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

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 microM) 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.[1]


  1. GRP94 (endoplasmin) co-purifies with and is phosphorylated by Golgi apparatus casein kinase. Brunati, A.M., Contri, A., Muenchbach, M., James, P., Marin, O., Pinna, L.A. FEBS Lett. (2000) [Pubmed]
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