Identification of protein substrates of Ca2+/calmodulin-dependent protein kinase II in the postsynaptic density by protein sequencing and mass spectrometry

被引：81

作者：

Yoshimura, Y

Shinkawa, T

Taoka, M

Kobayashi, K

Isobe, T

Yamauchi, T

机构：

[1] Univ Tokushima, Fac Pharmaceut Sci, Dept Biochem, Tokushima 7708505, Japan

[2] Tokyo Metropolitan Univ, Grad Sch Sci, Dept Chem, MEXT,Integrated Proteom Syst Project, Tokyo 158, Japan

[3] Tokyo Metropolitan Univ, Grad Sch Sci, Dept Chem, Hachioji, Tokyo 1920397, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 290卷 / 03期

关键词：

Ca2+/calmodulin-dependent protein kinase II (CaM kinase II); postsynaptic density; phosphorylation; two-dimensional gel electrophoresis; mass spectrometry; cytoskeletal protein; TOAD-64; PSD95/SAP90; SynGAP family;

D O I：

10.1006/bbrc.2001.6320

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：

Previously we detected more than 28 PSD proteins to be phosphorylated by CaM kinase II, and identified 14 protein substrates (Yoshimura, Y., Aoi, T., Yamauchi, T., Mol. Brain Res. 81, 118-128, 2000). In the present study, the remaining substrates were analyzed by protein sequencing and mass spectrometry. We found 6 proteins not previously known to be substrates of CaM kinase II, namely PSD95-associated protein, SAP97, TOAD-64, TNF receptor-associated protein, insulin-receptor tyrosine kinase 58153 kDa substrate, and homer 1b. (C) 2002 Elsevier Science (USA).

引用

页码：948 / 954

页数：7

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