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

Michele Pagano; Sun W. Tam; Anne M. Theodoras; Peggy Beer-Romero; Giannino Del Sal; Vincent Chau; P. Renée Yew; Giulio F. Draetta; Mark Rolfe

doi:10.1126/science.7624798

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

Michele Pagano, Sun W. Tam, Anne M. Theodoras, Peggy Beer-Romero, Giannino Del Sal, Vincent Chau, P. Renée Yew, Giulio F. Draetta, Mark Rolfe

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

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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.

Original language	English (US)
Pages (from-to)	682-685
Number of pages	4
Journal	Science
Volume	269
Issue number	5224
DOIs	https://doi.org/10.1126/science.7624798
State	Published - 1995
Externally published	Yes

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@article{9811fec231194883bd35d2f6bb220079,

title = "Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27",

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.",

author = "Michele Pagano and Tam, {Sun W.} and Theodoras, {Anne M.} and Peggy Beer-Romero and {Del Sal}, Giannino and Vincent Chau and Yew, {P. Ren{\'e}e} and Draetta, {Giulio F.} and Mark Rolfe",

year = "1995",

doi = "10.1126/science.7624798",

language = "English (US)",

volume = "269",

pages = "682--685",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

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TY - JOUR

T1 - Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27

AU - Pagano, Michele

AU - Tam, Sun W.

AU - Theodoras, Anne M.

AU - Beer-Romero, Peggy

AU - Del Sal, Giannino

AU - Chau, Vincent

AU - Yew, P. Renée

AU - Draetta, Giulio F.

AU - Rolfe, Mark

PY - 1995

Y1 - 1995

N2 - 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.

AB - 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.

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JF - Science

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ER -

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

Abstract

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