Goblin (ankyrin) in striated muscle: Identification of the potential membrane receptor for erythroid spectrin in muscle cells
Goblin, a high molecular weight (Mr, 260,000) polypeptide of avian erythrocyte plasma membranes characterized by hormone-dependent phosphorylation, is shown by a variety of criteria to be the avian equivalent of ankyrin, the membrane attachment protein for spectrin; a polyclonal monospecific goblin antiserum reacts specifically with ankyrin from mammalian erythrocyte ghosts; goblin and ankyrin have highly homologous, although distinct, two-dimensional peptide maps; and, in reconstitution experiments, goblin binds to spectrin and band 3 in approximately the same molar ratio as ankyrin. Immunoautoradiography and immunofluorescence with goblin antiserum reveal that a serologically related polypeptide Mr, 235,000) is present in highly purified membrane fractions of mammalian myocardium and in whole extracts of adult chicken cardiac and skeletal musclenonerythroid tissues which express predominantly the erythroid (αβ-) spectrin phenotype. Erythroid spectrin and goblin (ankyrin) are codistributed in skeletal muscle at the sarcolemma as discrete foci adjacent to the Z lines and, in pectoral muscle, also at the periphery of the Z discs. These spatial relationships indicate that goblin and spectrin in muscle cells form a structural framework that serves as the attachment site for the myofiber at the level of the Z line on the sarcolemma.
Additional Information© 1984 by the National Academy of Sciences. Communicated by Norman H. Horowitz, February 1, 1984. We are grateful to Dr. Larry R. Jones (Indiana University School of Medicine, Indianapolis) for generously providing the purified membrane fractions of mammalian myocardium, to Dr. V. Bennett (The Johns Hopkins School of Medicine, Baltimore) for the ankyrin antiserum, to Dr. Bruce Granger for his advice on the immunoblot procedure and critical comments on the manuscript, and to Dr. R.T. Moon for preparation of rabbit erythrocyte inside-out vesicles. This work was supported by grants from the National Institutes of Health, the National Science Foundation, and the Muscular Dystrophy Association of America (to E.L.). W.J.N. was supported also by a Senior Investigator Fellowship from the American Heart Association (Los Angeles Affiliate) and a grant from the National Institutes of Health. E.L. is the recipient of a Research Career Development Award from the National Institutes of Health. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Published - NELpnas84.pdf