LIMCH1 regulates nonmuscle myosin-II activity and suppresses cell migration

Yu Hung Lin, Yen Yi Zhen, Kun Yi Chien, I. Ching Lee, Wei Chi Lin, Mei Yu Chen, Li Mei Pai

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


Nonmuscle myosin II (NM-II) is an important motor protein involved in cell migration. Incorporation of NM-II into actin stress fiber provides a traction force to promote actin retrograde flow and focal adhesion assembly. However, the components involved in regulation of NM-II activity are not well understood. Here we identified a novel actin stress fiber- associated protein, LIM and calponin-homology domains 1 (LIMCH1), which regulates NM-II activity. The recruitment of LIMCH1 into contractile stress fibers revealed its localization complementary to actinin-1. LIMCH1 interacted with NM-IIA, but not NM-IIB, independent of the inhibition of myosin ATPase activity with blebbistatin. Moreover, the N-terminus of LIMCH1 binds to the head region of NM-IIA. Depletion of LIMCH1 attenuated myosin regulatory light chain (MRLC) diphosphorylation in HeLa cells, which was restored by reexpression of small interfering RNA-resistant LIMCH1. In addition, LIMCH1-depleted HeLa cells exhibited a decrease in the number of actin stress fibers and focal adhesions, leading to enhanced cell migration. Collectively, our data suggest that LIMCH1 plays a positive role in regulation of NM-II activity through effects on MRLC during cell migration.

Original languageEnglish
Pages (from-to)1054-1065
Number of pages12
JournalMolecular Biology of the Cell
Issue number8
Publication statusPublished - 2017 Apr 15

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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