3.8 Article

Nebulette interacts with filamin C

Journal

CELL MOTILITY AND THE CYTOSKELETON
Volume 65, Issue 2, Pages 130-142

Publisher

WILEY-LISS
DOI: 10.1002/cm.20249

Keywords

myofibrillogenesis; nebulin; titin; Ig repeat; actin-binding proteins

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The actin-binding proteins, nebulette, and nebulin, are comprised of a four-domain layout containing an acidic N-terminal region, a repeat domain, a serine-rich-linker region, and a Src homology-3 domain. Both proteins contain homologous N-terminal regions that are predicted to be in different environments within the sarcomere. The nebulin acidic N-terminal region is found at the distal ends of the thin filaments. Nebulette, however, is predicted to extend 150 nm from the center of the Z-line. To dissect out the functions of the N-terminal domain of nebulette, we have performed a yeast two-hybrid screen using nebulette residues 1-86 as bait. We have identified filamin-C, ZASP-1, and tropomyosin-1 as binding partners. Characterization of the nebulette-filamin interaction indicates that filamin-C predominantly interacts with the modules. These data suggest that filamin-C, a known component of striated muscle Z-lines, interacts with nebulette modules.

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