title: Rab GTPases-cargo direct interactions: fine modulators of intracellular trafficking.
abstract: Rab proteins are a large family of monomeric GTPases that comprise about 70 members. These proteins cycle from a GDP-bound to a GTP-bound state and are considered molecular switches of membrane traffic. Indeed, they control several steps of vesicular trafficking such as vesicle formation, vesicle movement on actin and tubulin cytoskeletal tracks, vesicle tethering, docking and fusion to the target compartment. Accordingly, Rab proteins are considered key factors in vesicular trafficking as they have a fundamental role in specifying identity and routing of vesicles and organelles. Given their role in membrane traffic, it is not surprising that Rab proteins control the cellular fate of several membrane molecules such as signal transduction receptors and ion channels, being thus fundamental for their correct function. However, much evidence of interaction of a number of Rab proteins with cargo has been reported, raising the question of the functional meaning of these interactions. Indeed, Rab proteins have been demonstrated to directly interact with several membrane proteins, such as signaling receptors, immunoglobulin receptors, integrins and ion channels. Growing evidence indicates that, through interactions with Rab proteins, cargos directly control their own fate. Furthermore, often a cargo protein has the ability to interact with more than one Rab and/or with the same Rab in different activation states. This review focuses on these interactions highlighting their role in modulating cargo's trafficking and functions.
authors.affiliation: Department of Biological and Environmental Sciences and Technologies (DiSTeBA), Università del Salento, Lecce, Italy.
authors.forename: Anna Laura
authors.initials: AL
authors.lastname: Aloisi
authors.forename: Cecilia
authors.initials: C
authors.lastname: Bucci
mesh_terms: D000818:Animals; D002465:Cell Movement; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism; D011992:Endosomes / Q000378:metabolism; D051157:Frizzled Receptors / Q000378:metabolism; D057809:HEK293 Cells; D006801:Humans; D007136:Immunoglobulins / Q000378:metabolism; D016023:Integrins / Q000378:metabolism; D008247:Lysosomes / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D011485:Protein Binding; D020033:Protein Isoforms / Q000378:metabolism; D021381:Protein Transport; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism; D044006:Receptors, Epoprostenol / Q000378:metabolism; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism; D023062:Receptors, Interleukin-8A / Q000378:metabolism; D023063:Receptors, Interleukin-8B / Q000378:metabolism; D044244:Receptors, Thromboxane A2, Prostaglandin H2 / Q000378:metabolism; D015398:Signal Transduction; D020691:rab GTP-Binding Proteins / Q000378:metabolism*
chemical_list: C505032:CFTR protein, human; D051157:Frizzled Receptors; D007136:Immunoglobulins; D016023:Integrins; D008565:Membrane Proteins; D020033:Protein Isoforms; D044006:Receptors, Epoprostenol; D043562:Receptors, G-Protein-Coupled; D023062:Receptors, Interleukin-8A; D023063:Receptors, Interleukin-8B; D044244:Receptors, Thromboxane A2, Prostaglandin H2; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D020794:Receptor Protein-Tyrosine Kinases; D020691:rab GTP-Binding Proteins