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CDC42 binding protein kinase alpha

MRCK, MRCKalpha, myotonic dystrophy kinase-related Cdc42-binding kinase alpha, myotonic dystrophy kinase-related Cdc42-binding kinase
The protein encoded by this gene is a member of the Serine/Threonine protein kinase family. This kinase contains multiple functional domains. Its kinase domain is highly similar to that of the myotonic dystrophy protein kinase (DMPK). This kinase also contains a Rac interactive binding (CRIB) domain, and has been shown to bind CDC42. It may function as a CDC42 downstream effector mediating CDC42 induced peripheral actin formation, and promoting cytoskeletal reorganization. Multiple alternatively spliced transcript variants have been described, and the full-length nature of two of them has been reported. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Cdc42, Rhodopsin, Actin, Akt, p21
Papers using MRCK antibodies
Rac1 is crucial for hair follicle integrity but is not essential for maintenance of the epidermis
Arkowitz Robert Alan, In PLoS ONE, 2005
... phospho-Rac1/Cdc42 (Ser71) were from Cell Signaling, Germany; monoclonal anti-IQGAP2 (Clone BB9), Upstate, MA, USA; polyclonal anti-MRCK alpha, Santa Cruz Biotechnology, CA, USA; anti-VASP, rhodamin-phalloidin; ...
Papers on MRCK
Molecular pathways: targeting the kinase effectors of RHO-family GTPases.
Chernoff et al., Philadelphia, United States. In Clin Cancer Res, 2015
When activated, RHO-family GTPases such as RAC1, CDC42, and RHOA, transmit signals by recruiting a variety of effector proteins, including the protein kinases PAK, ACK, MLK, MRCK, and ROCK.
Phosphorylation of Nonmuscle myosin II-A regulatory light chain resists Sendai virus fusion with host cells.
Jana et al., New Delhi, India. In Sci Rep, 2014
Inhibition of RLC phosphorylation using inhibitors against ROCK, but not PKC and MRCK, or overexpression of phospho-dead mutant of RLC enhances membrane fusion.
Myotonic dystrophy kinase-related Cdc42-binding kinases (MRCK), the ROCK-like effectors of Cdc42 and Rac1.
Manser et al., Singapore, Singapore. In Small Gtpases, 2014
The MRCK proteins are ∼190 kDa multi-domain proteins expressed in all cells and coordinate certain acto-myosin networks.
CCM-3/STRIPAK promotes seamless tube extension through endocytic recycling.
Derry et al., Toronto, Canada. In Nat Commun, 2014
We propose that endocytic recycling is mediated through the CDC-42-binding kinase MRCK-1, which interacts physically with CCM-3-STRIPAK.
A novel selective multikinase inhibitor of ROCK and MRCK effectively blocks cancer cell migration and invasion.
Yun et al., Penn Hills, United States. In Cancer Lett, 2014
Two structurally related protein kinase families, the Rho kinases (ROCK) and the myotonic dystrophy kinase-related Cdc42-binding kinases (MRCK) are required for migration and invasion of cancer cells.
Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) regulation of LIMK1 protein in lamellipodial F-actin dynamics.
Tan et al., Singapore, Singapore. In J Biol Chem, 2014
Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) has been shown to localize to the lamella of mammalian cells through its interaction with an adaptor protein, leucine repeat adaptor protein 35a (LRAP35a), which links it with myosin 18A (MYO18A) for activation of the lamellar actomyosin network essential for cell migration.
Evidence for a role of MRCK in mediating HeLa cell elongation induced by the C1 domain ligand HMI-1a3.
Tuominen et al., Helsinki, Finland. In Eur J Pharm Sci, 2014
Our experiments revealed that the isophthalates bind also to the C1 domains of β2-chimaerin, protein kinase D (PKD) and myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK), which are potential mediators of small GTPase signaling and cytoskeletal reorganization.
The actin-myosin regulatory MRCK kinases: regulation, biological functions and associations with human cancer.
Olson et al., Glasgow, United Kingdom. In J Mol Med (berl), 2014
Considerable effort has focussed on the role of MLC kinases, and yet the contributions of the myotonic dystrophy-related Cdc42-binding kinases (MRCK) proteins in MLC phosphorylation and cytoskeleton regulation have not been well characterized.
A novel small-molecule MRCK inhibitor blocks cancer cell invasion.
Olson et al., In Cell Commun Signal, 2013
Along with the related ROCK1 and ROCK2 kinases, the MRCK proteins initiate signalling events that lead to contractile force generation which powers cancer cell motility and invasion.
Rap1 potentiates endothelial cell junctions by spatially controlling myosin II activity and actin organization.
Mochizuki et al., Suita, Japan. In J Cell Biol, 2013
Here, we show that myotonic dystrophy kinase-related CDC42-binding kinase (MRCK)-mediated activation of non-muscle myosin II (NM-II) at cell-cell contacts is essential for Rap1-induced CAB formation.
Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase.
Leung et al., Singapore, Singapore. In Febs Lett, 2011
Data show that chelerythrine blocks cellular activity of MRCK resulted in the specific loss of NM II-associated MLC phosphorylation in the lamella, and the consequential suppression of cell migration.
Human MRCKalpha is regulated by cellular iron levels and interferes with transferrin iron uptake.
Vyoral et al., Praha, Czech Republic. In Biochem Biophys Res Commun, 2010
MRCKalpha takes part in transferrin (Tf)-iron uptake, probably via regulation of Tf- TfR endocytosis/endosome trafficking that is dependent on the cellular cytoskeleton.
Myotonic dystrophy protein kinase (DMPK) and its role in the pathogenesis of myotonic dystrophy 1.
Llagostera et al., Barcelona, Spain. In Cell Signal, 2008
DMPK is a Ser/Thr protein kinase homologous to the p21-activated kinases MRCK and ROCK/rho-kinase/ROK.
A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow.
Leung et al., Singapore, Singapore. In Cell, 2008
Study reports that MRCK and myosin II-related MYO18A linked by the adaptor protein LRAP35a form a functional tripartite complex, which is responsible for the assembly of lamellar actomyosin bundles and of a subnuclear actomyosin network.
Characterization of the interaction of phorbol esters with the C1 domain of MRCK (myotonic dystrophy kinase-related Cdc42 binding kinase) alpha/beta.
Blumberg et al., Bethesda, United States. In J Biol Chem, 2008
analysis of the interaction of phorbol esters with the C1 domain of MRCK (myotonic dystrophy kinase-related Cdc42 binding kinase) alpha/beta
Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells.
Sahai et al., London, United Kingdom. In Nat Cell Biol, 2007
Instead, carcinoma cells use Cdc42 and MRCK (myotonic dystrophy kinase-related CDC42-binding protein kinases) mediated regulation of MLC to follow the tracks generated by fibroblasts.
Regulation of ephexin1, a guanine nucleotide exchange factor of Rho family GTPases, by fibroblast growth factor receptor-mediated tyrosine phosphorylation.
Sakaguchi et al., Wakayama, Japan. In J Biol Chem, 2007
FGFR-mediated phosphorylation of ephexin1 enhances the guanine nucleotide exchange activity toward RhoA without affecting the activity to Rac1 or Cdc42.
PAK and other Rho-associated kinases--effectors with surprisingly diverse mechanisms of regulation.
Manser et al., Singapore, Singapore. In Biochem J, 2005
Here we focus on our current understanding of the way in which different Rho-associated serine/threonine kinases, denoted PAK (p21-activated kinase), MLK (mixed-lineage kinase), ROK (Rho-kinase), MRCK (myotonin-related Cdc42-binding kinase), CRIK (citron kinase) and PKN (protein kinase novel), interact with and are regulated by their partner GTPases.
Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion.
Marshall et al., London, United Kingdom. In Nat Cell Biol, 2005
a Cdc42-MRCK signal mediates myosin-dependent cell motility and there is convergence between Rho and Cdc42 signalling
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