Identification of Calponin as a Novel Substrate of Rho-Kinase

Kaneko, Takako; Amano, Mutsuki; Maeda, Akio; Goto, Hideyuki; Takahashi, Katsuhito; M, Ito; Kaibuchi, Kozo

doi:10.1006/bbrc.2000.2901

Cited by 110 publications

(71 citation statements)

References 46 publications

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“…Most of the ROCK substrates are cellular proteins associated with the regulation of actin cytoskeleton. Besides MLC and MYPT1, this important subset of ROCK substrates include CPI-17 [63], calponin [58], LIM kinases [80,99,132], ezrin/radixin/moesin (ERM) [83], adducin [37], sodium-hydrogen exchanger (NHE1) [137] and ZIP kinase [43].…”

Section: Substrates Of Rockmentioning

confidence: 99%

Rho kinase in the regulation of cell death and survival

Shi

Wei

2007

Arch. Immunol. Ther. Exp.

219

183

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SummaryRho kinase (ROCK) belongs to a family of serine/threonine kinases that are activated via interaction with Rho GTPases. ROCK is involved in a wide range of fundamental cellular functions such as contraction, adhesion, migration, and proliferation. Recent studies have shown that ROCK plays an important role in the regulation of apoptosis in various cell types and animal disease models. Two ROCK isoforms, ROCK1 and ROCK2, are assumed to be function redundant, based largely on kinase construct overexpression, and chemical inhibitors (Y27632 and fasudil), which inhibit both ROCK1 and ROCK2. Gene targeting and RNA interference approaches allow further dissection of distinct cellular, physiological and patho-physiological functions of the two ROCK isoforms. This review, based on recent molecular, cellular and animal studies, focuses on the current understanding of ROCK signaling in the regulation of apoptosis and highlights the new findings from recently generated ROCK-deficient mice.

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Section: Substrates Of Rockmentioning

confidence: 99%

Rho kinase in the regulation of cell death and survival

Shi

Wei

2007

Arch. Immunol. Ther. Exp.

219

183

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“…Rho family GTPases can be activated by angiotensin II, the hypertension-inducing effector molecule in the renin-angiotensin system involved in the regulation of blood pressure (37,38). Rho family GTPases activate Rho kinases (39) and a signaling cascade which leads to increased microtubule phosphorylation and facilitation of microtubule disassembly, actin filament assembly, and finally, promotion of smooth muscle contraction (40)(41)(42).…”

Section: Biological Functions Of the Identified Proteins And Their Pomentioning

confidence: 99%

Proteome Analysis of Cultivated Vascular Smooth Muscle Cells from a CADASIL Patient

Ihalainen

Soliymani

Iivanainen

et al. 2007

Mol Med

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Cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy (CADASIL) is a vascular dementing disease caused by mutations in the NOTCH3 gene, most which are missense mutations leading to an uneven number of cysteine residues in epidermal growth factor-like repeats in the extracellular domain of Notch3 receptor (N3ECD). CADASIL is characterized by degeneration of vascular smooth muscle cells (VSMC) and accumulation of N3ECD on the VSMCs of small and middle-sized arteries. Recent studies have demonstrated that impairment of Notch3 signaling is not the primary cause of the disease. In the present study we used proteomic analysis to characterize the protein expression pattern of a unique material of genetically genuine cultured human CADASIL VSMCs. We identified 11 differentially expressed proteins, which are involved in protein degradation and folding, contraction of VSMCs, and cellular stress. Our findings indicate that misfolding of Notch3 may cause endoplasmic reticulum stress and activation of unfolded protein response, leading to increased reactive oxygen species and inhibition of cell proliferation. In addition, upregulation of contractile proteins suggests an alteration in the signaling system of VSMC contraction. The accumulation of N3ECD on the cell surface possibly upregulates the angiotensin II regulatory feedback loop and thereby enhances the readiness of the cells to respond to angiotensin II stimulation.

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“…ROCK also directly phosphorylates MLC, 43 ± 45 and phosphorylates and consequently inhibits MLC phosphatase. 46,47 ROCK phosphorylation of calponin 48 and CPI-17 49 relieves their inhibition of myosin ATPase activity thereby promoting increased actin-myosin contractile force. Taken together, ROCK activation leads to a concerted series of events that promotes actin filament stabilisation, increased interaction with myosin and contractile force generation, which together drive cell contraction.…”

Section: Introductionmentioning

confidence: 99%

Rho GTPase signalling pathways in the morphological changes associated with apoptosis

2002

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The killing and removal of superfluous cells is an important step during embryonic development, tissue homeostasis, wound repair and the resolution of inflammation. A specific sequence of biochemical events leads to a form of cell death termed apoptosis, and ultimately to the disassembly of the dead cell for phagocytosis. Dynamic rearrangements of the actin cytoskeleton are central to the morphological changes observed both in apoptosis and phagocytosis. Recent research has highlighted the importance of Rho GTPase signalling pathways to these changes in cellular architecture. In this review, we will discuss how these signal transduction pathways affect the structure of the actin cytoskeleton and allow for the efficient clearance of apoptotic cells.

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Identification of Calponin as a Novel Substrate of Rho-Kinase

Cited by 110 publications

References 46 publications

Rho kinase in the regulation of cell death and survival

Rho kinase in the regulation of cell death and survival

Proteome Analysis of Cultivated Vascular Smooth Muscle Cells from a CADASIL Patient

Rho GTPase signalling pathways in the morphological changes associated with apoptosis

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