• Login
    View Item 
    •   Home
    • UMass Chan Student Research and Publications
    • Morningside Graduate School of Biomedical Sciences
    • Morningside GSBS Scholarly Publications
    • View Item
    •   Home
    • UMass Chan Student Research and Publications
    • Morningside Graduate School of Biomedical Sciences
    • Morningside GSBS Scholarly Publications
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of eScholarship@UMassChanCommunitiesPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywordsThis CollectionPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywordsProfilesView

    My Account

    LoginRegister

    Help

    AboutSubmission GuidelinesData Deposit PolicySearchingAccessibilityTerms of UseWebsite Migration FAQ

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Formation of c-Cbl.phosphatidylinositol 3-kinase complexes on lymphocyte membranes by a p56lck-independent mechanism

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Hartley, David Alan
    Corvera, Silvia
    UMass Chan Affiliations
    Department of Cell Biology
    Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    1996-09-06
    Keywords
    1-Phosphatidylinositol 3-Kinase; Binding Sites; Cell Membrane; Cytoskeleton; Cytosol; Humans; Lymphocyte Specific Protein Tyrosine Kinase p56(lck); Lymphocytes; Multienzyme Complexes; Phosphotransferases (Alcohol Group Acceptor); Proto-Oncogene Proteins; Proto-Oncogene Proteins c-cbl; Structure-Activity Relationship; *Ubiquitin-Protein Ligases; src-Family Kinases
    Life Sciences
    Medicine and Health Sciences
    
    Metadata
    Show full item record
    Link to Full Text
    http://www.jbc.org/content/271/36/21939.short
    Abstract
    The proto-oncogene c-Cbl was originally identified as a cellular homologue of the transforming protein expressed by the murine Cas NS-1 retrovirus. The full-length c-Cbl protein is a predominantly cytoplasmic protein, abundant in lymphoid cells, and potentially involved in signal transduction in several cell types. The specific signal transduction pathways in which c-Cbl participates, and its precise role in these pathways, are unclear. Previous studies from our laboratory have shown that c-Cbl is the predominant tyrosine-phosphorylated protein bound to the p85 subunit of phosphatidylinositol (PI) 3-kinase on T lymphocyte and B lymphocyte activation. To further understand the properties of c-Cbl and the significance of its interactions with PI 3-kinase, we have further studied the cellular biological and biochemical responses of c-Cbl to stimulation in lymphoid cells. We show that stimulation induces the association of a highly tyrosine-phosphorylated pool of c-Cbl with lymphocyte membranes and with a detergent-insoluble particulate fraction. Immunoprecipitation of c-Cbl from subcellular fractions reveals that p85 is predominantly associated with the c-Cbl pool recovered from the membrane fraction, despite the fact that this pool represents a small amount of total cellular c-Cbl. The formation of c-Cbl.PI 3-kinase complexes on lymphocyte membranes did not depend on the catalytic activity of PI 3-kinase since it was unaltered by the treatment of cells with wortmannin prior to stimulation. Interestingly, c-Cbl tyrosine phosphorylation and the formation of c-Cbl.PI 3-kinase complexes were also observed in a mutant Jurkat cell line, JCaM1.6, lacking p56(lck) expression. Because p56(lck) is critical for mitogenic signal transduction in response to T cell receptor activation, our results suggest that the activation of c-Cbl and the formation of c-Cbl.PI 3-kinase complexes occur upstream or independently of mitogenic signal transduction pathways in T cells.
    Source

    J Biol Chem. 1996 Sep 6;271(36):21939-43.

    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/33815
    PubMed ID
    8702998
    Related Resources

    Link to article in PubMed

    Collections
    Morningside GSBS Scholarly Publications

    entitlement

    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Lamar Soutter Library, UMass Chan Medical School | 55 Lake Avenue North | Worcester, MA 01655 USA
    Quick Guide | escholarship@umassmed.edu
    Works found in eScholarship@UMassChan are protected by copyright unless otherwise indicated.
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.