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RAP1 GTPase activating protein

Rap1GAP, Rap1 GTPase-activating protein, Rap1GAPII
This gene encodes a type of GTPase-activating-protein (GAP) that down-regulates the activity of the ras-related RAP1 protein. RAP1 acts as a molecular switch by cycling between an inactive GDP-bound form and an active GTP-bound form. The product of this gene, RAP1GAP, promotes the hydrolysis of bound GTP and hence returns RAP1 to the inactive state whereas other proteins, guanine nucleotide exchange factors (GEFs), act as RAP1 activators by facilitating the conversion of RAP1 from the GDP- to the GTP-bound form. In general, ras subfamily proteins, such as RAP1, play key roles in receptor-linked signaling pathways that control cell growth and differentiation. RAP1 plays a role in diverse processes such as cell proliferation, adhesion, differentiation, and embryogenesis. Alternative splicing results in multiple transcript variants encoding distinct proteins. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: Rap1, GAP, V1a, CAN, RAP
Papers using Rap1GAP antibodies
Camp-sensitive and rapamycin-sensitive regulation of the association of eukaryotic initiation-factor 4e and the translational regulator Phas-I in aortic smooth-muscle cells
Bond Mark et al., In Journal of Molecular and Cellular Cardiology, 1994
... #9251, #9258; Cell Signalling), V5-tag (#R960-25; Invitrogen), paxillin (#610051; BD Biosciences), BrdU (#B2531; Sigma) and Rap1GAP (#ab32373; Abcam).
Papers on Rap1GAP
[The effect of up-regulated expression of Rap1GAP on the invasion ability of HL-60 cells in vitro and in vivo].
Chen et al., Suzhou, China. In Zhonghua Xue Ye Xue Za Zhi, Jul 2015
OBJECTIVE: To investigate the effect of up-regulation of Rap1GAP on the invasion ability of leukemic HL-60 cells in vitro, and to establish leukemia mouse model to verify the effects in vivo.
GABAB receptor promotes its own surface expression by recruiting a Rap1-dependent signaling cascade.
Liu et al., Wuhan, China. In J Cell Sci, Jul 2015
Agonist stimulation of GABA(B) receptor signals through Gαi/o to inhibit Rap1GAPII (also known as Rap1GAP1b, an isoform of Rap1GAP1), thereby activating Rap1 (which has two isoforms, Rap1a and Rap1b) in cultured cerebellar granule neurons (CGNs).
High SIPA-1 expression in proximal tubules of human kidneys under pathological conditions.
Su et al., Wuhan, China. In J Huazhong Univ Sci Technolog Med Sci, Feb 2015
Signal-induced proliferation-associated protein 1 (SIPA-1) is a Rap1GTPase activating protein (Rap1GAP) expressed in the normal distal and collecting tubules of the murine kidney.
Crucial role of the Rap G protein signal in Notch activation and leukemogenicity of T-cell acute lymphoblastic leukemia.
Minato et al., Kyoto, Japan. In Sci Rep, 2014
Attenuation of the Rap signal by the expression of a dominant-negative Rap1A17 or Rap1GAP, Sipa1, in a T-ALL cell line resulted in the reduced Notch processing at site 2 due to impaired maturation of Adam10.
The Ras GTPase-activating protein Rasal3 supports survival of naive T cells.
Suzuki et al., Ichikawa, Japan. In Plos One, 2014
Our results showed that Rasal3 possesses RasGAP activity, but not Rap1GAP activity, and represses TCR-stimulated ERK phosphorylation in a T cell line.
Constitutively active signaling by the G protein βγ-subunit mediates intrinsically increased phosphodiesterase-4 activity in human asthmatic airway smooth muscle cells.
Grunstein et al., Philadelphia, United States. In Plos One, 2014
Importantly, along with increased Gβγ activation, asthmatic HASM cells also exhibit constitutively increased direct binding of the small Rap1 GTPase-activating protein, Rap1GAP, to the α-subunit of Gi protein, which serves to cooperatively facilitate Ras activation and, thereby, enable enhanced Gβγ-regulated ERK1/2-stimulated PDE activity.
RAP1GAP inhibits cytoskeletal remodeling and motility in thyroid cancer cells.
