例如:"lncRNA", "apoptosis", "WRKY"

Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate with STARS and directly bind F-actin.

J Biol Chem. 2007 Mar 16;282(11):8393-403. Epub 2006 Dec 28
Tomasa Barrientos 1 , Derk Frank , Koichiro Kuwahara , Svetlana Bezprozvannaya , G C Teg Pipes , Rhonda Bassel-Duby , James A Richardson , Hugo A Katus , Eric N Olson , Norbert Frey
Tomasa Barrientos 1 , Derk Frank , Koichiro Kuwahara , Svetlana Bezprozvannaya , G C Teg Pipes , Rhonda Bassel-Duby , James A Richardson , Hugo A Katus , Eric N Olson , Norbert Frey
+ et al

[No authors listed]

Author information
  • 1 Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148, USA.

摘要


In addition to regulating cell motility, contractility, and cytokinesis, the actin cytoskeleton plays a critical role in the regulation of transcription and gene expression. We have previously identified a novel muscle-specific actin-binding protein, STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. To further dissect the STARS/SRF pathway, we performed a yeast two-hybrid screen of a skeletal muscle cDNA library using STARS as bait, and we identified two novel members of the ABLIM protein family, ABLIM-2 and -3, as STARS-interacting proteins. ABLIM-1, which is expressed in retina, brain, and muscle tissue, has been postulated to function as a tumor suppressor. ABLIM-2 and -3 display distinct tissue-specific expression patterns with the highest expression levels in muscle and neuronal tissue. Moreover, these novel ABLIM proteins strongly bind F-actin, are localized to actin stress fibers, and synergistically enhance STARS-dependent activation of SRF. Conversely, knockdown of endogenous ABLIM expression utilizing small interfering RNA significantly blunted SRF-dependent transcription in C2C12 skeletal muscle cells. These findings suggest that the members of the novel ABLIM protein family may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription.