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CDC42 binding protein kinase beta

CDC42BPB, MRCKbeta, CDC42-binding protein kinase beta
This gene encodes a member of the serine/threonine protein kinase family. The encoded protein contains a Cdc42/Rac-binding p21 binding domain resembling that of PAK kinase. The kinase domain of this protein is most closely related to that of myotonic dystrophy kinase-related ROK. Studies of the similar gene in rat suggested that this kinase may act as a downstream effector of Cdc42 in cytoskeletal reorganization. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Cdc42, SET, Rhodopsin, p21, FINGER1
Papers on CDC42BPB
Protein kinases paralleling late-phase LTP formation in dorsal hippocampus in the rat.
Lubec et al., Vienna, Austria. In Neurochem Int, 2014
Induction of LTP was proven, elevated levels for protein kinases PKN1, RPS6KB1, STK4, CDC42BPB, PRKG, TLK, BMX and decreased levels for NEK7, MAK14 and PLK1 were observed.
Characterization of a chemical affinity probe targeting Akt kinases.
Kuster et al., Freising, Germany. In J Proteome Res, 2013
The results confirmed the inhibition of all Akt isoforms and of a number of known as well as CDC42BPB as a novel putative target for GSK690693.
ErbB2-driven breast cancer cell invasion depends on a complex signaling network activating myeloid zinc finger-1-dependent cathepsin B expression.
Kallunki et al., Copenhagen, Denmark. In Mol Cell, 2012
We identify Cdc42-binding protein kinase beta, extracellular regulated kinase 2, p21-activated protein kinase 4, and protein kinase C alpha as essential mediators of ErbB2-induced cysteine cathepsin expression and breast cancer cell invasiveness.
Common variants on 14q32 and 13q12 are associated with DLBCL susceptibility.
Matsuda et al., Tokyo, Japan. In J Hum Genet, 2011
By following two-stage GWAS approach and an independent replication study, we identified disease susceptibility locus within intron 3 of the CDC42BPB gene on 14q32 (rs751837; P=3.30 × 10(-7) and odds ratio (OR) of 3.5), a region of frequent chromosomal translocations in lymphoma, and variant on 13q12 (rs7097; P=6.57
Cdc42-dependent formation of the ZO-1/MRCKβ complex at the leading edge controls cell migration.
Zhang et al., Hong Kong, Hong Kong. In Embo J, 2011
Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration.
A Boolean-based systems biology approach to predict novel genes associated with cancer: Application to colorectal cancer.
Reverter et al., Brisbane, Australia. In Bmc Syst Biol, 2010
These genes include the following: 1) secreted proteins as potential biomarkers for the early detection of colorectal cancer (FXYD1, GUCA2B, REG3A); 2) kinases as potential drug candidates to prevent tumor growth (CDC42BPB, EPHB3, TRPM6); and 3) potential oncogenic transcription factors (CDK8, MEF2C, ZIC2).
Co-crystal structures of inhibitors with MRCKβ, a key regulator of tumor cell invasion.
Olson et al., London, United Kingdom. In Plos One, 2010
these results provide further validation for MRCK involvement in regulation of cancer cell invasion.
Overexpression and unique rearrangement of VH2 transcripts in immunoglobulin variable heavy chain genes in ankylosing spondylitis patients.
Nam et al., Germany. In Exp Mol Med, 2010
Q-PCR results demonstrated VH2 genes were overexpressed in ankylosing spondylitis patients. The sequence analysis revealed the majority of them contained CDC42 binding protein kinase Beta (CDC42 BPB) genes.
Gene expression profiling of TGFbeta2- and/or BMP7-treated trabecular meshwork cells: Identification of Smad7 as a critical inhibitor of TGF-beta2 signaling.
Tamm et al., Regensburg, Germany. In Exp Eye Res, 2009
Among the genes that were found to be regulated were CAPZA1, CDC42BPB, EFEMP1, FGF5, FSTL3, HBEGF, LTBP1, LTBP2, MATN2, NRP1, SERPINE1, SH3MD1, SMTN, SMAD7, TFPI2, TNFAIP6, and VEGF.
Visual screening and analysis for kinase-regulated membrane trafficking pathways that are involved in extensive beta-amyloid secretion.
Murata et al., Tokyo, Japan. In Genes Cells, 2009
As the result of our visual screening, which examined the effect of kinase inhibitors and a kinase siRNA library, we identified five kinases (CDC42BPB, PRKACA, PRKACG, GSK3 beta and CSNK2A1) that regulate CI-M6PR trafficking.
Molecular profiles of schizophrenia in the CNS at different stages of illness.
Thomas et al., Los Angeles, United States. In Brain Res, 2008
While only four genes, SAMSN1, CDC42BPB, DSC2 and PTPRE, were consistently expressed across all groups, there was dysfunction in overlapping systems among all stages, including cellular signal transduction, lipid metabolism and protein localization.
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
Proteins associated with Cisplatin resistance in ovarian cancer cells identified by quantitative proteomic technology and integrated with mRNA expression levels.
Lin et al., Seattle, United States. In Mol Cell Proteomics, 2006
S100 protein family members (8.7-fold), junction adhesion molecule Claudin 4 (7.2-fold), and CDC42-binding protein kinase beta (5.4-fold).
The mouse kinome: discovery and comparative genomics of all mouse protein kinases.
Manning et al., San Francisco, United States. In Proc Natl Acad Sci U S A, 2004
First identified and named MRCKb based on sequence similarity to MRCKa (CDC42bpa) and orthology to human MRCKb/CDC42bpb
The COOH terminus of Rho-kinase negatively regulates rho-kinase activity.
Kaibuchi et al., Ikoma, Japan. In J Biol Chem, 1999
The chemical compounds such as HA1077 and Y-32885 inhibited not only the Rho-kinase activity but also the activity of protein kinase N, one of the targets of Rho, but had less of an effect on the activity of myotonic dystrophy kinase-related Cdc42-binding kinase beta (MRCKbeta).
Cloning and chromosomal localization of human Cdc42-binding protein kinase beta.
Johnson et al., Glasgow, United Kingdom. In Genomics, 1999
Here we report the cDNA cloning of the human homologue of MRCKbeta, CDC42BPB, which was found by Northern blot analysis to be expressed in a wide range of tissues.
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