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 |
| State | Published - 2001 |
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Keywords
- Actomyosin array
- Cellularization
- Drosophila
- Myosin light chain kinase
- P21-activated kinase
- Regulatory light chain
ASJC Scopus subject areas
- Anatomy
- Cell Biology
Cite this
Role of myosin-II phosphorylation in V12Cdc42-mediated disruption of Drosophila cellularization. / Crawford, Janice M.; Su, Zuowei; Varlamova, Olga; Bresnick, Anne R.; Kiehart, Daniel P.
In: European Journal of Cell Biology, Vol. 80, No. 3, 2001, p. 240-244.Research output: Contribution to journal › Article
}
TY - JOUR
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.
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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UR - http://www.scopus.com/inward/citedby.url?scp=0035084536&partnerID=8YFLogxK
M3 - Article
VL - 80
SP - 240
EP - 244
JO - European Journal of Cell Biology
JF - European Journal of Cell Biology
SN - 0171-9335
IS - 3
ER -