Filamin 2 (FLN2): A muscle-specific sarcoglycan interacting protein

Terri G. Thompson, Yiu Mo Chan, Andrew A. Hack, Melissa Brosius, Michael Rajala, Hart G W Lidov, Elizabeth M. McNally, Simon Watkins, Louis M. Kunkel*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

221 Scopus citations

Abstract

Mutations in genes encoding for the sarcoglycans, a subset of proteins within the dystrophin-glycoprotein complex, produce a limb-girdle muscular dystrophy phenotype; however, the precise role of this group of proteins in the skeletal muscle is not known. To understand the role of the sarcoglycan complex, we looked for sarcoglycan interacting proteins with the hope of finding novel members of the dystrophin-glycoprotein complex. Using the yeast two-hybrid method, we have identified a skeletal muscle-specific form of filamin, which we term filamin 2 (FLN2), as a γ- and δ-sarcoglycan interacting protein. In addition, we demonstrate that FLN2 protein localization in limb-girdle muscular dystrophy and Duchenne muscular dystrophy patients and mice is altered when compared with unaffected individuals. Previous studies of filamin family members have determined that these proteins are involved in actin reorganization and signal transduction cascades associated with cell migration, adhesion, differentiation, force transduction, and survival. Specifically, filamin proteins have been found essential in maintaining membrane integrity during force application. The finding that FLN2 interacts with the sarcoglycans introduces new implications for the pathogenesis of muscular dystrophy.

Original languageEnglish (US)
Pages (from-to)115-126
Number of pages12
JournalJournal of Cell Biology
Volume148
Issue number1
DOIs
StatePublished - Jan 10 2000

Keywords

  • Cell signaling
  • Cytoskeleton
  • Dystrophin
  • Filamin C (FLNC)
  • Muscular dystrophy

ASJC Scopus subject areas

  • Cell Biology

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