Role of myosin-II phosphorylation in V12Cdc42-mediated disruption of Drosophila cellularization

Janice M. Crawford; Zuowei Su; Olga Varlamova; Anne R. Bresnick; Daniel P. Kiehart

doi:10.1078/0171-9335-00156

Role of myosin-II phosphorylation in V12Cdc42-mediated disruption of Drosophila cellularization

Janice M. Crawford, Zuowei Su, Olga Varlamova, Anne R. Bresnick, Daniel P. Kiehart

Biochemistry

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

6 Scopus citations

Abstract

Microinjection of constitutively active Cdc42 (V12Cdc42) disrupts the actomyosin cytoskeleton during cellularization (Crawford et al., Dev. Biol., 204, 151-164 (1998)). The p21-activated kinase (PAK) family of Ser/Thr kinases are effectors of GTP-bound forms of the small GTPases, Cdc42 and Rac. Drosophila PAK, which colocalizes with actin and myosin-II during cellularization, concentrates at sites of V12Cdc42-induced actomyosin disruption. In vitro biochemical analyses demonstrate that PAK phosphorylates the regulatory light chain (RLC) of Drosophila nonmuscle myosin-II on Ser21, a site known to activate myosin-II function. Although activated PAK does not disrupt the actomyosin cytoskeleton, it induces increased levels of Ser21 phosphorylated RLC. These findings suggest that increased levels of RLC phosphorylation do not contribute to disruption of the actomyosin hexagonal array.

Original language	English (US)
Pages (from-to)	240-244
Number of pages	5
Journal	European Journal of Cell Biology
Volume	80
Issue number	3
DOIs	https://doi.org/10.1078/0171-9335-00156
State	Published - 2001

Keywords

Actomyosin array
Cellularization
Drosophila
Myosin light chain kinase
P21-activated kinase
Regulatory light chain

ASJC Scopus subject areas

Pathology and Forensic Medicine
Histology
Cell Biology

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title = "Role of myosin-II phosphorylation in V12Cdc42-mediated disruption of Drosophila cellularization",

abstract = "Microinjection of constitutively active Cdc42 (V12Cdc42) disrupts the actomyosin cytoskeleton during cellularization (Crawford et al., Dev. Biol., 204, 151-164 (1998)). The p21-activated kinase (PAK) family of Ser/Thr kinases are effectors of GTP-bound forms of the small GTPases, Cdc42 and Rac. Drosophila PAK, which colocalizes with actin and myosin-II during cellularization, concentrates at sites of V12Cdc42-induced actomyosin disruption. In vitro biochemical analyses demonstrate that PAK phosphorylates the regulatory light chain (RLC) of Drosophila nonmuscle myosin-II on Ser21, a site known to activate myosin-II function. Although activated PAK does not disrupt the actomyosin cytoskeleton, it induces increased levels of Ser21 phosphorylated RLC. These findings suggest that increased levels of RLC phosphorylation do not contribute to disruption of the actomyosin hexagonal array.",

keywords = "Actomyosin array, Cellularization, Drosophila, Myosin light chain kinase, P21-activated kinase, Regulatory light chain",

author = "Crawford, {Janice M.} and Zuowei Su and Olga Varlamova and Bresnick, {Anne R.} and Kiehart, {Daniel P.}",

note = "Funding Information: Acknowledgements. We thank Dr. Louis Lim, Dr. Edward Manser and Dr. Nicholas Harden for V12Cd42, PAK-GST fusions and Drosophila PAK antiserum; Dr. Fumio Matsumura for anti-phosphoserine RLC antibody, Dr. James Lessard for anti-actin antibody, Dr. Vann Bennett for the use of his HPLC, members of the Kiehart and Bresnick labs for helpful discussions and Ruth Montague for help in preparing the final manuscript. This work was supported by NIH GM33830 and an Office of Naval Research grant to D. P. Kiehart; NIH Predoctoral fellowship GM07184 to J. M. Crawford and the American Heart Association to A. R. Bresnick.",

year = "2001",

doi = "10.1078/0171-9335-00156",

language = "English (US)",

volume = "80",

pages = "240--244",

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T1 - Role of myosin-II phosphorylation in V12Cdc42-mediated disruption of Drosophila cellularization

AU - Crawford, Janice M.

AU - Su, Zuowei

AU - Varlamova, Olga

AU - Bresnick, Anne R.

AU - Kiehart, Daniel P.

N1 - Funding Information: Acknowledgements. We thank Dr. Louis Lim, Dr. Edward Manser and Dr. Nicholas Harden for V12Cd42, PAK-GST fusions and Drosophila PAK antiserum; Dr. Fumio Matsumura for anti-phosphoserine RLC antibody, Dr. James Lessard for anti-actin antibody, Dr. Vann Bennett for the use of his HPLC, members of the Kiehart and Bresnick labs for helpful discussions and Ruth Montague for help in preparing the final manuscript. This work was supported by NIH GM33830 and an Office of Naval Research grant to D. P. Kiehart; NIH Predoctoral fellowship GM07184 to J. M. Crawford and the American Heart Association to A. R. Bresnick.

PY - 2001

Y1 - 2001

N2 - Microinjection of constitutively active Cdc42 (V12Cdc42) disrupts the actomyosin cytoskeleton during cellularization (Crawford et al., Dev. Biol., 204, 151-164 (1998)). The p21-activated kinase (PAK) family of Ser/Thr kinases are effectors of GTP-bound forms of the small GTPases, Cdc42 and Rac. Drosophila PAK, which colocalizes with actin and myosin-II during cellularization, concentrates at sites of V12Cdc42-induced actomyosin disruption. In vitro biochemical analyses demonstrate that PAK phosphorylates the regulatory light chain (RLC) of Drosophila nonmuscle myosin-II on Ser21, a site known to activate myosin-II function. Although activated PAK does not disrupt the actomyosin cytoskeleton, it induces increased levels of Ser21 phosphorylated RLC. These findings suggest that increased levels of RLC phosphorylation do not contribute to disruption of the actomyosin hexagonal array.

AB - Microinjection of constitutively active Cdc42 (V12Cdc42) disrupts the actomyosin cytoskeleton during cellularization (Crawford et al., Dev. Biol., 204, 151-164 (1998)). The p21-activated kinase (PAK) family of Ser/Thr kinases are effectors of GTP-bound forms of the small GTPases, Cdc42 and Rac. Drosophila PAK, which colocalizes with actin and myosin-II during cellularization, concentrates at sites of V12Cdc42-induced actomyosin disruption. In vitro biochemical analyses demonstrate that PAK phosphorylates the regulatory light chain (RLC) of Drosophila nonmuscle myosin-II on Ser21, a site known to activate myosin-II function. Although activated PAK does not disrupt the actomyosin cytoskeleton, it induces increased levels of Ser21 phosphorylated RLC. These findings suggest that increased levels of RLC phosphorylation do not contribute to disruption of the actomyosin hexagonal array.

KW - Actomyosin array

KW - Cellularization

KW - Drosophila

KW - Myosin light chain kinase

KW - P21-activated kinase

KW - Regulatory light chain

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JO - European Journal of Cell Biology

JF - European Journal of Cell Biology

SN - 0171-9335

IS - 3

ER -

Role of myosin-II phosphorylation in V12Cdc42-mediated disruption of Drosophila cellularization

Abstract

Keywords

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