Regulation of exocytosis by protein kinase C
Regulation of exocytosis by protein kinase C
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DOI：
10.1042/bst0331341
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发表时间：
2005-12-01
影响因子：
3.9
通讯作者：
Graham, ME
中科院分区：
文献类型：
--
作者：
Morgan, A;Burgoyne, RD;Graham, ME
PKC（蛋白激酶C）多年来被认为调节多种细胞类型中的受调节的胞吐作用。在神经元和神经内分泌细胞中，PKC调节胞吐过程的几个不同阶段，表明PKC的这些多重作用是由不同蛋白质靶点的磷酸化介导的。近年来，各种胞吐蛋白已被鉴定为PKC底物，其中最具特征的是SNAP-25（25 kDa突触体相关蛋白）和Munc 18。在本研究中，我们回顾了最近的证据表明，位点特异性磷酸化的SNAP-2S和Munc 18的PKC调节不同阶段的胞吐。
PKC (protein kinase C) has been known for many years to modulate regulated exocytosis in a wide variety of cell types. in neurons and neuroendocrine cells, PKC regulates several different stages of the exocytotic process, suggesting that these multiple actions of PKC are mediated by phosphorylation of distinct protein targets. In recent years, a variety of exocytotic proteins have been identified as PKC substrates, the best characterized of which are SNAP-25 (25 kDa synaptosome-associated protein) and Munc18. In the present study, we review recent evidence suggesting that site-specific phosphorylation of SNAP-2S and Munc18 by PKC regulates distinct stages of exocytosis.