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Published online 21 August 2000. doi:10.1083/jcb.150.4.771
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© The Rockefeller University Press, 0021-9525/2000//771 $5.00
The Journal of Cell Biology, Volume 150, Number 4, , 2000 771-784

Original Article

Regulation of Microtubule Dynamics and Myogenic Differentiation by Murf, a Striated Muscle Ring-Finger Protein



Jeffrey A. Spencera, Susan Eliazerb, Robert L. Ilaria, Jr.b, James A. Richardsonc, and Eric N. Olsona

a Department of Molecular Biology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75235-9148
b Department of Hematology and Oncology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75235-9148
c Department of Pathology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75235-9148
Department of Molecular Biology, University of Texas Southwestern Medical Center at Dallas, 6000 Harry Hines Blvd., Dallas, TX 75235-9148.(214) 648-1196(214) 648-1187

eolson{at}hamon.swmed.edu

The RING-finger domain is a novel zinc-binding Cys-His protein motif found in a growing number of proteins involved in signal transduction, ubiquitination, gene transcription, differentiation, and morphogenesis. We describe a novel muscle-specific RING-finger protein (MURF) expressed specifically in cardiac and skeletal muscle cells throughout pre- and postnatal mouse development. MURF belongs to the RING-B-box-coiled-coil subclass of RING-finger proteins, characterized by an NH2-terminal RING-finger followed by a zinc-finger domain (B-box) and a leucine-rich coiled-coil domain. Expression of MURF is required for skeletal myoblast differentiation and myotube fusion. The leucine-rich coiled-coil domain of MURF mediates association with microtubules, whereas the RING-finger domain is required for microtubule stabilization and an additional region is required for homo-oligomerization. Expression of MURF establishes a cellular microtubule network that is resistant to microtubule depolymerization induced by alkaloids, cold and calcium. These results identify MURF as a myogenic regulator of the microtubule network of striated muscle cells and reveal a link between microtubule organization and myogenesis.

Key Words: microtubule • RING-finger • cytoskeleton • striated muscle

© 2000 The Rockefeller University Press

Abbreviations used in this paper: MAP, microtubule-associated protein; MEF2, myocyte enhancer factor 2; MHC, myosin heavy chain; MOI, multiplicity of infection; MURF, muscle-specific RING-finger protein; RBCC, RING-B-box-coiled-coil; SRF, serum response factor.


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