| Popis: |
Publisher Summary The absence of any tyrosine residues in the amino acid sequence of B-50 eliminates it as a potential substrate for tyrosine kinases. Of a number of serine/threonine protein kinases tested for their abilities to phosphorylate B-50, only casein kinase II has been reported to phosphorylate B-50 with stoichiometry similar to that seen with protein kinase C. This chapter summarizes this work, compares the properties of casein kinase II and protein kinase C-mediated phosphorylation of B-50, and discusses the potential relationship between casein kinase II-mediated phosphorylation of B-50 and growth-associated processes. In addition, work from this and other laboratories on dephosphorylation of B-50 by a number of identified protein phosphatases has been summarized in the chapter. |
