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Rhotekin, RTKN
This gene encodes a scaffold protein that interacts with GTP-bound Rho proteins. Binding of this protein inhibits the GTPase activity of Rho proteins. This protein may interfere with the conversion of active, GTP-bound Rho to the inactive GDP-bound form by RhoGAP. Rho proteins regulate many important cellular processes, including cytokinesis, transcription, smooth muscle contraction, cell growth and transformation. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Rhodopsin, RhoA, Actin, ACID, CAN
Papers using Rhotekin antibodies
Activity of Rho-family GTPases during cell division as visualized with FRET-based probes
Matsuda Michiyuki et al., In The Journal of Cell Biology, 2001
... cDNA of Rhotekin was PCR amplified from a mouse spleen cDNA library (CLONTECH Laboratories, Inc.) ...
Papers on Rhotekin
Effect of RTKN on progression and metastasis of colon cancer in vitro.
Kong et al., Shanghai, China. In Biomed Pharmacother, Aug 2015
In the present study, we investigated the role of RTKN in colon cancer and explored underlying mechanisms.
Constitutive and Inducible Expression of Invasion-related Factors in PC-3 Prostate Cancer Cells.
Lindholm et al., South Korea. In J Cancer Prev, Jun 2015
METHODS: The high invasive and low invasive variant PC-3 cell sublines were obtained by serial selection following Matrigel-coated Transwell invasion and were characterized by Transwell invasion, luciferase reporter assay, and Rhotekin pull-down assay.
PKC-β exacerbates in vitro brain barrier damage in hyperglycemic settings via regulation of RhoA/Rho-kinase/MLC2 pathway.
Bayraktutan et al., Nottingham, United Kingdom. In J Cereb Blood Flow Metab, 2013
Hyperglycemia (25 mmol/L D-glucose) markedly increased RhoA/Rho-kinase protein expressions (in-cell westerns), MLC2 phosphorylation (immunoblotting), and PKC-β (PepTag assay) and RhoA (Rhotekin-binding assay) activities in HBMEC while concurrently reducing the expression of tight junction protein occludin.
Physiological roles of Rho and Rho effectors in mammals.
Narumiya et al., Kyoto, Japan. In Eur J Cell Biol, 2013
Upon binding GTP, Rho exerts its functions through downstream Rho effectors, such as ROCK, mDia, Citron, PKN, Rhophilin and Rhotekin.
Coupling S100A4 to Rhotekin alters Rho signaling output in breast cancer cells.
O'Connor et al., Lexington, United States. In Oncogene, 2013
In this study, we discovered that metastasis-associated protein S100A4 interacts with the Rho-binding domain (RBD) of Rhotekin, thus connecting S100A4 to the Rho pathway.
Dynamic functions of RhoA in tumor cell migration and invasion.
Chen et al., Lexington, United States. In Small Gtpases, 2013
This review highlights recent advances regarding how the cooperation of Rho effector Rhotekin and S100A4 suppresses stress fiber generation to permit RhoA-mediated lamellae formation.
A Salmonella typhimurium-translocated glycerophospholipid:cholesterol acyltransferase promotes virulence by binding to the RhoA protein switch regions.
Miller et al., Seattle, United States. In J Biol Chem, 2012
Using NMR and biochemistry, this work demonstrates that SseJ competes effectively with Rhotekin, ROCK, and PKN1 in binding to a similar RhoA surface.
cGMP-dependent protein kinase I is involved in neurite outgrowth via a Rho effector, rhotekin, in Neuro2A neuroblastoma cells.
Tsuji et al., Tokushima, Japan. In Biochem Biophys Res Commun, 2012
these findings suggest that cGK-Ialpha interacts with and phosphorylates rhotekin, thereby contributing to neurite outgrowth regulation.
Protein kinase D regulates RhoA activity via rhotekin phosphorylation.
Seufferlein et al., Ulm, Germany. In J Biol Chem, 2012
Protein kinase D regulates RhoA activity via phosphorylation rhotekin at Ser-435.
Inhibition of RhoA but not ROCK induces chondrogenesis of chick limb mesenchymal cells.
Sonn et al., Taegu, South Korea. In Biochem Biophys Res Commun, 2012
Inhibition of RhoA activity by CT04 was confirmed by pull down assay using the Rho-GTP binding domain of Rhotekin.
Thromboxane-induced actin polymerization in hypoxic pulmonary artery is independent of Rho.
Dakshinamurti et al., Winnipeg, Canada. In Am J Physiol Lung Cell Mol Physiol, 2012
Thromboxane receptor (TP) G protein coupling was measured by immunoprecipitation and probing for Gαq, G12, or G13, RhoA activation by Rhotekin-RBD affinity precipitation, and LIM kinase (LIMK) and cofilin phosphorylation by Western blot.
Identification of brain-specific angiogenesis inhibitor 2 as an interaction partner of glutaminase interacting protein.
Mohanty et al., İzmir, Turkey. In Biochem Biophys Res Commun, 2011
GIP has important roles in cellular signaling, protein scaffolding and modulation of tumor growth and interacts with a number of physiological partner proteins, including Glutaminase L, β-Catenin, FAS, HTLV-1 Tax, HPV16 E6, Rhotekin and Kir 2.3.
Role of p115RhoGEF in lipopolysaccharide-induced mouse brain microvascular endothelial barrier dysfunction.
Fei et al., Changsha, China. In Brain Res, 2011
The degree of RhoA activation was determined by a Rhotekin-based pull-down assay, and expression of p115RhoGEF, zonula occludens-1 (ZO-1), occludin and claudin-5 proteins were detected by Western blot analysis.
RhoA inactivation prevents photoreceptor axon retraction in an in vitro model of acute retinal detachment.
Townes-Anderson et al., Newark, United States. In Invest Ophthalmol Vis Sci, 2011
RhoA activation was determined with a Rhotekin binding assay.
Detection of activated Rho in fixed Xenopus tissue.
Steinbeisser et al., Heidelberg, Germany. In Dev Dyn, 2009
The assay makes use of a fusion protein of Rhotekin and Green-Fluorescent-Protein (RBD-GFP), which is produced in bacteria and can be purified biochemically.
miR-145 inhibits breast cancer cell growth through RTKN.
Zhao et al., Beijing, China. In Int J Oncol, 2009
Loss of miR-145 may provide a selective growth advantage for MCF-7 by targeting RTKN.
Interaction of a multi-domain adaptor protein, vinexin, with a Rho-effector, Rhotekin.
Asano et al., Kasugai, Japan. In Med Mol Morphol, 2009
Rhotekin forms a complex with vinexin and may play a role at focal adhesions.
SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are associated with altered interactions with SEPT4/SEPT11 and resistance to Rho/Rhotekin-signaling.
Nagata et al., Japan. In Hum Mutat, 2007
SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are associated with altered interactions with SEPT4/SEPT11 and resistance to Rho/Rhotekin-signaling
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