Document Detail

Calcium-dependent and -independent hetero-oligomerization in the synaptotagmin family.
MedLine Citation:
PMID:  11011146     Owner:  NLM     Status:  MEDLINE    
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.
M Fukuda; K Mikoshiba
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  128     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  2000 Oct 
Date Detail:
Created Date:  2000-12-22     Completed Date:  2000-12-22     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  637-45     Citation Subset:  IM    
Laboratory for Developmental Neurobiology, Brain Science Institute, RIKEN (The Institute of Physical and Chemical Research), Hirosawa, Wako, Saitama 351-0198, Japan.
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MeSH Terms
Base Sequence
COS Cells
Calcium / pharmacology*
Calcium-Binding Proteins / chemistry,  genetics,  metabolism
Cell Membrane / chemistry,  metabolism
Electrophoresis, Polyacrylamide Gel
Membrane Glycoproteins / chemistry*,  genetics,  metabolism*
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
Reg. No./Substance:
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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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