Author Correction Rab GTPases at a glance Samantha L. Schwartz, Canhong Cao, Olena Pylypenko, Alexey Rak and Angela Wandinger-Ness Journal of Cell Science 121, 246 (2008) doi:10.1242/jcs.03495 There was an error published in J. Cell Sci. 120, 3905-3910. The authors regret that in Table 1 under ‘(13) Rab1, Rab3, Rab8, Rab10, Rab12, Rab13, Rab15, Rab35, Rab40’, Rab35 was incorrectly referred to as an uncharacterized member of the Rab family. The correct details are given below. Rab Localization Function Reference Rab35 Plasma membrane, endosomes, intercellular bridge Rapid endocytic recycling and cytokinesis Kouranti et al., 2006 Cell Science at a Glance 3905 Rab GTPases at a brain) GTPases were first identified as associate with regulatory molecules and evolutionarily conserved, essential downstream effectors to exert their glance regulators of membrane trafficking functions (Chen et al., 2003; Pereira- Samantha L. Schwartz1, Canhong (Salminen and Novick, 1987; Schmitt et Leal and Seabra, 2000; Pfeffer, 2005). Cao1, Olena Pylypenko2 Alexey al., 1986; Touchot et al., 1987). The Rak2,3 and Angela Wandinger- proteins are members of the wider Ras Ness1,* superfamily of GTPases (Wennerberg et Rab GTPases regulate membrane al., 2005). Over 70 human Rab and Rab- trafficking, cell growth and 1Department of Pathology MSC08-4640, University of New Mexico, 2325 Camino de Salud NE, like members of the Ras superfamily differentiation CRF225, Albuquerque, NM 87131, USA have been identified (Colicelli, 2004; Characterization of around half of the 2Departments of Structural Biology and Physical Stenmark and Olkkonen, 2001), and the known Rab GTPases has revealed the Biochemistry, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany functions of 36 Rab GTPases have been extraordinary complexity of membrane 3Sanofi-Aventis, Centre de Recherche Paris,13, delineated. Rab GTPases are molecular trafficking circuits and shows that Rab Quai Jules Guesde–BP 14, 94403 Vitry sur Seine Cedex, France switches, cycling between active and GTPases are also essential for signaling *Author for correspondence (e-mail: inactive states and serving as scaffolds to and the control of cell proliferation [email protected]) integrate both membrane trafficking and and differentiation. Rab proteins are intracellular signaling in a temporally present on all compartments of the Journal of Cell Science 120, 3905-3910 Published by The Company of Biologists 2007 and spatially sensitive manner (Bucci endomembrane system (endoplasmic doi:10.1242/jcs.015909 and Chiariello, 2006; Zerial and reticulum, Golgi, endosomes, McBride, 2001). Despite the small sizes lysosomes), the nucleus, the plasma It has been two decades since the yeast of Rab proteins (20-25 kDa), structural membrane (including cell junctions and Ypt1 and Sec4 proteins and the analyses reveal they have multiple focal adhesions), mitochondria and mammalian Rab (Ras-related proteins in interaction surfaces through which they centrioles. In addition, they help regulate Rab GTPases at a Glance Samantha L. Schwartz, Canhong Cao, Olena Pylypenko, Alexey Rak and Angela Wandinger-Ness Rab structures Rab7-GTP Cilium jcs.biologists.org MTM1CS Rab5Q79L VPS34 IFT Rab7-GDP RAB7N1251I Rab7 Journal of Cell Science Rab12 Caveolae Rab7-GTP-RILP dimer (PDB ID 1YHN) Rab7-GDP-REP1 (PDB ID 1VGO) Apical membrane Rab23 Vesicle transport Secretory Rab8 CCV granule Centrioles Rab15 Donor membrane Melanosome Rab5a-c Caveosome Coat Rab4 Rab11a M6PR Rab13 Budding GDF TIP47 (fast) GDP Constitutive (slow) R GDP R ab ab M6P ab Rab4a GTP endocytosis R Early sorting Recycling REP endosome Rab17 Rab8b GEF GTP endosome GGT Rab GDP Rab27 Rab11a GDP Motor Regulated protein exocytosis Rab38 Rab22b Rab25 Cytoskeletal Rab32 MPC R Rab11a GDP transport R ab Rab27a,b Rab17 ab GTP Rab22a Rab7 SNARE Rab26 GDI Rab14 Basolateral Rab37 Tethering factor Rab6a membrane Rab3a-d GTP Rab9 GAP Late endosome Rab Rab11b Rab6a,b Pi Rab33b Rab14 GDP Cytoskeletal Rab22a ab Phagocytosis R filaments Rab7b Docking/fusion GDI Rab8 Endoplasmic reticulum Golgi Rab2 Lyososome Phagosome Acceptor membrane complex Signaling Rab1 EGF signaling Rab34 Macropinosome EGF Rab10 Rab23 Macropinocytosis NuRD Rab5 APPL1 APPL1 Rab34 GTP MeCP1 Autophagosome Basolateral Early Nucleus Sequestration of APPL1 Chromatin remodeling and changes Rab18 Rab5 membrane endosome on endosomes in gene expression in nucleus Rab24 GDP Lipid Rab3ab332 Relocation to cytoplasm Rab5 droplets Rab21 Metabolic signaling Insulin/AKT Ran MitochondriMitochondria Rab2 Rab8A Rab Rab8B GAPTbc1d4 Rab Rab10 GTP Tbc1d1 Rab14 GTP Endocytosis Focal adhesion PO4 Increased fusion of Glut4 Rab inactivation by Rab vesicles with plasma membrane GAP on cytoplasmic GAP GDP Glut4 storage vessels GAP inactivation