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GRP94 (endoplasmin) co‐purifies with and is phosphorylated by Golgi apparatus casein kinase
Author(s) -
Brunati Anna Maria,
Contri Antonella,
Muenchbach Martin,
James Peter,
Marin Oriano,
Pinna Lorenzo A.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01378-8
Subject(s) - golgi apparatus , casein kinase 2 , casein kinase 1 , casein , biochemistry , casein kinase 2, alpha 1 , phosphorylation , protein kinase a , kinase , biology , chemistry , microbiology and biotechnology , mitogen activated protein kinase kinase , endoplasmic reticulum
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.