Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton and regulate receptor transport

Vidal R.L.; Ramirez O.A.; Sandoval L.; Koenig-Robert, R; couve, a; Hartel, S

Keywords: acid, proteins, neurons, rat, localization, transport, animals, binding, rats, protein, cell, pregnancy, gaba, mice, embryo, receptor, agents, time, interaction, nerve, rna-binding, tissue, hippocampus, female, cytoskeleton, dendrite, drug, tubulin, article, antineoplastic, neurotransmitter, transfection, controlled, fluorescent, animal, green, kinesin, factors, c, study, 4, priority, nonhuman, journal, Receptors,, Rats,, Sprague-Dawley, a, aminobutyric, Cells,, Cultured, Inbred, Mice,, unclassified, BALB, Nocodazole, marlin1

Abstract

The cytoskeleton and cytoskeletal motors play a fundamental role in neurotransmitter receptor trafficking, but proteins that link GABAB receptors (GABABRs) to the cytoskeleton have not been described. We recently identified Marlin-1, a protein that interacts with GABABR1. Here, we explore the association of GABABRs and Marlin-1 to the cytoskeleton using a combination of biochemistry, microscopy and live cell imaging. Our results indicate that Marlin-1 is associated to microtubules and the molecular motor kinesin-I. We demonstrate that a fraction of Marlin-1 is mobile in dendrites of cultured hippocampal neurons and that mobility is microtubule-dependent. We also show that GABABRs interact robustly with kinesin-I and that intracellular membranes containing GABABRs are sensitive to treatments that disrupt a protein complex containing Marlin-1, kinesin-I and tubulin. Finally, we report that a kinesin-I mutant severely impairs receptor transport. We conclude that Marlin-1 and kinesin-1 link GABABRs to the tubulin cytoskeleton in neurons. © 2007 Elsevier Inc. All rights reserved.

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Título según SCOPUS: Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton and regulate receptor transport
Título de la Revista: MOLECULAR AND CELLULAR NEUROSCIENCE
Volumen: 35
Número: 3
Editorial: ACADEMIC PRESS INC ELSEVIER SCIENCE
Fecha de publicación: 2007
Página de inicio: 501
Página final: 512
Idioma: eng
URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-34347214798&partnerID=q2rCbXpz
DOI:

10.1016/j.mcn.2007.04.008

Notas: SCOPUS