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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.
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RABEX-5 mRNA expression was significantly upregulated in colorectal cancer tissues.
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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.
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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
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findings reveal a key role for RABGEF1 in dampening keratinocyte-intrinsic MYD88 signaling and sustaining epidermal barrier function
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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.
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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
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Expression of RABEX-5 is significantly higher in gastric cancer tissues and is associated with tumor size and lymph node metastasis.
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analysis of Rabex-5 GEF activation by Rabaptin-5
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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
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RABEX-5 mRNA expression is a strong predictor of poor prognosis in prostate cancer patients treated by radical prostatectomy.
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Interaction of Rabex-5 with Rab5 depends on interaction of the MIU domain with the ubiquitinated L1 to drive its internalization.
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KCa2.3 is localized to a caveolin-rich domain within the plasma membrane and is endocytosed in a dynamin- and Rab5-dependent manner.
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a novel mechanistic insight into how Rabex-5 regulates internalization and postendocytic trafficking of ubiquitinated L1 destined for lysosomal degradation.
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RABEX-5 and RAB5 may be involved in the development of breast cancer metastasis.
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functions as an E3 ligase for Ras
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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
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Here, we report that Rabex-5, a guanine nucleotide exchange factor for Rab5, binds to ubiquitin through two independent ubiquitin binding domains
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Fc epsilon RI-mediated mast cell functional activation is dependent on RabGEF1's GEF activity
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crystal structure of the RABEX-5 catalytic core in complex with nucleotide-free RAB21, a key intermediate in the exchange reaction pathway