A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation Vereshchagina, N., Bennett, D., Szoor, B., Kirchner, J., Gross, S., Vissi, E., White-Cooper, H., Alphey, L. (2004). the essential role of PP1beta in Drosophila is to regulate nonmuscle myosin.  Mol. Biol. Cell 15(10): 4395--4405. (Export to RIS)
FlyBase ID FBrf0180501
Publication Type Research paper
PubMed ID 15269282
PubMed Abstract Reversible phosphorylation of myosin regulatory light chain (MRLC) is a key regulatory mechanism controlling myosin activity and thus regulating the actin/myosin cytoskeleton. We show that Drosophila PP1beta, a specific isoform of serine/threonine protein phosphatase 1 (PP1), regulates nonmuscle myosin and that this is the essential role of PP1beta. Loss of PP1beta leads to increased levels of phosphorylated nonmuscle MRLC (Sqh) and actin disorganisation; these phenotypes can be suppressed by reducing the amount of active myosin. Drosophila has two nonmuscle myosin targeting subunits, one of which (MYPT-75D) resembles MYPT3, binds specifically to PP1beta, and activates PP1beta's Sqh phosphatase activity. Expression of a mutant form of MYPT-75D that is unable to bind PP1 results in elevation of Sqh phosphorylation in vivo and leads to phenotypes that can also be suppressed by reducing the amount of active myosin. The similarity between fly and human PP1beta and MYPT genes suggests this role may be conserved.
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Language of Publication English
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Publication Type Journal
Abbreviation Mol. Biol. Cell
Title Molecular Biology of the Cell
Publication Year 1992-
ISBN/ISSN 1059-1524
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