细胞周期蛋白依赖性激酶5对突触小泡内吞作用至关重要。
Cdk5 is essential for synaptic vesicle endocytosis.
作者信息
Tan Timothy C, Valova Valentina A, Malladi Chandra S, Graham Mark E, Berven Leise A, Jupp Orla J, Hansra Gurdip, McClure Sonya J, Sarcevic Boris, Boadle Ross A, Larsen Martin R, Cousin Michael A, Robinson Phillip J
机构信息
Cell Signalling Unit, Children's Medical Research Institute, Locked Bag 23, Wentworthville, NSW 2145, Australia.
出版信息
Nat Cell Biol. 2003 Aug;5(8):701-10. doi: 10.1038/ncb1020.
Synaptic vesicle endocytosis (SVE) is triggered by calcineurin-mediated dephosphorylation of the dephosphin proteins. SVE is maintained by the subsequent rephosphorylation of the dephosphins by unidentified protein kinases. Here, we show that cyclin-dependent kinase 5 (Cdk5) phosphorylates dynamin I on Ser 774 and Ser 778 in vitro, which are identical to its endogenous phosphorylation sites in vivo. Cdk5 antagonists and expression of dominant-negative Cdk5 block phosphorylation of dynamin I, but not of amphiphysin or AP180, in nerve terminals and inhibit SVE. Thus Cdk5 has an essential role in SVE and is the first dephosphin kinase identified in nerve terminals.
突触小泡内吞作用（SVE）由钙调磷酸酶介导的去磷酸蛋白去磷酸化引发。SVE通过去磷酸蛋白随后被未知蛋白激酶重新磷酸化得以维持。在此，我们表明细胞周期蛋白依赖性激酶5（Cdk5）在体外使发动蛋白I的丝氨酸774和丝氨酸778位点磷酸化，这与其在体内的内源性磷酸化位点相同。Cdk5拮抗剂和显性负性Cdk5的表达可阻断神经末梢中发动蛋白I的磷酸化，但不影响发动蛋白、 amphiphysin或AP180的磷酸化，并抑制SVE。因此，Cdk5在SVE中起关键作用，并且是在神经末梢中鉴定出的首个去磷酸蛋白激酶。
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