| Autor: |
Morgan A; The Physiological Laboratory, School of Biomedical Sciences, University of Liverpool, Liverpool, UK. amorgan@liv.ac.uk, Burgoyne RD, Barclay JW, Craig TJ, Prescott GR, Ciufo LF, Evans GJ, Graham ME |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical Society transactions [Biochem Soc Trans] 2005 Dec; Vol. 33 (Pt 6), pp. 1341-4. |
| DOI: |
10.1042/BST0331341 |
| Abstrakt: |
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-25 and Munc18 by PKC regulates distinct stages of exocytosis. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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