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• W3100452120 abstract "Research Article15 December 1994free access Human cyclin F. C. Bai C. Bai Howard Hughes Medical Institute, Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030. Search for more papers by this author R. Richman R. Richman Howard Hughes Medical Institute, Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030. Search for more papers by this author S.J. Elledge S.J. Elledge Howard Hughes Medical Institute, Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030. Search for more papers by this author C. Bai C. Bai Howard Hughes Medical Institute, Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030. Search for more papers by this author R. Richman R. Richman Howard Hughes Medical Institute, Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030. Search for more papers by this author S.J. Elledge S.J. Elledge Howard Hughes Medical Institute, Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030. Search for more papers by this author Author Information C. Bai1, R. Richman1 and S.J. Elledge1 1Howard Hughes Medical Institute, Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030. The EMBO Journal (1994)13:6087-6098https://doi.org/10.1002/j.1460-2075.1994.tb06955.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Cyclins are important regulators of cell cycle transitions through their ability to bind and activate cyclin-dependent protein kinases. In mammals several classes of cyclins exist which are thought to co-ordinate the timing of different events necessary for cell cycle progression. Here we describe the identification of a novel human cyclin, cyclin F, isolated as a suppressor of the G1/S deficiency of a Saccharomyces cerevisiae cdc4 mutant. Cyclin F is the largest cyclin, with a molecular weight of 87 kDa, and migrates as a 100-110 kDa protein. It contains an extensive PEST-rich C-terminus and a cyclin box region that is most closely related to cyclins A and B. Cyclin F mRNA is ubiquitiously expressed in human tissues. It fluctuates dramatically through the cell cycle, peaking in G2 like cyclin A and decreasing prior to decline of cyclin B mRNA. Cyclin F protein accumulates in interphase and is destroyed at mitosis at a time distinct from cyclin B. Cyclin F shows regulated subcellular localization, being localized in the nucleus in most cells, with a significant percentage of cells displaying only perinuclear staining. Overexpression of cyclin F, or a mutant lacking the PEST region, in human cells resulted in a significant increase in the G2 population, implicating cyclin F in the regulation of cell cycle transitions. The ubiquitous expression and phylogentic conservation of cyclin F suggests that it is likely to coordinate essential cell cycle events distinct from those regulated by other cyclins. Previous ArticleNext Article Volume 13Issue 241 December 1994In this issue RelatedDetailsLoading ..." @default.
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• W3100452120 date "1994-12-01" @default.
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• W3100452120 title "Human cyclin F." @default.
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• W3100452120 doi "https://doi.org/10.1002/j.1460-2075.1994.tb06955.x" @default.
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