title: Novel topography of the Rab11-effector interaction network within a ciliary membrane targeting complex.
abstract: Small GTPases function as universal molecular switches due to the nucleotide dependent conformational changes of their switch regions that allow interacting proteins to discriminate between the active GTP-bound and the inactive GDP-bound states. Guanine nucleotide exchange factors (GEFs) recognize the inactive GDP-bound conformation whereas GTPase activating proteins (GAPs), and the GTPase effectors recognize the active GTP-bound state. Small GTPases are linked to each other through regulatory and effector proteins into functional networks that regulate intracellular membrane traffic through diverse mechanisms that include GEF and GAP cascades, GEF-effector interactions, common effectors and positive feedback loops linking interacting proteins. As more structural and functional information is becoming available, new types of interactions between regulatory proteins, and new mechanisms by which GTPases are networked to control membrane traffic are being revealed. This review will focus on the structure and function of the novel Rab11-FIP3-Rabin8 dual effector complex and its implications for the targeting of sensory receptors to primary cilia, dysfunction of which causes cilia defects underlying human diseases and disorders know as ciliopathies.
authors.affiliation: a Department of Structural Cell Biology ; Max-Planck-Institute of Biochemistry ; Martinsried , Germany.
authors.forename: Melanie
authors.initials: M
authors.lastname: Vetter
authors.affiliation: b Departments of Surgery ; Division of Ophthalmology; University of New Mexico ; Albuquerque , NM USA.
authors.forename: Jing
authors.initials: J
authors.lastname: Wang
authors.affiliation: a Department of Structural Cell Biology ; Max-Planck-Institute of Biochemistry ; Martinsried , Germany.
authors.forename: Esben
authors.initials: E
authors.lastname: Lorentzen
authors.affiliation: b Departments of Surgery ; Division of Ophthalmology; University of New Mexico ; Albuquerque , NM USA.|c Cell Biology and Physiology ; University of New Mexico ; Albuquerque , NM USA.
authors.forename: Dusanka
authors.initials: D
authors.lastname: Deretic
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism*; D002923:Cilia / Q000235:genetics / Q000378:metabolism; D000072661:Ciliopathies / Q000201:enzymology / Q000235:genetics / Q000473:pathology; D000081410:Germinal Center Kinases; D006801:Humans; D051550:I-kappa B Kinase / Q000235:genetics / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000235:genetics / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D020691:rab GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D000099193:rab11 GTP-Binding Proteins
chemical_list: D000081410:Germinal Center Kinases; D051550:I-kappa B Kinase; D009097:Multienzyme Complexes; D017346:Protein Serine-Threonine Kinases; D020691:rab GTP-Binding Proteins; D000099193:rab11 GTP-Binding Proteins; C491731:IKBKG protein, human
keywords: GTPase effectors; Golgi; Rab GTPases; cilium; membrane trafficking