EVIDENCE THAT SER-82 IS A UNIQUE PHOSPHORYLATION SITE ON VIMENTIN FOR CA2+-CALMODULIN-DEPENDENT PROTEIN KINASE-II

被引：68
作者：
ANDO, S
TOKUI, T
YAMAUCHI, T
SUGIURA, H
TANABE, K
INAGAKI, M
机构：
[1] AICHI CANC CTR,RES INST,EXPTL RADIOL LAB,CHIKUSA KU,NAGOYA,AICHI 464,JAPAN
[2] TOKYO METROPOLITAN INST NEUROSCI,DEPT NEUROCHEM,FUCHU,TOKYO 183,JAPAN
[3] MIE UNIV,SCH MED,DEPT PATHOL,TSU,MIE 514,JAPAN
[4] AICHI CANC CTR,RES INST,BIOPHYS UNIT,CHIKUSA KU,NAGOYA,AICHI 464,JAPAN
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 175卷 / 03期
关键词：
D O I：
10.1016/0006-291X(91)91658-Y
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
We identified the sites on vimentin that are phosphorylated by Ca2+-calmodulin-dependent protein kinase II (CaM-kinase II). Sequential analysis of the purified phosphopeptides demonstrated that the sites are -Thr-Arg-Thr-Tyr-Ser(PO4)38-Leu-Gly-Ser-Ala- and -Val-Arg-Leu-Leu-Gln-Asp-Ser(PO4)82-Val-Asp-, which are located within the amino-terminal head domain of vimentin. For Ser-82 but not Ser-38, the proposed CaM-kinase II recognition amino acid sequence (Arg-X-X- Ser Thr) was not found. Studies with a series of synthetic peptide analogs corresponding to Ser-82 and its surrounding amino acid sequence indicate that Asp-84 acts as an essential substrate specificity determinant for the Ser-82 phosphorylation by CaM-kinase II. The CaM-kinase II recognition site may be more extensive than heretofore determined. © 1991.
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页码：955 / 962
页数：8
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