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

FEBS Letters

Brunati, Anna Maria¹  James, Peter²  Muenchbach, Martin²  Pinna, Lorenzo A.¹  Marin, Oriano¹  Contri, Antonella¹ 

[1] Dipartimento di Chimica Biologica, Centro per lo Studio delle Biomembrane del CNR and CRIBI, University of Padova, Viale G. Colombo 3, 35121 Padua, Italy;Protein Chemistry Laboratory, ETH Zurich, Zurich, Switzerland

关键词: Casein kinase;    Protein kinase;    Golgi apparatus;    GRP94;    Endoplasmin;    Phosphorylation;    G-CK;    Golgi apparatus casein kinase;    CK2;    casein kinase-2;    GRP;    glucose-regulated protein;    FSBA;    p-fluorosulfonylbenzoyl 5′-adenosine;   

DOI  :  10.1016/S0014-5793(00)01378-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 (G-CK) from rat lactating mammary gland has been shown by 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 μM) 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.

【 授权许可】

Unknown