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Activation of yeast plasma membrane ATPase by phorbol ester.

作者信息

Portillo F, Mazón M J

出版信息

FEBS Lett. 1985 Nov 11;192(1):95-8. doi: 10.1016/0014-5793(85)80050-8.

DOI:10.1016/0014-5793(85)80050-8
PMID:2996943
Abstract

Addition of 12-O-tetradecanoylphorbol-13-acetate (TPA) to yeast cells produces a 2-fold activation of the plasma membrane ATPase. The activation is reversible and time-and dose-dependent. The activated enzyme shows an increased affinity for its substrate, ATP, and its optimum pH is shifted to a more alkaline range. These changes are similar to those observed in the reported activation by glucose. Upon incubation of yeast cells with 32Pi incorporation of radioactivity in a membrane polypeptide of 105 kDa is observed after addition of either glucose or TPA.

摘要

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