例如:"lncRNA", "apoptosis", "WRKY"

Myosin light chain kinase A is activated by cGMP-dependent and cGMP-independent pathways.

FEBS Lett.2006 Apr 3;580(8):2059-64. Epub 2006 Mar 10
Jonathan M Goldberg 1 , Eric S Wolpin , Leonard Bosgraaf , Bryan K Clarkson , Peter J M Van Haastert , Janet L Smith
Jonathan M Goldberg 1 , Eric S Wolpin , Leonard Bosgraaf , Bryan K Clarkson , Peter J M Van Haastert , Janet L Smith
+ et al

[No authors listed]

Author information
  • 1 Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472-2829, USA.

摘要


Stimulation of Dictyostelium cells with the chemoattractant cAMP results in transient phosphorylation of the myosin regulatory light chain (RLC). We show that myosin light chain kinase A (MLCK-A) is responsible for RLC phosphorylation during chemotaxis, and that MLCK-A itself is transiently phosphorylated on threonine-166, dramatically increasing its catalytic activity. MLCK-A activation during chemotaxis is highly responsive to cellular cGMP levels and the cGMP-binding protein GbpC. MLCK-A- cells have a partial cytokinesis defect, and do not phosphorylate RLC in response to concanavalin A (conA), but cells lacking cGMP or GbpC divide normally and phosphorylate in response to conA. Thus MLCK-A is activated by a cGMP/GbpC-independent mechanism activated during cytokinesis or by conA, and a cGMP/GbpC-dependent pathway during chemotaxis.