Phorbol Myristate Acetate Induces the Phosphorylation of Plasma Membrane‐Associated Proteins in Sea Urchin Eggs: Protein phosphorylation/protein kinase C/egg activation

D. E. Chandler, V. D. Vacquier

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Immediately after fertilization sea urchin eggs undergo an increase in cytoplasmic pH from 6.8 to 7.2. This pH change occurs by activation of a Na+/H+ antiporter, and is a necessary signal for later steps in metabolic activation of development. Activators of protein kinase C such as phorbol myristate acetate (PMA) and diacylglycerol produce a similar pH increase in eggs. Phosphorylation of the antiporter or a regulatory protein may be a step in activating Na+/H+ exchange. Here we show that treatment of sea urchin eggs (S. purpuratus) with PMA results in increased phosphorylation of over a dozen proteins. Of these, three proteins of Mr=240, 92 and 80 kD are located in the egg cortex; under‐representation of these bands in isolated cortical granules suggests that they are plasma membrane‐associated. Phosphorylation of the 92 kD band is concentration‐dependent over a range of 10 to 1000 nM PMA and occurs over a time‐course of 1 to 3 min. Phosphoamino acid analysis indicates that phosphorylation is on serine residues. Phosphorylation appeares to be mediated by protein kinase C since the inactive PMA analogue, 4α‐phorbol 12, 13‐didecanoate, does not induce phosphorylation nor does experimental alkalinization of the egg cytoplasm.

Original languageEnglish (US)
Pages (from-to)49-59
Number of pages11
JournalDevelopment, Growth & Differentiation
Volume30
Issue number1
DOIs
StatePublished - Feb 1988

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology

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