Signaling from Rho to the Actin Cytoskeleton Through Protein Kinases ROCK and LIM-kinase

American Association for the Advancement of Science (AAAS) - Tập 285 Số 5429 - Trang 895-898 - 1999
Masao Maekawa1, Toshimasa Ishizaki1, Shuken Boku1, Naoki Watanabe1, Akiko Fujita1, Akihiro Iwamatsu2, Takashi Obinata3, Kazumasa Ohashi4, Kensaku Mizuno4, Shuh Narumiya1
1Department of Pharmacology, Kyoto University Faculty of Medicine, Kyoto 606-8315, Japan.
2Central Laboratories for Key Technology, Kirin Brewery, Yokohama 236-0004, Japan.
3Department of Biology, Faculty of Science, Chiba University, Chiba 263-8522, Japan
4Biological Institute, Graduate School of Science, Tohoku University, Sendai 980-8578, Japan

Tóm tắt

The actin cytoskeleton undergoes extensive remodeling during cell morphogenesis and motility. The small guanosine triphosphatase Rho regulates such remodeling, but the underlying mechanisms of this regulation remain unclear. Cofilin exhibits actin-depolymerizing activity that is inhibited as a result of its phosphorylation by LIM-kinase. Cofilin was phosphorylated in N1E-115 neuroblastoma cells during lysophosphatidic acid–induced, Rho-mediated neurite retraction. This phosphorylation was sensitive to Y-27632, a specific inhibitor of the Rho-associated kinase ROCK. ROCK, which is a downstream effector of Rho, did not phosphorylate cofilin directly but phosphorylated LIM-kinase, which in turn was activated to phosphorylate cofilin. Overexpression of LIM-kinase in HeLa cells induced the formation of actin stress fibers in a Y-27632–sensitive manner. These results indicate that phosphorylation of LIM-kinase by ROCK and consequently increased phosphorylation of cofilin by LIM-kinase contribute to Rho-induced reorganization of the actin cytoskeleton.

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Tài liệu tham khảo

10.1016/S0955-0674(97)80152-4

10.1093/oxfordjournals.jbchem.a021401

10.1126/science.279.5350.509

10.1126/science.273.5272.245

10.1016/S0962-8924(97)01127-6

10.1038/40187

10.1074/jbc.273.10.5542

10.1083/jcb.140.3.647

K. Jalink et al. J. Cell. Biol . 126 801 (1994).

Hirose M. et al. 141 1625 (1998).

After LPA stimulation N1E-115 cells were lysed with 10 mM tris-HCl (pH 7.5) containing 1 mM EGTA 5 mM MgCl 2 1 mM dithiothreitol 1% (v/v) Triton X-100 and mixtures of phosphatase inhibitors and protease inhibitors. Lysates were centrifuged and the supernatant corresponding to 2 × 10 4 cells was subjected to two-dimensional electrophoresis with a linear pH gradient from 3.5 to 10 followed by autoradiography.

Purification and identification details of P1 and P2 proteins are available at www.sciencemag.org/feature/data/1041678.shl.

10.1091/mbc.6.11.1423

10.1016/S0021-9258(17)36603-6

In the transfection experiments in this study COS-7 cells were transfected with combinations of the following vectors: pFL-C1-FLAG–tagged wild-type (WT) or S3A cofilin pCAG-Myc–tagged ROCKΔ1 (14) pUCD2-SRα-FLAG–tagged LIMK1 (17) pUC-SRα-Myc–tagged LIMK 2 [

10.1074/jbc.270.52.31321

] pCMV5-FLAG–tagged N 17 -Rac (8) pEXV-Myc–tagged V 14 -Rho (14) and pCAG-Myc–tagged ROCK-KDIA (14). After transfection cells were cultured for 15 hours in Dulbecco's minimum essential medium containing 10% fetal bovine serum (Fig. 1C) or in serum-free OPTI-MEM (Gibco) (Figs. 2B and 3A). In the experiments in Figs. 1C and 3A the cells were then labeled for 4 hours with [ 32 P]orthophosphate (50 μCi/ml). Cells were lysed in 20 mM tris-HCl (pH 7.5) containing 1 mM EDTA 1 mM EGTA 5 mM MgCl 2 5 mM 2-mercaptoethanol 0.05% Triton X-100 and mixtures of phosphatase inhibitors and protease inhibitors. FLAG-tagged cofilin was immunoprecipitated with anti-FLAG (M2) affinity beads (Sigma) and subjected to SDS–polyacrylamide gel electrophoresis (SDS-PAGE) followed by autoradiography or immunoblot analysis (Figs. 1C and 3A). FLAG-tagged LIMK1 was immunoprecipitated and subjected to kinase assay (16) (Fig. 2B).

10.1016/S0014-5793(97)00107-5

10.1083/jcb.122.3.623

10.1074/jbc.270.29.17582

10.1046/j.1365-2443.1996.05005.x

His 6 -tagged cofilin was expressed in Escherichia coli and His 6 -tagged ROCKΔ4 (residues 1 to 477) was produced in Sf9 cells. Kinase reactions were done in a total volume of 23 μl at 30°C for 10 min with 50 μM [γ- 32 P]ATP (adenosine 5′-triphosphate) and 4 μg of either cofilin or histone type 2 as substrates in kinase buffer [25 mM Hepes - NaOH (pH 7.5) 10 mM MgCl 2 5 mM MnCl 2 0.1 mM EGTA 0.05% Brij 35 5 mM 2-mercaptoethanol phosphatase inhibitors and protease inhibitors].

10.1038/31729

; N. Yang et al. ibid. p. 809.

M. Maekawa et al. unpublished data.

10.1038/40418

; M.-F. Carlier et al. J. Cell Biol. 136 1307 (1997).

N. Watanabe et al. EMBO J. 16 1307 (1997).

10.1016/0092-8674(93)90544-Z

10.1126/science.283.5410.2083

Supported by grants from the Ministry of Education Science and Culture of Japan and from the Human Frontier Science Program. We thank E. Nishida I. Yahara and T. Doi for advice and A. Shinohara for mass spectrometry. M.M. thanks S. Maekawa for encouragement.