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Gene Review:

Syt3 - synaptotagmin III

Mus musculus

Synonyms: AI385753, Synaptotagmin III, Synaptotagmin-3, SytIII, sytIII

Fukuda, M. et al., Ibata, K. et al., Berntson, A.K. et al.

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High impact information on Syt3

Based on the sequence comparison between the IP4-sensitive and -insensitive isoforms, we performed site-directed mutagenesis of synaptotagmin III and identified several amino acid substitutions that abolish IP4 binding activity [1].
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 [2].
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+ [2].
Distribution of the presynaptic calcium sensors, synaptotagmin I/II and synaptotagmin III, in the goldfish and rodent retinas [3].

References

Inositol 1,3,4,5-tetrakisphosphate binding activities of neuronal and non-neuronal synaptotagmins. Identification of conserved amino acid substitutions that abolish inositol 1,3,4,5-tetrakisphosphate binding to synaptotagmins III, V, and X. Ibata, K., Fukuda, M., Mikoshiba, K. J. Biol. Chem. (1998) [Pubmed]
Regulation by bivalent cations of phospholipid binding to the C2A domain of synaptotagmin III. Fukuda, M., Kojima, T., Mikoshiba, K. Biochem. J. (1997) [Pubmed]
Distribution of the presynaptic calcium sensors, synaptotagmin I/II and synaptotagmin III, in the goldfish and rodent retinas. Berntson, A.K., Morgans, C.W. Journal of vision [electronic resource]. (2003) [Pubmed]

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