Retooling of the beta 4 integrin in tumor cells--ligands lost and kinase gained.
In carcinoma cells, the beta 4 integrin functions in a ligand-independent manner to promote proliferation, migration, and invasion. An interesting new paper describes a mechanism whereby the beta 4 integrin cytoplasmic tail becomes an integrin ligand-independent adaptor protein for the Met receptor tyrosine kinase, thereby enhancing the mitogenic, morphogenic, and motogenic properties of Met.
Hemler
M E
ME
Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.
D048868:Adaptor Proteins, Signal Transducing; D033942:Adaptor Proteins, Vesicular Transport; D000818:Animals; D015703:Antigens, CD / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D039663:Integrin beta4; D008024:Ligands; D008954:Models, Biological; D009374:Neoplasms, Experimental / Q000378:metabolism* / Q000473:pathology; D019869:Phosphatidylinositol 3-Kinases / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism; D019859:Proto-Oncogene Proteins c-met / Q000378:metabolism*; D055765:Shc Signaling Adaptor Proteins; D015398:Signal Transduction / Q000502:physiology; D000071425:Src Homology 2 Domain-Containing, Transforming Protein 1; D014407:Tumor Cells, Cultured
D048868:Adaptor Proteins, Signal Transducing; D033942:Adaptor Proteins, Vesicular Transport; D015703:Antigens, CD; D039663:Integrin beta4; D008024:Ligands; D011506:Proteins; C528024:SHC1 protein, human; D055765:Shc Signaling Adaptor Proteins; D000071425:Src Homology 2 Domain-Containing, Transforming Protein 1; D019869:Phosphatidylinositol 3-Kinases; D019859:Proto-Oncogene Proteins c-met