Effects of Zn 2+  ions on protein phosphorylation in epithelial cell membranes | Zendy

Alitalo Kari | Zendy; KeskiOja Jorma | Zendy; Bornstein Paul | Zendy

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Effects of Zn 2+ ions on protein phosphorylation in epithelial cell membranes

Author(s) -

Alitalo Kari,

KeskiOja Jorma,

Bornstein Paul

Publication year - 1983

Publication title -

journal of cellular physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.529

H-Index - 174

eISSN - 1097-4652

pISSN - 0021-9541

DOI - 10.1002/jcp.1041150314

Subject(s) - phosphorylation , divalent , phosphoprotein , threonine , membrane , phosphatase , vesicle , chemistry , serine , protein phosphorylation , dephosphorylation , kinase , biochemistry , biophysics , protein kinase a , biology , organic chemistry

The regulation of protein phosphorylation by Zn 2+ ions and by other divalent cations was studied in membrane vesicles from a normal mouse epithelial cell line, MMC‐E ( Mus musculus castaneous ). Four major phosphoacceptor polypeptides were found in these membranes. Micromolar concentrations of Zn 2+ ions inhibited the phosphorylation of the epidermal growth factor (EGF) receptor and of threonine residues in a 47,000‐dalton polypeptide. In contrast, two polypeptides with molecular weights of 54,000 and 57,000 showed increased phosphorylation, mainly of serine residues, in the p. esence of Zn 2+ ions. These results were not obtained using similar concentrations of other divalent cations and were apparently not due to an effect of Zn 2+ ions on phosphoprotein phosphatases. Thus, the effects of Zn 2+ ions on protein phosphorylation in membrane vesicles are complex and are not restricted to an inhibition of a single protein phosphatase or kinase.

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