Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow

@article{Kosako2000RhokinaseROCKII,
  title={Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow},
  author={Hidetaka Kosako and Toshimichi Yoshida and Fumio Matsumura and Toshimasa Ishizaki and Shuh Narumiya and Masaki Inagaki},
  journal={Oncogene},
  year={2000},
  volume={19},
  pages={6059-6064}
}
The small GTPase Rho and one of its targets, Rho-kinase (also termed ROK or ROCK), are implicated in various cellular functions including stress fiber formation, smooth muscle contraction, tumor cell invasion and cell motility. We have previously reported that Rho-kinase accumulates at the cleavage furrow during cytokinesis in several cultured cells. Here, using Rho-kinase inhibitors, Y-27632 and HA1077, we found that Rho-kinase is responsible for the phosphorylation of myosin regulatory light… 
Aurora‐B and Rho‐kinase/ROCK, the two cleavage furrow kinases, independently regulate the progression of cytokinesis: possible existence of a novel cleavage furrow kinase phosphorylates ezrin/radixin/moesin (ERM)
TLDR
The results suggest that Aurora‐B and Rho‐kinase/ROCK regulate the progression of cytokinesis without communicating to each other, and there may exist a novel protein kinase which phosphorylates ERM at the cleavage furrow.
Rho-binding kinase (LET-502) and myosin phosphatase (MEL-11) regulate cytokinesis in the early Caenorhabditis elegans embryo.
TLDR
It is demonstrated that these genes function together to regulate the rate of cleavage furrow contraction, with Rho-binding kinase/LET-502 mediating contraction, whereas myosin phosphatase/MEL-11 acts as a brake to contraction: early embryonic cleavage often fails or is slowed when let-502 is mutated, whereas mel-11 mutations result in ectopic furrowing and faster furrow ingression.
Rho-kinase contributes to diphosphorylation of myosin II regulatory light chain in nonmuscle cells
TLDR
It is suggested that Rho-kinase contributes to MRLC diphosphorylation and reorganization of actin filaments in nonmuscle cells.
Citron kinase, a Rho-dependent kinase, induces di-phosphorylation of regulatory light chain of myosin II.
TLDR
It is found that citron kinase phosphorylated regulatory light chain (MLC) of myosin II at both Ser-19 and Thr-18 in vitro and the kinase domain was able to increase di-phosphorylation and restore stress fiber assembly even when ROCK was inhibited with a specific inhibitor, Y-27632.
PAK and other Rho-associated kinases--effectors with surprisingly diverse mechanisms of regulation.
TLDR
This work focuses on the current understanding of the way in which different Rho-associated serine/threonine kinases, denoted PAK (p21-activated kinase), MLK (mixed-lineage kinase) and ROK (Rho-kinase), interact with and are regulated by their partner GTPases.
Aurora B but Not Rho/MLCK Signaling Is Required for Localization of Diphosphorylated Myosin II Regulatory Light Chain to the Midzone in Cytokinesis
TLDR
It is shown that depletion of the Rho signaling proteins MKLP1, MgcRacGAP, or ECT2 inhibited the localization of 1P-MRLC to the contractile ring but not the localization in dividing HeLa cells, suggesting that Aurora B, but not Rho/MLCK signaling, is essential for the localization to the midzone.
Chloride Conductance Is Required for the Protein Kinase A and Rac1-dependent Phosphorylation of Moesin at Thr-558 by KCl in PC12 Cells*
TLDR
The results suggest that the phosphorylation of moesin at Thr-558 in PC12 cells by KCl treatment is PKA- and Rac1-dependent and that KCl-induced chloride conductance is involved in the activation of this signaling system.
In vivo phosphorylation of regulatory light chain of myosin II in sea urchin eggs and its role in controlling myosin localization and function during cytokinesis.
TLDR
RLC mono-phosphorylation by more than two RLC kinases play a main role in regulation and localization of myosin in the dividing sea urchin eggs, and it was revealed that localization ofMyosin heavy chain in the cleavage furrow, but not in the cortex, was perturbed by inhibition of RLC Mono-ph phosphorylation.
Rho-associated coiled-coil kinase (ROCK) signaling and disease
TLDR
This review focuses on the role of the ROCK-signaling pathways in disease including cancer, which regulate many key cellular functions associated with malignancy, including cell proliferation, motility and viability.
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TLDR
The results raise the possibility that Rho-kinase might be involved in the formation of the contractile ring by modulating these F-actin-binding proteins during cytokinesis and in the phosphorylation and regulation of IF proteins at the cleavage furrow.
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TLDR
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