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RAP2B, member of RAS oncogene family

Rap2B, small GTP-binding protein
This intronless gene belongs to a family of RAS-related genes. The proteins encoded by these genes share approximately 50% amino acid identity with the classical RAS proteins and have numerous structural features in common. The most striking difference between the RAP and RAS proteins resides in their 61st amino acid: glutamine in RAS is replaced by threonine in RAP proteins. Evidence suggests that this protein may be polyisoprenylated and palmitoylated. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Rhodopsin, Actin, ACID, RhoA, CAN
Papers using Rap2B antibodies
Nitric oxide inhibits Leydig cell steroidogenesis.
Deretic Vojo, In PLoS Pathogens, 1995
... The anti-myc antibody, the anti-Rap2b antibody, and Rap2b siRNA were purchased from Santa Cruz Biotechnology (Buenos Aires, Argentina) ...
Papers on Rap2B
Arf6 controls platelet spreading and clot retraction via integrin αIIbβ3 trafficking.
Whiteheart et al., Lexington, United States. In Blood, Feb 2016
ADP-ribosylation factor 6 (Arf6) is a small GTP-binding protein known to regulate endocytic trafficking, especially of integrins.
Statins up-regulate SmgGDS through β1-integrin/Akt1 pathway in endothelial cells.
Shimokawa et al., Asahi, Japan. In Cardiovasc Res, Feb 2016
We have recently demonstrated that the pleiotropic effects of statins are partly mediated through up-regulation of small GTP-binding protein dissociation stimulator (SmgGDS) with a resultant Rac1 degradation and reduced oxidative stress.
Genetic deletion of Rhes or pharmacological blockade of mTORC1 prevent striato-nigral neurons activation in levodopa-induced dyskinesia.
Morari et al., Ferrara, Italy. In Neurobiol Dis, Jan 2016
Ras homolog enriched in striatum (Rhes) is a small GTP-binding protein that modulates signal transduction at dopamine receptors, and also activates mammalian target of rapamycin complex 1 (mTORC1).
Rho Kinase and Dopaminergic Degeneration: A Promising Therapeutic Target for Parkinson's Disease.
Guerra et al., Santiago de Compostela, Spain. In Neuroscientist, Dec 2015
The small GTP-binding protein Rho plays an important role in several cellular functions.
JAK2 tyrosine kinase mediates integrin activation induced by CXCL12 in B-cell chronic lymphocytic leukemia.
Laudanna et al., Verona, Italy. In Oncotarget, Nov 2015
We also show that JAK2 mediates the activation of the small GTP-binding protein RhoA, in turn controlling LFA-1 affinity triggering by CXCL12.
Lysine-acetylation as a fundamental regulator of Ran function: Implications for signaling of proteins of the Ras-superfamily.
Lammers et al., Köln, Germany. In Small Gtpases, Nov 2015
UNASSIGNED: The small GTP-binding protein Ran is involved in the regulation of essential cellular processes in interphase but also in mitotic cells: Ran controls the nucleocytoplasmic transport of proteins and RNA, it regulates mitotic spindle formation and nuclear envelope assembly.
2015 ATVB Plenary Lecture: translational research on rho-kinase in cardiovascular medicine.
Satoh et al., Sendai, Japan. In Arterioscler Thromb Vasc Biol, Aug 2015
Rho-kinase (ROCKs) is an important downstream effector of the small GTP-binding protein Ras homolog gene family member A. There are 2 isoforms of ROCK, ROCK1 and ROCK2, and they have different functions in several vascular components.
Modulation of actin dynamics by Rac1 to target cognitive function.
Tejada-Simon, Houston, United States. In J Neurochem, Jun 2015
Less research, however, has been done regarding the role of this small GTP-binding protein in brain development, where it has an important role in dendritic spine morphogenesis through the regulation of actin.
Regulation of bone and skeletal development by the SHP-2 protein tyrosine phosphatase.
King et al., Dallas, United States. In Bone, 2014
Src homology-2 protein tyrosine phosphatase (SHP-2) that is encoded by the PTPN11 gene in humans is an intracellular signaling molecule that couples growth factor receptors to activation of the Ras small GTP-binding protein that regulates cell growth, proliferation and differentiation.
The trials and tubule-ations of Rab6 involvement in Golgi-to-ER retrograde transport.
Simpson et al., Dublin, Ireland. In Biochem Soc Trans, 2014
At least two mechanisms of transport move material in the retrograde direction: one regulated by the cytoplasmic coatomer protein I complex (COPI), and a second COPI-independent pathway utilizing the small GTP-binding protein Rab6.
Genome-wide RNAi screening identifies human proteins with a regulatory function in the early secretory pathway.
Pepperkok et al., Dublin, Ireland. In Nat Cell Biol, 2012
Network analyses revealed a so far unappreciated link between early secretory pathway function, small GTP-binding protein regulation, actin cytoskeleton organization and EGF-receptor-mediated signalling.
Proteome analysis of the thalamus and cerebrospinal fluid reveals glycolysis dysfunction and potential biomarkers candidates for schizophrenia.
Turck et al., München, Germany. In J Psychiatr Res, 2010
This protein has been found differentially expressed in thalami from patients with schizophrenia.
MINK and TNIK differentially act on Rap2-mediated signal transduction to regulate neuronal structure and AMPA receptor function.
Sheng et al., Cambridge, United States. In J Neurosci, 2010
MINK interaction with Rap2 plays a critical role in maintaining the morphological integrity of dendrites and synaptic transmission.
Neurogenin 2 controls cortical neuron migration through regulation of Rnd2.
Guillemot et al., London, United Kingdom. In Nature, 2008
Here we show that the proneural protein neurogenin 2 (Neurog2), which controls neurogenesis in the embryonic cerebral cortex, directly induces the expression of the small GTP-binding protein Rnd2 (ref.
Targeting of the small GTPase Rap2b, but not Rap1b, to lipid rafts is promoted by palmitoylation at Cys176 and Cys177 and is required for efficient protein activation in human platelets.
Torti et al., Pavia, Italy. In Cell Signal, 2008
These results demonstrate that Rap2b, but not the more abundant Rap1b, is associated to lipid rafts in human platelets.
The Rab8 GTPase regulates apical protein localization in intestinal cells.
Harada et al., Japan. In Nature, 2007
The small GTP-binding protein Rab8 was thought to regulate basolateral transport in polarized kidney epithelial cells through the AP1B-complex-mediated pathway.
Identification of genes differentially expressed in human primary lung squamous cell carcinoma.
Cheng et al., Beijing, China. In Lung Cancer, 2007
A cDNA library consisting of 220 upregulated genes in tumour tissue was established and named as LSCC. Differential expression was confirmed in five of these genes, including IGFBP5, SQLE, RAP2B, CLDN1, and TBL1XR1.
Crystal structure of the RUN domain of the RAP2-interacting protein x.
Yokoyama et al., Yokohama, Japan. In J Biol Chem, 2006
the putative Rap2 binding site of the RPIPx RUN domain interacts with the extended segment in a segment-swapping manner
Mutations in a member of the Ras superfamily of small GTP-binding proteins causes Bardet-Biedl syndrome.
Leroux et al., Canada. In Nat Genet, 2004
These findings implicate a small GTP-binding protein in ciliary transport and the pathogenesis of a pleiotropic disorder.
The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras.
Negishi et al., Kyoto, Japan. In Science, 2004
This activity required the interaction of Plexin-B1 with Rnd1, a small GTP-binding protein of the Rho family.
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