Transformation by Rous sarcoma virus prevents acetylcholine receptor clustering on cultured chicken muscle fibers.
Acetylcholine receptors aggregate in the membrane of cultured chicken myotubes; the process of receptor clustering can be stimulated by exogenous factors that we, among others, have begun to characterize. Chicken myoblasts transformed by temperature-sensitive mutants of Rous sarcoma virus, such as tsNY68, fuse to form multinucleated myotubes at 42 degrees C, the nonpermissive temperature for transformation. However, tsNY68-infected myotubes do not cluster acetylcholine receptors at 42 degrees C, even in the presence of active clustering agents. This phenomenon is not merely a result of viral infection, since myotubes infected with a transformation-deficient viral mutant, td107A, behave like noninfected myotubes with respect to receptor clustering; thus, the effects of tsNY68 on the clustering process must be mediated by the src gene product. These experiments may provide a method of identifying essential elements of acetylcholine receptor clusters.
D000818:Animals; D001358:Avian Sarcoma Viruses / Q000235:genetics*; D002471:Cell Transformation, Neoplastic; D002478:Cells, Cultured; D002642:Chick Embryo; D004594:Electrophysiology; D005455:Fluorescent Antibody Technique; D008854:Microscopy, Electron; D009132:Muscles / Q000196:embryology / Q000502:physiology* / Q000648:ultrastructure; D009154:Mutation; D015688:Oncogene Protein pp60(v-src); D011494:Protein Kinases / Q000235:genetics; D011950:Receptors, Cholinergic / Q000378:metabolism*; D013696:Temperature; D014764:Viral Proteins / Q000235:genetics
D011950:Receptors, Cholinergic; D014764:Viral Proteins; D011494:Protein Kinases; D015688:Oncogene Protein pp60(v-src)