Abbreviations: CCV, clathrin-coated vesicle; GAP, GTPase activating protein; GDF, GDI dissociation factor; GDI, GDP dissociation inhibitor; GGT, geranylgeranyltransferase; GDP, guanosine diphosphate; GEF, guanine nucleotide exchange factor; GTP, guanosine triphosphate; IFT, intraflagellar transport; M6P, mannose 6-phosphate; M6PR, cation-independent mannose 6-phosphate receptor; MPC, motor protein complex; Rab, Ras-related in brain; REP, Rab escort protein; RILP, Rab interacting lysosomal protein; SNARE, soluble NSF attachment receptor; TIP47, tail-interacting protein 47kD. © Journal of Cell Science 2007 (120, pp. 3905-3910) (See poster insert) 3906 Journal of Cell Science 120 (22) a vast array of basic cellular functions – destinations (colored lines on the poster junctional proteins and integrins and by from macromolecular homeostasis to denote such domains; the micrograph defining epithelial transport circuits to growth control. illustrates alternating Rab7 and Rab5 cilia (connecting with intraflagellar domains on dilated early endosomes) transport, IFT), the apical (AM) and Rab proteins are best known for their (Barbero et al., 2002; Vitale et al., 1998; basolateral (BM) membranes, and apical essential roles in exocytic and endocytic Vonderheit and Helenius, 2005). In this recycling endosomes (AREs). They thus membrane trafficking, which encompass way, Rab GTPases regulate plasma play major regulatory roles maintaining the constitutive and regulated secretory membrane delivery, organelle biogenesis compartment identity, regulating cargo routes, endocytosis via caveolae or and degradative pathways (lysosomal and delivery, controlling protein and lipid clathrin-coated vesicles (CCVs), autophagic). They also contribute to cell- storage/degradation and modulating micropinocytosis and phagocytosis. They type-specific functions, such as regulated specialized trafficking functions. control anterograde and retrograde secretion (secretory granules/lysosomes trafficking between compartments to in endocrine and exocrine cells), synaptic Rab proteins are increasingly found coordinate cargo delivery and membrane transmission [synaptic vesicles (SVs) in downstream of signaling cascades and recycling and also subcompartmentalize neurons] and phagocytosis (in can impact gene expression and growth organelles by organizing specific macrophages and dendritic cells). In control. Rab5, for example, is implicated membrane domains that function in epithelia, Rab GTPases help generate in EGF signaling and thought to trafficking of cargo to different polarity by regulating the trafficking of sequester APPL1, an adaptor protein Table 1. The Rab family Rab Localization Function References (1) Rab23 Rab23 Plasma membrane and endosomes Trafficking of sonic hedgehog signaling components; Evans et al., 2003 embryogenesis; ciliary trafficking (2) Rab29, Rab32, Rab38, Rab7L1 Rab32 Perinuclear vesicles; mitochondria Post-Golgi trafficking of melanogenic enzymes; binds Alto et al., 2002; Wasmeier et al., 2006 PKA and regulates mitochondrial dynamics Rab38 Tyrosinase-positive vesicles Post-Golgi biogenesis of melanosomes Wasmeier et al., 2006 (3) RabL2, RabL3, RabL5 (4) Ran Ran Nucleus, cytoplasm Nucleocytoplasmic transport Joseph, 2006 (5) Rab7, Rab7b, Rab9 Journal of Cell Science Rab7, Rab7b Late endosomes, lysosomes Transport from early to late endosomes; lysosome Feng et al., 2001; Bucci et al., 2000; Wang biogenesis; b) transport to lysosomes, TLR4 et al., 2007 signaling Rab9a,b,c Late endosomes Lysosomal enzyme and cholesterol trafficking; late Ganley et al., 2004; Lombardi et al., 1993; endosome to trans-Golgi transport Narita et al., 2005 (6) Rab28, RabL4 (7) Rab34, Rab36 Rab34 Cell surface membrane ruffles, Regulation of spatial distribution of lysosomes; Colucci et al., 2005; Sun and Endo, 2005; lysosomes Formation of macropinosomes Sun et al., 2003; Wu et al., 2005 (8) Rab6, Rab41 Rab6a,a′,b,c (a,a′,b) Golgi, (b) ERGIC-53-positive Retrograde transport; (a,b) Golgi to ER and intra- Jiang and Storrie, 2005; Martinez et al., vesicles and neuronal cell specific Golgi tranport,Golgi stress response (a′) endosome to 1994; Del Nery et al., 2006; Opdam et al., Golgi transport; (c) multi-drug resistance regulation 2000; Shan et al., 2000 (9) Rab5, Rab17, Rab20, Rab21, Rab22a/Rab31, Rab24 Rab5a,b,c Clathrin coated vesicles, caveosomes, Endocytosis, early endosome fusion, caveolar vesicle Pelkmans et al., 2004; Barbieri et al., 2000; and early endosomes. targeting to early endosomes; (a) EGF receptor Arnett et al., 2004; Bucci et al., 1995 activation; (b) neuroprotection Rab17 Epithelial specific; apical recycling Transport through apical recycling endosomes; Zacchi et al., 1998 endosome polarized sorting Rab20 Epithelial specific; kidney