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Cell

Title:		CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression
Author(s):		Truman AW; Kristjansdottir K; Wolfgeher D; Hasin N; Polier S; Zhang H; Perrett S; Prodromou C; Jones GW; Kron SJ;
Address:		"Ludwig Center for Metastasis Research, The University of Chicago, Chicago, IL 60637, USA"
Journal Title:		Cell
Year:		2012
Volume:		151
Issue:		6
Page Number:		1308 - 1318
DOI:		10.1016/j.cell.2012.10.051
ISSN/ISBN:		1097-4172 (Electronic) 0092-8674 (Print) 0092-8674 (Linking)
Abstract:		"In budding yeast, the essential functions of Hsp70 chaperones Ssa1-4 are regulated through expression level, isoform specificity, and cochaperone activity. Suggesting a novel regulatory paradigm, we find that phosphorylation of Ssa1 T36 within a cyclin-dependent kinase (CDK) consensus site conserved among Hsp70 proteins alters cochaperone and client interactions. T36 phosphorylation triggers displacement of Ydj1, allowing Ssa1 to bind the G1 cyclin Cln3 and promote its degradation. The stress CDK Pho85 phosphorylates T36 upon nitrogen starvation or pheromone stimulation, destabilizing Cln3 to delay onset of S phase. In turn, the mitotic CDK Cdk1 phosphorylates T36 to block Cln3 accumulation in G2/M. Suggesting broad conservation from yeast to human, CDK-dependent phosphorylation of Hsc70 T38 similarly regulates Cyclin D1 binding and stability. These results establish an active role for Hsp70 chaperones as signal transducers mediating growth control of G1 cyclin abundance and activity"
Keywords:		Adenosine Triphosphatases/*metabolism Cell Cycle Cell Proliferation Cyclin D1/metabolism Cyclins/*metabolism HEK293 Cells HSC70 Heat-Shock Proteins/metabolism HSP70 Heat-Shock Proteins/*metabolism Humans Phosphorylation Saccharomyces cerevisiae/cytology/*;
Notes:		"MedlineTruman, Andrew W Kristjansdottir, Kolbrun Wolfgeher, Donald Hasin, Naushaba Polier, Sigrun Zhang, Hong Perrett, Sarah Prodromou, Chrisostomos Jones, Gary W Kron, Stephen J eng 095605/Wellcome Trust/United Kingdom GM60443/GM/NIGMS NIH HHS/ 095605/Z11/Z/WT_/Wellcome Trust/United Kingdom R01 GM060443/GM/NIGMS NIH HHS/ R01 CA164492/CA/NCI NIH HHS/ Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't 2012/12/12 Cell. 2012 Dec 7; 151(6):1308-18. doi: 10.1016/j.cell.2012.10.051"