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RAB33B, member RAS oncogene family

Small GTP-binding proteins of the RAB family, such as RAB33B, play important roles at defined steps of vesicular transport in protein secretion and the endocytosis pathway (Zheng et al., 1998 [PubMed 9512502]).[supplied by OMIM, Feb 2010] (from NCBI)
Top mentioned proteins: Rab5, ATG16L1, Rab6, GAP, Rab33A
Papers on Rab33B
RUTBC1 Functions as a GTPase-activating Protein for Rab32/38 and Regulates Melanogenic Enzyme Trafficking in Melanocytes.
Ohbayashi et al., Tsukuba, Japan. In J Biol Chem, Feb 2016
In this study we investigated RUTBC1, which was originally characterized as a Rab9-binding protein and GAP for Rab32 and Rab33B in vitro, and the results demonstrated that RUTBC1 functions as a physiological GAP for Rab32/38 in the trafficking of all three melanogenic enzymes in mouse melanocytes.
Rab33B and its autophagic Atg5/12/16L1 effector assist in hepatitis B virus naked capsid formation and release.
Prange et al., Mainz, Germany. In Cell Microbiol, May 2015
Naked capsid release does not require functions of the endosome-associated Rab5, Rab7 and Rab27 proteins, but depends on functional Rab33B, a GTPase participating in autophagosome formation via interaction with the Atg5-Atg12/Atg16L1 complex.
The GTPase Rab26 links synaptic vesicles to the autophagy pathway.
Jahn et al., Göttingen, Germany. In Elife, 2014
Both endogenous and induced clusters co-localize with autophagy-related proteins such as Atg16L1, LC3B and Rab33B but not with other organelles.
Regulation of autophagy by the Rab GTPase network.
Wu et al., Chongqing, China. In Cell Death Differ, 2014
Rab1, Rab5, Rab7, Rab9A, Rab11, Rab23, Rab32, and Rab33B participate in autophagosome formation, whereas Rab9 is required in non-canonical autophagy.
Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase.
Pfeffer et al., Stanford, United States. In J Biol Chem, 2013
We show here that the medial Golgi-localized Rab33B GTPase has the potential to link functionally to the late Golgi, Rab6 GTPase, by its capacity for association with Ric1 and Rgp1 proteins.
Are Rab proteins the link between Golgi organization and membrane trafficking?
Storrie et al., Little Rock, United States. In Cell Mol Life Sci, 2012
These include Rab6, Rab33B, Rab1, Rab2, Rab18, and Rab43.
RUTBC1 protein, a Rab9A effector that activates GTP hydrolysis by Rab32 and Rab33B proteins.
Pfeffer et al., Stanford, United States. In J Biol Chem, 2011
Biochemical screening of RUTBC1 Rab protein substrates revealed highest in vitro GTP hydrolysis-activating activity with Rab32 and Rab33B.
Crystal structures of human TBC1D1 and TBC1D4 (AS160) RabGTPase-activating protein (RabGAP) domains reveal critical elements for GLUT4 translocation.
Shoelson et al., Boston, United States. In J Biol Chem, 2011
Like the yeast Gyp1p RabGAP domain, whose structure was solved previously in complex with mouse Rab33B, the human TBC1D1 and TBC1D4 domains both have 16 α-helices and no β-sheet elements.
OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation.
Fukuda et al., Sendai, Japan. In J Cell Biol, 2011
We further provide evidence that Rab33B, an Atg16L1-binding protein, is a target substrate of OATL1 and is involved in the fusion between autophagosomes and lysosomes, the same as OATL1.
Proteomic approach with LCMS-IT-TOF identified an increase of Rab33B after transient focal cerebral ischemia in mice.
Hara et al., Gifu, Japan. In Exp Transl Stroke Med, 2009
Among these proteins, we focused on Rab33b, a member of RAS oncogene family and we found that Rab33b was up-regulated in the ischemic striatum and the number of Rab33B-positive cells increased in a time-dependent manner.
Direct link between Atg protein and small GTPase Rab: Atg16L functions as a potential Rab33 effector in mammals.
Itoh et al., Sendai, Japan. In Autophagy, 2008
We recently reported finding that Atg16L specifically and directly interacts with the Golgi-resident small GTPase Rab33B (and Rab33A) via the coiled-coil domain of Atg16L.
Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation.
Fukuda et al., Sendai, Japan. In Mol Biol Cell, 2008
Rab33 modulates autophagosome formation through interaction with Atg16L
Cisternal rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress.
Storrie et al., Little Rock, United States. In Mol Biol Cell, 2005
Similarly, we found that Golgi tubulation induced by brefeldin A, a known microtubule-dependent process, was inhibited by GDP-restricted rab6a, rab6a', and rab33b, the most commonly studied cisternal rab proteins.
Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER.
Nilsson et al., Heidelberg, Germany. In Febs Lett, 2001
The role of rab33b, a Golgi-specific rab protein, was investigated.
A novel Rab GTPase, Rab33B, is ubiquitously expressed and localized to the medial Golgi cisternae.
Kakinuma et al., Sapporo, Japan. In J Cell Sci, 1998
We report here the molecular cloning and characterization of a novel Rab protein, Rab33B.
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