GRP94 (endoplasmin) co-purifies with and is phosphorylated by Golgi apparatus casein kinase

被引:42
作者
Brunati, AM
Contri, A
Muenchbach, M
James, P
Marin, O
Pinna, LA
机构
[1] CNR, Dipartimento Chim Biol, Ctr Studio Biomembrane, I-35121 Padua, Italy
[2] Univ Padua, CRIBI, I-35121 Padua, Italy
[3] Swiss Fed Inst Technol, Prot Chem Lab, Zurich, Switzerland
来源
FEBS LETTERS | 2000年 / 471卷 / 2-3期
关键词
casein kinase; protein kinase; Golgi apparatus; GRP94; endoplasmin; phosphorylation;
D O I
10.1016/S0014-5793(00)01378-8
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
A phosphorylatable protein band of about 94 kDa (as judged by SDS-PAGE) which co-purifies and co-immunoprecipitates with Golgi apparatus casein kinase (C-CK) from rat lactating mammary gland has been shown bg mass spectrometric sequence analysis to be identical or very similar to the glucose-regulated protein, GRP94, GRP94 is also readily phosphorylated by G-CK (K-m = 0.2 mu M) at seryl sites which are different from the sites affected by casein kinase-2 (CK2) in the same protein. A study with peptide substrates would indicate that the G-CK sites in GRP94 conform to the motif S-R/K-E-X (X being different from D and E) which is not recognized by CK2. (C) 2000 Federation of European Biochemical Societies.
引用
收藏
页码:151 / 155
页数:5
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