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PMID: 7624798 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27.

Science (New York, N.Y.) ·Vol. 269 ·No. 5224 ·1995-08-04 ·Pages 682-5

Pagano M, Tam SW, Theodoras AM, Beer-Romero P, Del Sal G, Chau V, Yew PR, Draetta GF, Rolfe M

Abstract

The p27 mammalian cell cycle protein is an inhibitor of cyclin-dependent kinases. Both in vivo and in vitro, p27 was found to be degraded by the ubiquitin-proteasome pathway. The human ubiquitin-conjugating enzymes Ubc2 and Ubc3 were specifically involved in the ubiquitination of p27. Compared with proliferating cells, quiescent cells exhibited a smaller amount of p27 ubiquitinating activity, which accounted for the marked increase of p27 half-life measured in these cells. Thus, the abundance of p27 in cells is regulated by degradation. The specific proteolysis of p27 may represent a mechanism for regulating the activity of cyclin-dependent kinases.

MeSH Terms

Adenosine Triphosphate/metabolism Anaphase-Promoting Complex-Cyclosome Animals Cell Cycle Proteins Cell Line Cyclin-Dependent Kinase Inhibitor p27 Cyclin-Dependent Kinases/antagonists & inhibitors Cysteine Endopeptidases/metabolism Electroporation Enzyme Inhibitors/metabolism Humans Kinetics Leupeptins/pharmacology Ligases/metabolism Mice Microtubule-Associated Proteins/metabolism Multienzyme Complexes/metabolism Proteasome Endopeptidase Complex Rabbits Recombinant Proteins/metabolism Succinates/pharmacology Tumor Cells, Cultured Tumor Suppressor Proteins Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligase Complexes Ubiquitin-Protein Ligases Ubiquitins/metabolism

Chemicals

Cdkn1b protein, mouse Cell Cycle Proteins Enzyme Inhibitors Leupeptins Microtubule-Associated Proteins Multienzyme Complexes Recombinant Proteins Succinates Tumor Suppressor Proteins Ubiquitins acetylleucyl-leucyl-norleucinal Cyclin-Dependent Kinase Inhibitor p27 2,3-epoxysuccinic acid Adenosine Triphosphate CDC34 protein, human Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligase Complexes Anaphase-Promoting Complex-Cyclosome Ubiquitin-Protein Ligases Cyclin-Dependent Kinases Cysteine Endopeptidases Proteasome Endopeptidase Complex Ligases

Authors & Affiliations

9 authors, click to expand affiliations / ORCID

Pagano M

Mitotix Inc., Cambridge, MA 02139, USA.

Tam S W

Theodoras A M

Beer-Romero P

Del Sal G

Chau V

Yew P R

Draetta G F

Rolfe M

Article Info

Journal

Science (New York, N.Y.)

Abbr.

Science

ISSN

0036-8075

DOI

10.1126/science.7624798

Published

1995-08-04

Pages

682-5

Language

English

Region

United States

NLM ID

0404511

Subset

Corrections

CommentIn

PMID: 7624789

External Links

PubMed source DOI: 10.1126/science.7624798 View journal details

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Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27.

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