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anti-Mouse (Murine) RABGEF1 Anticorps:
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Human Polyclonal RABGEF1 Primary Antibody pour ICC, IF - ABIN4348995
Lucitti, Sealock, Buckley, Zhang, Xiao, Dudley, Faber: Variants of Rab GTPase-Effector Binding Protein-2 Cause Variation in the Collateral Circulation and Severity of Stroke. dans Stroke 2016
Show all 2 Pubmed References
AP-1/sigma1A-ArfGAP1-Rabex-5 complex formation leads to more endosomal Rabex-5 and enhanced, Rab5(GTP)-stimulated Vps34 PI3-kinase activity, which is essential for multivesicular body endosome formation.
findings reveal a key role for RABGEF1 in dampening keratinocyte-intrinsic MYD88 signaling and sustaining epidermal barrier function
Knockdown of RABEX-5 also inhibited wound healing, migration and the invasive abilities of gastric cancer cells.
Hyperinsulinemia induced insulin resistance in 3T3-L1 adipocytes by retaining GLUT4 in a Rab5-activity-dependent compartment.
Kruppel-like factor 5 is indispensable for adhesion, homing, lodging and retention of haematopoietic stem cells and progenitors in the bone marrow through Rab5-dependent post-translational regulation of beta1/beta2 integrins
Rab5 is required for phagocytosis of heat-inactivated Pseudomonas aeruginosa by macrophages.
Rabex-5 regulates neurite morphogenesis of hippocampal neurons by activating at least two downstream targets, Rab5, which is localized in both axons and dendrites, and Rab17, which is localized in dendrites alone
a novel mechanistic insight into how Rabex-5 regulates internalization and postendocytic trafficking of ubiquitinated L1 destined for lysosomal degradation.
Data show that RabGEF1 can negatively regulate thymic stromal lymphopoietin (TSLP) production in vivo and that excessive production of TSLP contributes to many of the phenotypic abnormalities in Rabgef1-/- mice.
Data reveal the affinity of Rabex-5/Rabaptin-5/Rab5-GTP interaction in the cell, which is quantitatively related to the Rabex-5 concentration for the onset of the indirect positive feedback pathway.
Data report the identification of Rab22 as a binding site on early endosomes for direct recruitment of Rabex-5 and activation of Rab5, establishing a Rab22-Rab5 signaling relay to promote early endosome fusion.
RabGEF1 is a negative regulator of Fc epsilon RI-dependent mast cell activation, and a lack of RabGEF1 results in the development of skin inflammation in vivo.
p85alpha protein may play a role in the down-regulation of activated receptors through its temporal control of the GTPase cycles of Rab5 and Rab4
RabGEF1 plays a critical role in the regulation of SCF/c-Kit-mediated signaling events and biological responses in mast cells.
Data show that RabGEF1 is a negative regulator of Ras signalling and FcepsilonRI-dependent mast cell activation in vitro, and a lack of RabGEF1 results in the development of elevated numbers of mast cells in the skin and severe skin inflammation in vivo.
Insulin-stimulated Interaction between insulin receptor substrate 1 and p85alpha and activation of protein kinase B/Akt require Rab5.
Our data demonstrate that TeNT H(C) uses a retrograde transport pathway shared with p75(NTR), TrkB, and BDNF, which is strictly dependent on the activities of both Rab5 and Rab7
The authors demonstrate that RABGEF1, the upstream factor of the endosomal Rab GTPase cascade, is recruited to damaged mitochondria via ubiquitin binding downstream of Parkin. RABGEF1 directs the downstream Rab proteins, RAB5 and RAB7A, to damaged mitochondria, whose associations are further regulated by mitochondrial Rab-GAPs.
RABEX-5 mRNA expression was significantly upregulated in colorectal cancer tissues.
we identify Rabex-5 as a Immunomodulatory drugs (IMiDs) target molecule that functions to restrain TLR activated auto-immune promoting pathways. We propose that release of Rabex-5 from complex with Cereblon enables the suppression of immune responses, contributing to the antiinflammatory properties of IMiDs.
RABGEF1 mediates recycling endosome fusion with GAS-containing autophagosome-like vacuoles through the STX6-VAMP3-VTI1B complex; SNAREs are involved in autophagosome formation in response to bacterial infection
The results contradict the model of feedback activation of Rab5 and instead indicate that Rbpt5 is recruited by both Rabex5 recognizing ubiquitylated cargo and by Rab4 to activate Rab5 in a feed-forward manner.
RABEX-5 is a potential useful indicator and predicts a poor long-term prognosis for small cell lung cancer(SCLC), which should be considered in defining the prognosis with other well-known prognosticators in C-SCLC patients
Expression of RABEX-5 is significantly higher in gastric cancer tissues and is associated with tumor size and lymph node metastasis.
analysis of Rabex-5 GEF activation by Rabaptin-5
This implies that Rap regulates endothelial barrier function by dual control of cytoskeletal tension. The molecular details of the signaling pathways are becoming to be elucidated
RABEX-5 mRNA expression is a strong predictor of poor prognosis in prostate cancer patients treated by radical prostatectomy.
Interaction of Rabex-5 with Rab5 depends on interaction of the MIU domain with the ubiquitinated L1 to drive its internalization.
KCa2.3 is localized to a caveolin-rich domain within the plasma membrane and is endocytosed in a dynamin- and Rab5-dependent manner.
RABEX-5 and RAB5 may be involved in the development of breast cancer metastasis.
functions as an E3 ligase for Ras
GGAs, a family of Arf-dependent clathrin adaptors involved in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5 complex, a Rab4/Rab5 effector regulating endosome fusion
Here, we report that Rabex-5, a guanine nucleotide exchange factor for Rab5, binds to ubiquitin through two independent ubiquitin binding domains
Fc epsilon RI-mediated mast cell functional activation is dependent on RabGEF1's GEF activity
crystal structure of the RABEX-5 catalytic core in complex with nucleotide-free RAB21, a key intermediate in the exchange reaction pathway
these data suggest differential physiological roles of the two ubiquitin binding domains in Rabex-5.
Receptor recycling is mediated by AP-1/clathrin-coated vesicles and regulated by rab4 and rabaptin-5/rabex-5.
Rabex-5 is a ubiquitin ligase that binds ubiquitin and undergoes ubiquitination; the N-terminal region of Rabex-5 (residues 1-76) is important for ubiquitin binding and ubiquitination.
The structure of the N-terminal portion of Rabex-5 bound to ubiquitin at 2.5-A resolution shows that Rabex-5-ubiquitin interactions occur at two sites
Rabex-5 can target to early endosomes via the EET domain and activate Rab5 in a Rabaptin-5-independent manner in vivo.
Data show that ubiquitin binding is essential for the recruitment of Rabex-5 from the cytosol to endosomes, independently of its guanine nucleotide exchange factor activity and of Rab5.
RABGEF1 forms a complex with rabaptin-5 (RABPT5\; MIM 603616) that is required for endocytic membrane fusion, and it serves as a specific guanine nucleotide exchange factor (GEF) for RAB5 (RAB5A\; MIM 179512) (Horiuchi et al., 1997
Rab5 exchange factor
, Ras negative regulator Rabex-5
, Ras negative regulator Rabex-5/Rin2
, rab5 GDP/GTP exchange factor
, rabaptin-5-associated exchange factor for Rab5
, Rab5 guanine nucleotide exchange factor Rabex-5
, RAB guanine nucleotide exchange factor (GEF) 1
, Rab5 GDP/GTP exchange factor
, BTB/POZ domain-containing protein KCTD7
, RAB guanine nucleotide exchange factor (GEF) 1 L homeolog