CDC2 KINASE PHOSPHORYLATION OF DESMIN AT 3 SERINE THREONINE RESIDUES IN THE AMINO-TERMINAL HEAD DOMAIN

被引:32
作者
KUSUBATA, M
MATSUOKA, Y
TSUJIMURA, K
ITO, H
ANDO, S
KAMIJO, M
YASUDA, H
OHBA, Y
OKUMURA, E
KISHIMOTO, T
INAGAKI, M
机构
[1] TOKYO METROPOLITAN GERIATR HOSP & INST GERONTOL,DEPT NEUROPHYSIOL,35-2 SAKAE CHO,ITABASHI KU,TOKYO 173,JAPAN
[2] MIE UNIV,SCH MED,DEPT PATHOL,TSU,MIE 514,JAPAN
[3] NAGOYA CITY UNIV,FAC PHARMACEUT SCI,DEPT CHEM HYG & NUTR,MIZUHO KU,NAGOYA,AICHI 464,JAPAN
[4] AICHI CANC CTR,RES INST,BIOPHYS UNIT,CHIKUSA KU,NAGOYA,AICHI 464,JAPAN
[5] KANAZAWA UNIV,FAC PHARMACEUT SCI,DIV BIOL,KANAZAWA,ISHIKAWA 920,JAPAN
[6] TOKYO INST TECHNOL,FAC BIOSCI & BIOTECHNOL,CELL & DEV BIOL LAB,MIDORI KU,YOKOHAMA,KANAGAWA 227,JAPAN
关键词
D O I
10.1006/bbrc.1993.1138
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
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. © 1993 Academic Press.
引用
收藏
页码:927 / 934
页数:8
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