QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 15, Issue 10, 4395-4405, October 2004

This Article Full Text Full Text (PDF) Supplemental Figure All Versions of this Article: E04-02-0139v1 15/10/4395    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Vereshchagina, N. Articles by Alphey, L. Search for Related Content PubMed PubMed Citation Articles by Vereshchagina, N. Articles by Alphey, L.

The Essential Role of PP1 in Drosophila Is to Regulate Nonmuscle Myosin

Natalia Vereshchagina ^*, Daimark Bennett ^*, Balázs Ször, Jasmin Kirchner, Sascha Gross, Emese Vissi, Helen White-Cooper, and Luke Alphey 

Department of Zoology, University of Oxford, Oxford OX1 3PS, United Kingdom

Submitted February 19, 2004; Revised July 2, 2004; Accepted July 12, 2004
Monitoring Editor: Lawrence Goldstein

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 PP1, a specific isoform of serine/threonine protein phosphatase 1 (PP1), regulates nonmuscle myosin and that this is the essential role of PP1. Loss of PP1 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 PP1, and activates PP1'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 PP1 and MYPT genes suggests this role may be conserved.

The online version of this article contains supplemental material accessible through http://www.molbiolcell.org.

^* These authors contributed equally to this work.

Corresponding author. E-mail address: Luke.Alphey{at}zoo.ox.ac.uk.

This article has been cited by other articles:

				C. Gally, F. Wissler, H. Zahreddine, S. Quintin, F. Landmann, and M. Labouesse Myosin II regulation during C. elegans embryonic elongation: LET-502/ROCK, MRCK-1 and PAK-1, three kinases with different roles Development, September 15, 2009; 136(18): 3109 - 3119. [Abstract] [Full Text] [PDF]

				S. Tan, E. Lyulcheva, J. Dean, and D. Bennett Mars promotes dTACC dephosphorylation on mitotic spindles to ensure spindle stability J. Cell Biol., October 23, 2008; 182(1): 27 - 33. [Abstract] [Full Text] [PDF]

				T. Sueyoshi, R. Moore, J. Sugatani, Y. Matsumura, and M. Negishi PPP1R16A, The Membrane Subunit of Protein Phosphatase 1{beta}, Signals Nuclear Translocation of the Nuclear Receptor Constitutive Active/Androstane Receptor Mol. Pharmacol., April 1, 2008; 73(4): 1113 - 1121. [Abstract] [Full Text] [PDF]

				J. Kirchner, S. Gross, D. Bennett, and L. Alphey Essential, Overlapping and Redundant Roles of the Drosophila Protein Phosphatase 1{alpha} and 1{beta} Genes Genetics, May 1, 2007; 176(1): 273 - 281. [Abstract] [Full Text] [PDF]

				J. Kirchner, S. Gross, D. Bennett, and L. Alphey The Nonmuscle Myosin Phosphatase PP1{beta} (flapwing) Negatively Regulates Jun N-Terminal Kinase in Wing Imaginal Discs of Drosophila Genetics, April 1, 2007; 175(4): 1741 - 1749. [Abstract] [Full Text] [PDF]

				J. Yong, I. Tan, L. Lim, and T. Leung Phosphorylation of Myosin Phosphatase Targeting Subunit 3 (MYPT3) and Regulation of Protein Phosphatase 1 by Protein Kinase A J. Biol. Chem., October 20, 2006; 281(42): 31202 - 31211. [Abstract] [Full Text] [PDF]