ArticleThe Biochemical journal1997
Regulation by bivalent cations of phospholipid binding to the C2A domain of synaptotagmin III.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 37 citations in OpenAlex.
- Divalent Cations and the Divergence ofBiochemistry · 2019Article
- Sensitivity of intracellular calcium-binding sites for exo- and endocytosis of synaptic vesicles to Sr, Ba, and Mg ions.Neuroscience and behavioral physiology · 2010Article
- DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated GLUT4 vesicle fusion in adipocytes.Diabetes · 2009Article
- The C2A domain of synaptotagmin-like protein 3 (Slp3) is an atypical calcium-dependent phospholipid-binding machine: comparison with the C2A domain of synaptotagmin I.The Biochemical journal · 2002Article
- Evidence for two distinct processes in the final stages of neurotransmitter release as detected by binomial analysis in calcium and strontium solutions.The Journal of physiology · 2002Article
- Cation charge and size selectivity of the C2 domain of cytosolic phospholipase A(2).Biochemistry · 2002Article
- The N-terminal cysteine cluster is essential for membrane targeting of B/K protein.The Biochemical journal · 2001Article
- Characterization of KIAA1427 protein as an atypical synaptotagmin (Syt XIII).The Biochemical journal · 2001Article
- Crystal structure of the cytosolic C2A-C2B domains of synaptotagmin III. Implications for Ca(+2)-independent snare complex interaction.The Journal of cell biology · 1999Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synaptotagmins are Ca2+-and phospholipid-binding proteins of synaptic vesicles that might function as Ca2+ receptors for neurotransmitter release via their first C2 (C2A) domain. Here we describe the effect of Mg2+ on phospholipid binding to the C2A domains of multiple synaptotagmins (II-VI), and demonstrate that only synaptotagmin III can bind negatively charged phospholipids [phosphatidylserine (PS) and phosphatidylinositol] in a Mg2+-dependent manner. The Mg2+-dependent interaction with PS was found to have an EC50 of approx. 30 microM Mg2+, which is comparable to that of Sr2+ and Ba2+ (EC50 values of approx. 10 microM). This binding property of the C2A domain is specific to synaptotagmin III, because none of the C2A domains of other proteins, such as rabphilin 3A, Doc2alpha, Doc2beta or Gap1(m), showed phospholipid binding activity in the presence of 1 mM Mg2+. Our results suggest that synaptotagmin III is involved in presynaptic functions different from those of synaptotagmins I and II.
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