Regulation of cysteine-rich protein 2 localization by the development of actin fibers during smooth muscle cell differentiation

Biochem Biophys Res Commun. 2011 Jul 22;411(1):96-101. doi: 10.1016/j.bbrc.2011.06.100. Epub 2011 Jun 28.


Cysteine-rich protein 2 (CRP2) is a cofactor for smooth muscle cell (SMC) differentiation. Here, we examined the mechanism of CRP2 distribution dynamics during SMC differentiation. CRP2 protein directly associated with F-actin through its N-terminal LIM domain and Gly-rich region, as determined by ELISA. In undifferentiated cells that contain few actin stress fibers, CRP2 was broadly distributed throughout the whole cell, including the nucleus. After induction of SMC differentiation, CRP2 localized to actin stress fibers as they formed. The stress fiber-localized CRP2 entered the nucleus because of induced actin depolymerization. These CRP2 dynamics were reproduced by in silico simulation. CRP2 localization dynamics, which affect CRP2 function, are regulated by the formation of actin stress fibers in conjunction with SMC differentiation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Animals
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Differentiation*
  • Cell Line
  • LIM Domain Proteins
  • Mice
  • Myocytes, Smooth Muscle / cytology*
  • Myocytes, Smooth Muscle / metabolism
  • Photobleaching
  • Stress Fibers / metabolism*


  • Actins
  • Carrier Proteins
  • Crip2 protein, mouse
  • LIM Domain Proteins