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    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 期刊論文 >  Protease-activated Receptor-1 Down-regulation: A MUTANT HeLa CELL LINE SUGGESTS NOVEL REQUIREMENTS FOR PAR1 PHOSPHORYLATION AND RECRUITMENT TO CLATHRIN-COATED PITS


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/81425


    Title: Protease-activated Receptor-1 Down-regulation: A MUTANT HeLa CELL LINE SUGGESTS NOVEL REQUIREMENTS FOR PAR1 PHOSPHORYLATION AND RECRUITMENT TO CLATHRIN-COATED PITS
    Authors: JoAnn Trejo;Yoram Altschuler;Hua-Wen Fu;Keith E. Mostov;Shaun R. Coughlin
    教師: 傅化文
    Date: 2000
    Publisher: American Society for Biochemistry and Molecular Biology
    Relation: Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, Volume 275, Issue 40, OCT 2000, Pages 31255-31265
    Keywords: MAP KINASE CASCADE
    THROMBIN-RECEPTOR
    COUPLED RECEPTOR
    STRUCTURAL REQUIREMENTS
    VESICLE FORMATION
    BETA-ARRESTIN
    SUBSTANCE-P
    INTERNALIZATION
    DYNAMIN
    RESENSITIZATION
    Abstract: Protease-activated receptor-1 (PAR1), a G protein-coupled receptor (GPCR) for thrombin, is irreversibly activated by a proteolytic mechanism, then internalized and degraded in lysosomes. The latter is critical for temporal fidelity of thrombin signaling. Toward understanding PAR1 down-regulation, we first investigated the pathway of PAR1 internalization. Activated PAR1 was rapidly recruited to clathrin-coated pits, where it colocalized with transferrin receptor (TfnR). Dominant-negative dynamin and clathrin hub mutants both blocked PAR1 internalization. Blockade of PAR1 internalization with dynamin K44A also inhibited activation-dependent PAR1 degradation. Thus activated PAR1 internalizes via clathrin-coated pits together with receptors that recycle and is then sorted away from such receptors and delivered to lysosomes. In the course of these studies we identified a mutant HeLa cell line, designated JT1, that was defective in PAR1 internalization. PAR1 signaled robustly in JT1 cells but was not phosphorylated or recruited to clathrin-coated pits after activation. Internalization of TfnR was intact in JT1 cells and internalization of β2-adrenergic receptor, a GPCR that internalizes and recycles, was present but perhaps reduced. Taken together, these studies suggest that PAR1 is internalized in a dynamin- and clathrin-dependent manner like TfnR and β2-adrenergic receptor but requires a distinct gene product for recruitment into this pathway.
    Relation Link: http://www.asbmb.org/
    URI: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/81425
    Appears in Collections:[分子與細胞生物研究所] 期刊論文
    [生命科學系] 期刊論文

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