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Phosphorylation of Syntaxin‐1a by casein kinase 2α regulates pre‐synaptic vesicle exocytosis from the reserve pool
Journal of Neurochemistry ( IF 4.7 ) Pub Date : 2020-08-27 , DOI: 10.1111/jnc.15161
Vanilla Hua Shi 1 , Tim J Craig 1, 2 , Paul Bishop 1 , Yasuko Nakamura 1 , Dan Rocca 1 , Kevin A Wilkinson 1 , Jeremy M Henley 1
Affiliation  

The t‐soluble NSF‐attachment protein receptor protein Syntaxin‐1a (Stx‐1a) is abundantly expressed at pre‐synaptic terminals where it plays a critical role in the exocytosis of neurotransmitter‐containing synaptic vesicles. Stx‐1a is phosphorylated by Casein kinase 2α (CK2α) at Ser14, which has been proposed to regulate the interaction of Stx‐1a and Munc‐18 to control of synaptic vesicle priming. However, the role of CK2α in synaptic vesicle dynamics remains unclear. Here, we show that CK2α over‐expression reduces evoked synaptic vesicle release. Furthermore, shRNA‐mediated knockdown of CK2α in primary hippocampal neurons strongly enhanced vesicle exocytosis from the reserve pool, with no effect on the readily releasable pool of primed vesicles. In neurons in which endogenous Stx‐1a was knocked down and replaced with a CK2α phosphorylation‐deficient mutant, Stx‐1a(D17A), vesicle exocytosis was also increased. These results reveal a previously unsuspected role of CK2α phosphorylation in specifically regulating the reserve synaptic vesicle pool, without changing the kinetics of release from the readily releasable pool.

中文翻译:

酪蛋白激酶 2α 对 Syntaxin-1a 的磷酸化调节储备池的突触前小泡胞吐作用

t 可溶性 NSF 附着蛋白受体蛋白 Syntaxin-1a (Stx-1a) 在突触前末端大量表达,在含有神经递质的突触小泡的胞吐作用中发挥关键作用。Stx-1a 被酪蛋白激酶 2α (CK2α) 在 Ser14 位点磷酸化,已被提议调节 Stx-1a 和 Munc-18 的相互作用以控制突触小泡启动。然而,CK2α 在突触小泡动力学中的作用仍不清楚。在这里,我们表明 CK2α 过表达减少了诱发的突触小泡释放。此外,shRNA 介导的原代海马神经元中 CK2α 的敲低强烈增强了储备池中的囊泡胞吐作用,而对易于释放的已启动囊泡池没有影响。在内源性 Stx-1a 被敲除并被 CK2α 磷酸化缺陷突变体 Stx-1a(D17A) 取代的神经元中,囊泡胞吐作用也增加了。这些结果揭示了 CK2α 磷酸化在特异性调节储备突触小泡池中的先前未预料到的作用,而不会改变从易于释放的池中释放的动力学。
更新日期:2020-08-27
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