Show simple item record

dc.contributor.authorSuen, KinMan
dc.contributor.authorLin, Chichuan
dc.contributor.authorGeorge, Roger R.
dc.contributor.authorMelo, Fernando A.
dc.contributor.authorBiggs, Eleanor R.
dc.contributor.authorAhmed, Zamal
dc.contributor.authorDrake, Melanie N.
dc.contributor.authorArur, Swathi
dc.contributor.authorArold, Stefan T.
dc.contributor.authorLadbury, John E S D
dc.date.accessioned2015-08-03T11:04:27Z
dc.date.available2015-08-03T11:04:27Z
dc.date.issued2013-05-01
dc.identifier.issn15459993
dc.identifier.pmid23584453
dc.identifier.doi10.1038/nsmb2557
dc.identifier.doi10.1038/nsmb.2557
dc.identifier.urihttp://hdl.handle.net/10754/562754
dc.description.abstractControl mechanisms that prevent aberrant signaling are necessary to maintain cellular homeostasis. We describe a new mechanism by which the adaptor protein Shc directly binds the MAP kinase Erk, thus preventing its activation in the absence of extracellular stimuli. The Shc-Erk complex restricts Erk nuclear translocation, restraining Erk-dependent transcription of genes, including those responsible for oncogenic growth. The complex forms through unique binding sites on both the Shc PTB domain and the N-terminal lobe of Erk. Upon receptor tyrosine kinase stimulation, a conformational change within Shc - induced through interaction with the phosphorylated receptor - releases Erk, allowing it to fulfill its role in signaling. Thus, in addition to its established role in promoting MAP kinase signaling in stimulated cells, Shc negatively regulates Erk activation in the absence of growth factors and thus could be considered a tumor suppressor in human cells. © 2013 Nature America, Inc. All rights reserved.
dc.publisherNature Publishing Group
dc.titleInteraction with Shc prevents aberrant Erk activation in the absence of extracellular stimuli
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentComputational Bioscience Research Center (CBRC)
dc.contributor.departmentStructural Biology and Engineering
dc.identifier.journalNature Structural and Molecular Biology
dc.contributor.institutionDepartment of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Houston, TX, United States
dc.contributor.institutionGraduate School of Biomedical Sciences, University of Texas MD Anderson Cancer Center, Houston, TX, United States
dc.contributor.institutionProtein Purification Facility, London Research Institute, Cancer Research UK, London, United Kingdom
dc.contributor.institutionDepartment of Biology and Biochemistry, University of Bath, Bath, United Kingdom
dc.contributor.institutionDepartment of Genetics, University of Texas MD Anderson Cancer Center, Houston, TX, United States
dc.contributor.institutionCenter for Biomolecular Structure and Function, University of Texas MD Anderson Cancer Center, Houston, TX, United States
kaust.personArold, Stefan T.


This item appears in the following Collection(s)

Show simple item record