The role of the calponin homology domain of smoothelin-like 1 (SMTNL1) in myosin phosphatase inhibition and smooth muscle contraction.

Journal Article (Journal Article)

In this study, we provide further insight into the contribution of the smoothelin-like 1 (SMTNL1) calponin homology (CH)-domain on myosin light chain phosphatase (SMPP-1M) activity and smooth muscle contraction. SMTNL1 protein was shown to have inhibitory effects on SMPP-1M activity but not on myosin light chain kinase (MLCK) activity. Treatment of beta-escin permeabilized rabbit, ileal smooth muscle with SMTNL1 had no effect on the time required to reach half-maximal force (t(1/2)) during stimulation with pCa6.3 solution. The addition of recombinant SMTNL1 protein to permeabilized, smooth muscle strips caused a significant decrease in contractile force. While the calponin homology (CH)-domain was essential for maximal SMTNL1-associated relaxation, it alone did not cause significant changes in force. SMTNL1 was poorly dephosphorylated by PP-1C in the presence of the myosin targeting subunit (MYPT1), suggesting that phosphorylated SMTNL1 does not possess "substrate trapping" properties. Moreover, while full-length SMTNL1 could suppress SMPP-1M activity toward LC(20) in vitro, truncated SMTNL1 lacking the CH-domain was ineffective. In summary, our findings suggest an important role for the CH-domain in mediating the effects of SMTNL1 on smooth muscle contraction.

Full Text

Duke Authors

Cited Authors

  • Borman, MA; Freed, TA; Haystead, TAJ; Macdonald, JA

Published Date

  • July 2009

Published In

Volume / Issue

  • 327 / 1-2

Start / End Page

  • 93 - 100

PubMed ID

  • 19219534

Pubmed Central ID

  • PMC2846773

Electronic International Standard Serial Number (EISSN)

  • 1573-4919

Digital Object Identifier (DOI)

  • 10.1007/s11010-009-0047-z


  • eng

Conference Location

  • Netherlands