The degradation of p27 and cancer

Shuhei Kotoshiba, Keiichi Nakayama

Research output: Contribution to journalReview article

3 Citations (Scopus)

Abstract

The cell cycle of eukaryotic cells is regulated by a series of protein complexes composed of cyclins and cyclin-dependent kinases (CDKs), the activity of which is suppressed by a group of CDK inhibitors (CKIs). Among the CKIs, p27 plays a pivotal role in the control of cell proliferation. Degradation of p27 is a critical event for reentry of cells into the cell cycle from G0 phase and occurs through ubiquitination by two ubiquitin ligase complexes (KPC and SCFSkP2) and subsequent degradation by the 26S-proteasome. A tumor suppressing function of p27 has been demonstrated in mouse models and studies of human tumors. This review will focus on the regulation of p27 proteolysis and its consequences for tumorigenesis.

Original languageEnglish
Pages (from-to)2047-2056
Number of pages10
JournalNippon rinsho. Japanese journal of clinical medicine
Volume63
Issue number11
Publication statusPublished - Jan 1 2005

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Cyclin-Dependent Kinases
Cell Cycle
Cell Cycle Resting Phase
Cyclins
Ubiquitination
Eukaryotic Cells
Ligases
Ubiquitin
Proteolysis
Neoplasms
Carcinogenesis
Cell Proliferation
Proteins
ATP dependent 26S protease

All Science Journal Classification (ASJC) codes

  • Medicine(all)

Cite this

The degradation of p27 and cancer. / Kotoshiba, Shuhei; Nakayama, Keiichi.

In: Nippon rinsho. Japanese journal of clinical medicine, Vol. 63, No. 11, 01.01.2005, p. 2047-2056.

Research output: Contribution to journalReview article

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