NDLI: Tyr728 in the kinase domain of the murine kinase suppressor of RAS 1 regulates binding and activation of the mitogen-activated protein kinase kinase.

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Tyr728 in the kinase domain of the murine kinase suppressor of RAS 1 regulates binding and activation of the mitogen-activated protein kinase kinase.

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Tyr728 in the kinase domain of the murine kinase suppressor of RAS 1 regulates binding and activation of the mitogen-activated protein kinase kinase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Baljuls, Angela Sibilski, Claudia Rudel, Thomas Rapp, Ulf R. Kollipara, Laxmikanth Mueller, Thomas Zahedi, René P.
Description	Author Affiliation: Sibilski C ( From the Department of Microbiology, Biocenter, and.)
Abstract	In metazoans, the highly conserved MAPK signaling pathway regulates cell fate decision. Aberrant activation of this pathway has been implicated in multiple human cancers and some developmental disorders. KSR1 functions as an essential scaffold that binds the individual components of the cascade and coordinates their assembly into multiprotein signaling platforms. The mechanism of KSR1 regulation is highly complex and not completely understood. In this study, we identified Tyr(728) as a novel regulatory phosphorylation site in KSR1. We show that Tyr(728) is phosphorylated by LCK, uncovering an additional and unexpected link between Src kinases and MAPK signaling. To understand how phosphorylation of Tyr(728) may regulate the role of KSR1 in signal transduction, we integrated structural modeling and biochemical studies. We demonstrate that Tyr(728) is involved in maintaining the conformation of the KSR1 kinase domain required for binding to MEK. It also affects phosphorylation and activation of MEK by RAF kinases and consequently influences cell proliferation. Moreover, our studies suggest that phosphorylation of Tyr(728) may affect the intrinsic kinase activity of KSR1. Together, we propose that phosphorylation of Tyr(728) may regulate the transition between the scaffolding and the catalytic function of KSR1 serving as a control point used to fine-tune cellular responses.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	49
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-12-06
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Mitogen-Activated Protein Kinase Kinases Metabolism Protein Kinases Chemistry Amino Acid Sequence Animals Cell Line Cell Proliferation Enzyme Activation Lymphocyte Specific Protein Tyrosine Kinase P56(lck) MAP Kinase Signaling System Mice Models, Molecular Molecular Dynamics Simulation Molecular Sequence Data Mutagenesis, Site-Directed Phosphorylation Protein Binding Protein Conformation Genetics Protein Structure, Tertiary Sequence Homology, Amino Acid Tyrosine Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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