PMID- 10613909
OWN - NLM
STAT- MEDLINE
DCOM- 20000204
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 147
IP  - 7
DP  - 1999 Dec 27
TI  - Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and
      Cdc42-activated LIM-kinase 2.
PG  - 1519-32
AB  - The rapid turnover of actin filaments and the tertiary meshwork formation are
      regulated by a variety of actin-binding proteins. Protein phosphorylation of
      cofilin, an actin-binding protein that depolymerizes actin filaments, suppresses 
      its function. Thus, cofilin is a terminal effector of signaling cascades that
      evokes actin cytoskeletal rearrangement. When wild-type LIMK2 and kinase-dead
      LIMK2 (LIMK2/KD) were respectively expressed in cells, LIMK2, but not LIMK2/KD,
      phosphorylated cofilin and induced formation of stress fibers and focal
      complexes. LIMK2 activity toward cofilin phosphorylation was stimulated by
      coexpression of activated Rho and Cdc42, but not Rac. Importantly, expression of 
      activated Rho and Cdc42, respectively, induced stress fibers and filopodia,
      whereas both Rho- induced stress fibers and Cdc42-induced filopodia were
      abrogated by the coexpression of LIMK2/KD. In contrast, the coexpression of
      LIMK2/KD with the activated Rac did not affect Rac-induced lamellipodia
      formation. These results indicate that LIMK2 plays a crucial role both in Rho-
      and Cdc42-induced actin cytoskeletal reorganization, at least in part by
      inhibiting the functions of cofilin. Together with recent findings that LIMK1
      participates in Rac-induced lamellipodia formation, LIMK1 and LIMK2 function
      under control of distinct Rho subfamily GTPases and are essential regulators in
      the Rho subfamilies-induced actin cytoskeletal reorganization.
FAU - Sumi, T
AU  - Sumi T
AD  - Division of Biochemistry, Department of Oncology, Biomedical Research Center,
      Osaka University Medical School, Suita, Japan.
FAU - Matsumoto, K
AU  - Matsumoto K
FAU - Takai, Y
AU  - Takai Y
FAU - Nakamura, T
AU  - Nakamura T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Actin Depolymerizing Factors)
RN  - 0 (Actins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Microfilament Proteins)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.1 (LIMK1 protein, human)
RN  - EC 2.7.11.1 (LIMK2 protein, human)
RN  - EC 2.7.11.1 (Lim Kinases)
RN  - EC 2.7.11.1 (Limk1 protein, mouse)
RN  - EC 2.7.11.1 (Limk2 protein, mouse)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (rho-Associated Kinases)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.5.2 (cdc42 GTP-Binding Protein)
RN  - EC 3.6.5.2 (rho GTP-Binding Proteins)
SB  - IM
MH  - Actin Depolymerizing Factors
MH  - Actins/*metabolism
MH  - Animals
MH  - COS Cells
MH  - Cytoskeleton/enzymology/*metabolism
MH  - DNA-Binding Proteins/physiology
MH  - GTP Phosphohydrolases/physiology
MH  - HeLa Cells
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Lim Kinases
MH  - Mice
MH  - Microfilament Proteins/biosynthesis/genetics/*metabolism
MH  - Mutation
MH  - Phosphorylation
MH  - Protein Kinases/chemistry/metabolism/*physiology
MH  - Protein-Serine-Threonine Kinases/physiology
MH  - cdc42 GTP-Binding Protein/*physiology
MH  - rho GTP-Binding Proteins/*physiology
MH  - rho-Associated Kinases
PMC - PMC2174243
EDAT- 1999/12/30 00:00
MHDA- 1999/12/30 00:01
CRDT- 1999/12/30 00:00
PHST- 1999/12/30 00:00 [pubmed]
PHST- 1999/12/30 00:01 [medline]
PHST- 1999/12/30 00:00 [entrez]
AID - 10.1083/jcb.147.7.1519 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Dec 27;147(7):1519-32. doi: 10.1083/jcb.147.7.1519.