The Rab GTPase family
By Harald A. Stenmark, V. Olkkonen. Genome Biology, 2001
772 citations recorded by the source corpus.
SummaryThe Rab family is part of the Ras superfamily of small GTPases. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they function as regulators of distinct steps in membrane traffic pathways. In the GTP-bound form, the Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion.
Subfields: Cell Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/5afab3e9b8272aa71e9c3cb0150e9a5ba212d483
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Citations in the corpus
- Macronuclear Genome Sequence of the Ciliate Tetrahymena thermophila, a Model Eukaryote (2006, neutral): “Based on localization and functional studies, including comparisons between yeast and humans [156], Rabs have been divided into eight groups [157].”
- Analysis of the Small GTPase Gene Superfamily of Arabidopsis1 (2003, background): “Furthermore, given the specific distributions of Rab GTPases to different cellular membranes, it was hypothesized that Rab GTPases would, in conjunction with SNARE proteins, provide specificity for membrane fusion events (for reviews, see Stenmark and Olkkonen, 2001; Zerial and McBride, 2001).”
- The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors. (2001, background): “Rab GTPases recruit and/or activate several proteins involved in membrane fusion and vesicular transport [5, 6].”
- Role for Rab7 in maturation of late autophagic vacuoles (2004, background): “It is possible that overexpression of Rab7 sequestered some effectors, such as GDI and REP (Somsel Rodman and Wandinger-Ness, 2000; Stenmark and Olkkonen, 2001), shared by other Rab proteins, which may also be necessary for autophagic vacuole maturation.”
- Efficiency of siRNA delivery by lipid nanoparticles is limited by endocytic recycling (2013, positive): “Late endosomes have been shown to exchange material with the Golgi/ER from where the cargo can be secreted to the extracellular milieu 32,33 and/or multivesicular bodies that can fuse with the plasma membrane to release their intracellular content as exosomes 34 .”