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PMID: 2555717 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs.

Nature ·Vol. 342 ·No. 6249 ·1989-11-30 ·Pages 505-11

Watanabe N, Vande Woude GF, Ikawa Y, Sagata N

Abstract

The Xenopus c-mos proto-oncogene product, pp39mos, accumulates in the unfertilized egg during maturation, is hyperphosphorylated and exhibits protein kinase activity. On fertilization, or soon after the completion of meiosis, the accumulated pp39mos undergoes selective proteolysis. Using an in vitro protease assay system, we show here that this specific proteolysis is caused by the calcium-dependent cysteine protease, calpain.

MeSH Terms

Animals Calpain/metabolism Fertilization Gene Expression Regulation Growth Substances/metabolism Maturation-Promoting Factor Meiosis Molecular Weight Oocytes/physiology Phosphorylation Progesterone/pharmacology Proto-Oncogene Proteins/metabolism Proto-Oncogene Proteins c-mos RNA, Messenger/genetics Time Factors Xenopus laevis

Chemicals

Growth Substances Proto-Oncogene Proteins RNA, Messenger Progesterone Proto-Oncogene Proteins c-mos Maturation-Promoting Factor Calpain

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Watanabe N

Tsukuba Life Science Center Riken, Ibaraki, Japan.

Vande Woude G F

Ikawa Y

Sagata N

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/342505a0

Published

1989-11-30

Pages

505-11

Language

English

Region

England

NLM ID

0410462

Subset

Corrections

CommentIn

PMID: 2531291

External Links

PubMed source DOI: 10.1038/342505a0 View journal details

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Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs.

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