Chondroitin sulfate proteoglycan 4 enhanced melanoma motility and growth requires a cysteine in the core protein transmembrane domain.

作者: Jianbo Yang , Matthew A. Price , Leah E.C. Wanshura , Jinsong He , Mei Yi

DOI: 10.1097/CMR.0000000000000574

关键词:

摘要: Chondroitin sulfate proteoglycan 4 (CSPG4) is a cell surface that enhances malignant potential in melanoma and several other tumor types. CSPG4 functions as transmembrane scaffold cells to activate oncogenic signaling pathways such focal adhesion kinase (FAK) extracellular signal regulated kinases 1,2, control motility, invasion anchorage independent growth. Here, we demonstrate promotes directional motility growth of by organizing positioning complex containing activated FAK lipid rafts within the plasma membrane migrating cells. This FAK-containing transduction platform, which consists syntenin-1, active Src caveolin-1 requires cytoplasmic domain for assembly. Enhanced promoted this also cysteine residue C2230. Substituting C2230 with alanine still permits assembly complex, however remains an inactive state. fails promote activation 1,2. Therapies target could be novel strategy limiting progression disrupting its function compartmentalized motogenic growth-promoting node.

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