Meinkoth et al., Philadelphia, United States. In Endocr Relat Cancer, 2012
Downregulation of RAP1GAP in thyroid tumors enhances SRC-dependent signals that regulate cellular architecture and motility.
Rap1GAP regulates renal cell carcinoma invasion.
Daaka et al., Gainesville, United States. In Cancer Lett, 2012
Over-expression of Rap1GAP attenuated levels of both cadherins and integrins that are known to regulate the cancer cells invasion in renal cel carcinoma.
Id proteins synchronize stemness and anchorage to the niche of neural stem cells.
Lasorella et al., New York City, United States. In Nat Cell Biol, 2012
The interrogation of the gene modules directly targeted by Id deletion in NSCs revealed that Id proteins repress bHLH-mediated activation of Rap1GAP, thus serving to maintain the GTPase activity of RAP1, a key mediator of cell adhesion.
Plexins are GTPase-activating proteins for Rap and are activated by induced dimerization.
Zhang et al., Dallas, United States. In Sci Signal, 2012
Plexins are GTPase-activating proteins for Rap and are activated by induced dimerization
Prostaglandin E2 regulates renal cell carcinoma invasion through the EP4 receptor-Rap GTPase signal transduction pathway.
Daaka et al., Augusta, United States. In J Biol Chem, 2011
Human kidney cells evidence increased EP4 and decreased Rap1GAP expression levels in the malignant compared with benign samples.
Rap1GAP impairs cell-matrix adhesion in the absence of effects on cell-cell adhesion.
Meinkoth et al., Philadelphia, United States. In Cell Adh Migr, 2011
Rap1GAP is a more effective inhibitor of cell-matrix adhesion compared to cell-cell adhesion.
RapGAPs in brain: multipurpose players in neuronal Rap signalling.
Kreutz et al., Magdeburg, Germany. In Eur J Neurosci, 2010
In the brain, the most prominent RapGAPs are Rap1GAP and those of the spine-associated RapGAP (SPAR) family.
Regulatory function and expression of rap1gap gene in hematopoietic cells-review.
Chen et al., Suzhou, China. In Zhongguo Shi Yan Xue Ye Xue Za Zhi, 2009
Rap1 is a small G protein belonging to the RAS superfamily.
Role of the Go/i signaling network in the regulation of neurite outgrowth.
Iyengar et al., New York City, United States. In Can J Physiol Pharmacol, 2006
The CB1 cannabinoid receptor, a Go/i-coupled receptor expressed endogenously in Neuro2A cells, triggers neurite outgrowth by activating Rap1, which promotes the Galphao-stimulated proteasomal degradation of Rap1GAPII.
Rap1 signal controls B cell receptor repertoire and generation of self-reactive B1a cells.
Minato et al., Kyoto, Japan. In Immunity, 2006
We previously reported that the mice deficient for SPA-1, a Rap1 GTPase-activating protein, developed hematopoietic stem cell disorders.
Rap1 and SPA-1 in hematologic malignancy.
Minato et al., Kyoto, Japan. In Trends Mol Med, 2004
In lymphohematopoietic tissues, SPA-1 is a principal Rap1 GTPase-activating protein.
The GTPase-activating protein Rap1GAP uses a catalytic asparagine.
Wittinghofer et al., Dortmund, Germany. In Nature, 2004
Here we present the crystal structure of the catalytic domain of the Rap1-specific Rap1GAP at 2.9 A. By mutational analysis, fluorescence titration and stopped-flow kinetic assay, we demonstrate that Rap1GAP provides a catalytic asparagine to stimulate GTP hydrolysis.
Return of the GDI: the GoLoco motif in cell division.
Siderovski et al., Chapel Hill, United States. In Annu Rev Biochem, 2003
The GoLoco motif is present as an independent element within multidomain signaling regulators, such as Loco, RGS12, RGS14, and Rap1GAP, as well as in tandem arrays in proteins, such as AGS3, G18, LGN, Pcp-2/L7, and Partner of Inscuteable (Pins/Rapsynoid).
Myeloproliferative stem cell disorders by deregulated Rap1 activation in SPA-1-deficient mice.
Minato et al., Kyoto, Japan. In Cancer Cell, 2003
SPA-1 (signal-induced proliferation-associated gene-1) is a principal Rap1 GTPase-activating protein in hematopoietic progenitors.
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