The essential role of PP1beta in Drosophila is to regulate nonmuscle myosin

Natalia Vereshchagina; Daimark Bennett; Balázs Szöor; Jasmin Kirchner; Sascha Gross; Emese Vissi; Helen White-Cooper; Luke Alphey

doi:10.1091/mbc.e04-02-0139

The essential role of PP1beta in Drosophila is to regulate nonmuscle myosin

Natalia Vereshchagina, Daimark Bennett, Balázs Szöor, Jasmin Kirchner, Sascha Gross, Emese Vissi, Helen White-Cooper, Luke Alphey

Division of Developmental Biology & Medicine (L5)

Oxford University

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	4347-4760
Number of pages	14
Journal	Molecular Biology of the Cell
Volume	15
Issue number	10
DOIs	https://doi.org/10.1091/mbc.e04-02-0139
Publication status	Published - 21 Jul 2004

Keywords

Amino Acid Sequence
Animals
Cytoskeleton/metabolism
Drosophila Proteins/classification
Drosophila melanogaster/anatomy & histology
Humans
Isoenzymes/classification
Male
Molecular Sequence Data
Mutation
Myosin Light Chains/genetics
Myosin-Light-Chain Phosphatase/classification
Phenotype
Phosphoprotein Phosphatases/classification
Phosphorylation
Protein Binding
Protein Phosphatase 1
Protein Subunits/classification

Access to Document

10.1091/mbc.e04-02-0139

Cite this

@article{ae4b87e9900644a8a473c1abb93f0817,

title = "The essential role of PP1beta in Drosophila is to regulate nonmuscle myosin",

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.",

keywords = "Amino Acid Sequence, Animals, Cytoskeleton/metabolism, Drosophila Proteins/classification, Drosophila melanogaster/anatomy & histology, Humans, Isoenzymes/classification, Male, Molecular Sequence Data, Mutation, Myosin Light Chains/genetics, Myosin-Light-Chain Phosphatase/classification, Phenotype, Phosphoprotein Phosphatases/classification, Phosphorylation, Protein Binding, Protein Phosphatase 1, Protein Subunits/classification",

author = "Natalia Vereshchagina and Daimark Bennett and Bal{\'a}zs Sz{\"o}or and Jasmin Kirchner and Sascha Gross and Emese Vissi and Helen White-Cooper and Luke Alphey",

year = "2004",

month = jul,

day = "21",

doi = "10.1091/mbc.e04-02-0139",

language = "English",

volume = "15",

pages = "4347--4760",

journal = "Molecular Biology of the Cell",

issn = "1059-1524",

publisher = "American Society for Cell Biology",

number = "10",

}

TY - JOUR

T1 - The essential role of PP1beta in Drosophila is to regulate nonmuscle myosin

AU - Vereshchagina, Natalia

AU - Bennett, Daimark

AU - Szöor, Balázs

AU - Kirchner, Jasmin

AU - Gross, Sascha

AU - Vissi, Emese

AU - White-Cooper, Helen

AU - Alphey, Luke

PY - 2004/7/21

Y1 - 2004/7/21

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Cytoskeleton/metabolism

KW - Drosophila Proteins/classification

KW - Drosophila melanogaster/anatomy & histology

KW - Humans

KW - Isoenzymes/classification

KW - Male

KW - Molecular Sequence Data

KW - Mutation

KW - Myosin Light Chains/genetics

KW - Myosin-Light-Chain Phosphatase/classification

KW - Phenotype

KW - Phosphoprotein Phosphatases/classification

KW - Phosphorylation

KW - Protein Binding

KW - Protein Phosphatase 1

KW - Protein Subunits/classification

U2 - 10.1091/mbc.e04-02-0139

DO - 10.1091/mbc.e04-02-0139

M3 - Article

C2 - 15269282

SN - 1059-1524

VL - 15

SP - 4347

EP - 4760

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

IS - 10

ER -

The essential role of PP1beta in Drosophila is to regulate nonmuscle myosin

Abstract

Keywords

Access to Document

Fingerprint

Cite this