rabphilin3的C2A和C2B结构域与钙离子和磷脂的相互作用。

Interaction of both the C2A and C2B domains of rabphilin3 with Ca2+ and phospholipid.

作者信息

Oishi H, Sasaki T, Takai Y

机构信息

Department of Cell Physiology, National Institute for Physiological Sciences, Okazaki, Japan.

出版信息

Biochem Biophys Res Commun. 1996 Dec 13;229(2):498-503. doi: 10.1006/bbrc.1996.1833.

DOI:10.1006/bbrc.1996.1833

PMID:8954927

Abstract

Rabphilin3, a downstream target molecule of the Rab3 subfamily small G proteins, has two C2 domains (the C2A and C2B domains) at its C-terminal region and is implicated in Ca(2+)-dependent neurotransmitter release. Rabphilin3 interacts with Ca2+ and phospholipid at its C2 domain, but it remains to be clarified which domain, the C2A or C2B domain, interacts with these compounds. We have found here that both the C2A and C2B domains interact with Ca2+ with similar kinetics but interact with phospholipid with slightly different kinetics.

摘要

Rabphilin3是Rab3亚家族小G蛋白的下游靶分子，在其C末端区域有两个C2结构域（C2A和C2B结构域），并参与钙（2+）依赖性神经递质释放。Rabphilin3在其C2结构域与Ca2+和磷脂相互作用，但仍有待阐明是哪个结构域，即C2A还是C2B结构域，与这些化合物相互作用。我们在此发现，C2A和C2B结构域与Ca2+相互作用的动力学相似，但与磷脂相互作用的动力学略有不同。