Colocalisation of CD9 and mortalin in CD9-induced mitotic catastrophe in human prostate cancer cells.
CD9, a member of the tetraspanin family of proteins, is involved in a variety of cellular interactions with many other proteins and molecules. Although CD9 has been implicated in cell fusion, migration and cancer progression, the detailed function of this protein is not completely understood and likely depends on interactions with different protein partners, which are not yet all known. Using co-immunoprecipitation and mass-spectrometric protein sequencing, we have identified in prostate cancer cells, a novel CD9 partner, the 75-kDa protein HSPA9B, also known as mortalin. We further show that introduction and overexpression of wild-type CD9 into human PC-3 prostate cancer cells induces mitotic catastrophe. We also demonstrate, by immunocolocalisation studies, the interaction of CD9 and mortalin in PC-3 cells undergoing mitotic catastrophe. Our results not only identified mortalin as a new CD9 partner, but also clarify the mechanisms by which CD9 may control prostate cancer progression.
Zvereff
V
V
Division of Experimental Medicine, Department of Medicine, McGill University, Montreal, Quebec, Canada.
Wang
J-C
JC
Shun
K
K
Lacoste
J
J
Chevrette
M
M
D015703:Antigens, CD / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D049109:Cell Proliferation; D005455:Fluorescent Antibody Technique; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D015151:Immunoblotting; D007124:Immunoenzyme Techniques; D047468:Immunoprecipitation; D008297:Male; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008938:Mitosis; D011471:Prostatic Neoplasms / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D060245:Tetraspanin 29; D014407:Tumor Cells, Cultured
D015703:Antigens, CD; C554869:CD9 protein, human; D018840:HSP70 Heat-Shock Proteins; D008562:Membrane Glycoproteins; D060245:Tetraspanin 29; C080352:mortalin