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在氨基末端头部结构域的三个丝氨酸/苏氨酸残基处,结蛋白的cdc2激酶磷酸化作用。

cdc2 kinase phosphorylation of desmin at three serine/threonine residues in the amino-terminal head domain.

作者信息

Kusubata M, Matsuoka Y, Tsujimura K, Ito H, Ando S, Kamijo M, Yasuda H, Ohba Y, Okumura E, Kishimoto T

机构信息

Department of Neurophysiology, Tokyo Metropolitan Institute of Gerontology, Japan.

出版信息

Biochem Biophys Res Commun. 1993 Feb 15;190(3):927-34. doi: 10.1006/bbrc.1993.1138.

DOI:10.1006/bbrc.1993.1138
PMID:8439342
Abstract

Phosphorylation of desmin filament by cdc2 kinase induced a transition toward the depolymerized state of the filament. Sequence analysis of purified phosphopeptides derived from cdc2 kinase-phosphorylated desmin revealed that Ser-6, Ser-22 and Thr-64 in the N-terminal head domain were the sites phosphorylated.

摘要

细胞周期蛋白依赖性激酶2(cdc2激酶)使结蛋白丝磷酸化,导致丝向解聚状态转变。对源自cdc2激酶磷酸化结蛋白的纯化磷酸肽进行序列分析,结果显示N端头部结构域中的丝氨酸-6、丝氨酸-22和苏氨酸-64是磷酸化位点。

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