Protein kinases associated with isolated mitotic spindles from mammalian cells: identification of a casein kinase II-like enzyme.
Mitotic spindles isolated from prometaphase-arrested mammalian cells contain associated protein kinases that are extracted by high salt treatment. Their fractionation by ion-exchange chromatography reveals three major peaks of protein kinase activity that phosphorylate brain microtubule-associated proteins and differ in their substrate specificity. One of them has been identified as a casein kinaseII-like enzyme. A mitotic spindle-associated 325 kDa protein related to brain MAP1B is a major substrate for this casein kinase II-like enzyme. Another mitotic spindle protein kinase has been tentatively identified as a proline-directed protein kinase.
Díaz-Nido
J
J
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Avila
J
J
D000818:Animals; D016466:CHO Cells; D047390:Casein Kinase II; D006224:Cricetinae; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000032:analysis*; D017346:Protein Serine-Threonine Kinases / Q000032:analysis*; D008941:Spindle Apparatus / Q000201:enzymology*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014407:Tumor Cells, Cultured
D008869:Microtubule-Associated Proteins; C085284:microtubule-associated protein 1B; D011494:Protein Kinases; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases