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findings reveal a key role for RABGEF1 in dampening keratinocyte-intrinsic MYD88 (show MYD88 Proteins) 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 (show INS Proteins) resistance in 3T3-L1 adipocytes by retaining GLUT4 (show SLC2A4 Proteins) in a Rab5 (show RAB5A Proteins)-activity-dependent compartment.
Kruppel-like factor 5 (show KLF5 Proteins) is indispensable for adhesion, homing, lodging and retention of haematopoietic stem cells and progenitors in the bone marrow through Rab5 (show RAB5A Proteins)-dependent post-translational regulation of beta1/beta2 integrins
Rab5 (show RAB5A Proteins) 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 (show RAB5A Proteins), which is localized in both axons and dendrites, and Rab17 (show RAB17 Proteins), 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 (show TSLP Proteins)) production in vivo and that excessive production of TSLP (show TSLP Proteins) contributes to many of the phenotypic abnormalities in Rabgef1-/- mice.
Data reveal the affinity of Rabex-5/Rabaptin-5/Rab5 (show RAB5A Proteins)-GTP (show AK3 Proteins) 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 (show RAD51AP1 Proteins) as a binding site on early endosomes for direct recruitment of Rabex-5 and activation of Rab5 (show RAB5A Proteins), establishing a Rab22 (show RAD51AP1 Proteins)-Rab5 (show RAB5A Proteins) signaling relay to promote early endosome fusion.
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 (show CRBN Proteins) 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 (show RAB5A Proteins) and instead indicate that Rbpt5 is recruited by both Rabex5 recognizing ubiquitylated cargo and by Rab4 (show RAB4A Proteins) to activate Rab5 (show RAB5A Proteins) 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 (show LRPAP1 Proteins) 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 (show RAB5A Proteins) depends on interaction of the MIU domain with the ubiquitinated L1 to drive its internalization.
these data suggest differential physiological roles of the two ubiquitin binding domains in Rabex-5.
Receptor recycling is mediated by AP-1 (show JUN Proteins)/clathrin-coated vesicles and regulated by rab4 (show RAB4A Proteins) 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 (show ARHGEF12 Proteins) activity and of Rab5 (show RAB5A Proteins).
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