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

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 190卷 / 03期

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

页码：927 / 934

页数：8

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