The cyclin B2 component of MPF is a substrate for the c-mosxe proto-oncogene product

Linda M. Roy; Balraj Singh; Jean Gautier; Ralph B. Arlinghaus; Steven K. Nordeen; James L. Maller

doi:10.1016/0092-8674(90)90192-H

The cyclin B2 component of MPF is a substrate for the c-mos^xe proto-oncogene product

Linda M. Roy, Balraj Singh, Jean Gautier, Ralph B. Arlinghaus, Steven K. Nordeen, James L. Maller

Surgical Oncology

Research output: Contribution to journal › Article › peer-review

99 Scopus citations

Abstract

Previous studies from this laboratory have shown that purified MPF from Xenopus eggs contains cyclin B2 complexed with cdc2 kinase. The activation of MPF during oocyte maturation is known to require expression of the c-mos^xe proto-oncogene. We show here that immunoprecipitates of either v-mos from Moloney murine sarcoma virus-transformed NIH 3T3 cells or c-mos from Xenopus eggs phosphorylate cyclin B2 in vitro. Phosphopeptide analysis reveals a pattern similar to that observed with cdc2 kinase. Moreover, ablation of c-mos^xe from oocytes by antisense oligonucleotide injection reduces the rate of cyclin B2 phosphorylation in oocyte extracts by 40%. These results suggest that the mechanism of activation of MPF by c-mos^xe involves phosphorylation of the cyclin component.

Original language	English (US)
Pages (from-to)	825-831
Number of pages	7
Journal	Cell
Volume	61
Issue number	5
DOIs	https://doi.org/10.1016/0092-8674(90)90192-H
State	Published - Jun 1 1990

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

Access to Document

10.1016/0092-8674(90)90192-H

Cite this

@article{dda13f38c9e8415484704d80533d09ad,

title = "The cyclin B2 component of MPF is a substrate for the c-mosxe proto-oncogene product",

abstract = "Previous studies from this laboratory have shown that purified MPF from Xenopus eggs contains cyclin B2 complexed with cdc2 kinase. The activation of MPF during oocyte maturation is known to require expression of the c-mosxe proto-oncogene. We show here that immunoprecipitates of either v-mos from Moloney murine sarcoma virus-transformed NIH 3T3 cells or c-mos from Xenopus eggs phosphorylate cyclin B2 in vitro. Phosphopeptide analysis reveals a pattern similar to that observed with cdc2 kinase. Moreover, ablation of c-mosxe from oocytes by antisense oligonucleotide injection reduces the rate of cyclin B2 phosphorylation in oocyte extracts by 40%. These results suggest that the mechanism of activation of MPF by c-mosxe involves phosphorylation of the cyclin component.",

author = "Roy, {Linda M.} and Balraj Singh and Jean Gautier and Arlinghaus, {Ralph B.} and Nordeen, {Steven K.} and Maller, {James L.}",

note = "Funding Information: We thank Tim Hunt and Jeremy Minshull (University of Cambridge, England) for providing bacterial strains carrying the cyclin 82 gene. This work was supported by grants from the National Institutes of Health (J. L. M. and R. 8. A.) and the Council for Tobacco Research (S. K. N.). J. G. is on leave from CNAS Unit 675, Toulouse, France. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact,",

year = "1990",

month = jun,

day = "1",

doi = "10.1016/0092-8674(90)90192-H",

language = "English (US)",

volume = "61",

pages = "825--831",

journal = "Cell",

issn = "0092-8674",

publisher = "Cell Press",

number = "5",

}

TY - JOUR

T1 - The cyclin B2 component of MPF is a substrate for the c-mosxe proto-oncogene product

AU - Roy, Linda M.

AU - Singh, Balraj

AU - Gautier, Jean

AU - Arlinghaus, Ralph B.

AU - Nordeen, Steven K.

AU - Maller, James L.

N1 - Funding Information: We thank Tim Hunt and Jeremy Minshull (University of Cambridge, England) for providing bacterial strains carrying the cyclin 82 gene. This work was supported by grants from the National Institutes of Health (J. L. M. and R. 8. A.) and the Council for Tobacco Research (S. K. N.). J. G. is on leave from CNAS Unit 675, Toulouse, France. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact,

PY - 1990/6/1

Y1 - 1990/6/1

N2 - Previous studies from this laboratory have shown that purified MPF from Xenopus eggs contains cyclin B2 complexed with cdc2 kinase. The activation of MPF during oocyte maturation is known to require expression of the c-mosxe proto-oncogene. We show here that immunoprecipitates of either v-mos from Moloney murine sarcoma virus-transformed NIH 3T3 cells or c-mos from Xenopus eggs phosphorylate cyclin B2 in vitro. Phosphopeptide analysis reveals a pattern similar to that observed with cdc2 kinase. Moreover, ablation of c-mosxe from oocytes by antisense oligonucleotide injection reduces the rate of cyclin B2 phosphorylation in oocyte extracts by 40%. These results suggest that the mechanism of activation of MPF by c-mosxe involves phosphorylation of the cyclin component.

AB - Previous studies from this laboratory have shown that purified MPF from Xenopus eggs contains cyclin B2 complexed with cdc2 kinase. The activation of MPF during oocyte maturation is known to require expression of the c-mosxe proto-oncogene. We show here that immunoprecipitates of either v-mos from Moloney murine sarcoma virus-transformed NIH 3T3 cells or c-mos from Xenopus eggs phosphorylate cyclin B2 in vitro. Phosphopeptide analysis reveals a pattern similar to that observed with cdc2 kinase. Moreover, ablation of c-mosxe from oocytes by antisense oligonucleotide injection reduces the rate of cyclin B2 phosphorylation in oocyte extracts by 40%. These results suggest that the mechanism of activation of MPF by c-mosxe involves phosphorylation of the cyclin component.

UR - http://www.scopus.com/inward/record.url?scp=0025338516&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025338516&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(90)90192-H

DO - 10.1016/0092-8674(90)90192-H

M3 - Article

C2 - 2140529

AN - SCOPUS:0025338516

SN - 0092-8674

VL - 61

SP - 825

EP - 831

JO - Cell

JF - Cell

IS - 5

ER -

The cyclin B2 component of MPF is a substrate for the c-mos^xe proto-oncogene product

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this