak Ca(2+)-dependent (Syts IX) or no homo-oligomerization activity (Syt IV). Syt VII (Group D) has unique Ca(2+)-dependent homo-oligomerization properties with EC(50) values of about 150 microM Ca(2+) [Fukuda, M., and Mikoshiba, K. (2000) J. Biol. Chem. 275, 28180-28185]. Syts IV, VIII, and XI did not show any apparent hetero-oligomerization activity, but some sets of synaptotagmin isoforms can hetero-oligomerize in a Ca(2+)-dependent and/or -independent manner. Our data suggest that Ca(2+)-dependent and -independent hetero-oligomerization of synaptotagmins may create a variety of Ca(2+)-sensors. |
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Authors:
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M Fukuda; K Mikoshiba |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of biochemistry Volume: 128 ISSN: 0021-924X ISO Abbreviation: J. Biochem. Publication Date: 2000 Oct |
Date Detail:
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Created Date: 2000-12-22 Completed Date: 2000-12-22 Revised Date: 2007-12-19 |
Medline Journal Info:
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Nlm Unique ID: 0376600 Medline TA: J Biochem Country: JAPAN |
Other Details:
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Languages: eng Pagination: 637-45 Citation Subset: IM |
Affiliation:
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Laboratory for Developmental Neurobiology, Brain Science Institute, RIKEN (The Institute of Physical and Chemical Research), Hirosawa, Wako, Saitama 351-0198, Japan. mnfukuda@brain.riken.go.jp |
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Base Sequence COS Cells Calcium / pharmacology* Calcium-Binding Proteins / chemistry, genetics, metabolism Cell Membrane / chemistry, metabolism Dimerization Electrophoresis, Polyacrylamide Gel Epitopes Glycosylation Membrane Glycoproteins / chemistry*, genetics, metabolism* Mice Molecular Sequence Data Nerve Tissue Proteins / chemistry*, genetics, metabolism* Precipitin Tests Protein Isoforms / chemistry, genetics, metabolism Protein Structure, Quaternary / drug effects Protein Structure, Tertiary / drug effects Recombinant Fusion Proteins / metabolism Synaptotagmins Transfection |
| Chemical | |
Reg. No./Substance:
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0/Calcium-Binding Proteins; 0/Epitopes; 0/Membrane Glycoproteins; 0/Nerve Tissue Proteins; 0/Protein Isoforms; 0/Recombinant Fusion Proteins; 134193-27-4/Synaptotagmins; 7440-70-2/Calcium |
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