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.
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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