Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein

Jeffrey A. Spencer, Susan Eliazer, Robert L. Ilaria, James A. Richardson, Eric N. Olson

Research output: Contribution to journalArticlepeer-review

149 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)771-784
Number of pages14
JournalJournal of Cell Biology
Issue number4
StatePublished - Aug 21 2000


  • Cytoskeleton
  • Microtubule
  • RING-finger
  • Striated muscle

ASJC Scopus subject areas

  • Cell Biology


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