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First published online 5 October 2004
doi: 10.1242/jcs.01379

Journal of Cell Science 117, 5367-5379 (2004)
Published by The Company of Biologists 2004
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Research Article

New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4(a) receptor splice variant: roles in receptor targeting

Lara Joubert1, Brendon Hanson2, Gaël Barthet1, Michèle Sebben1, Sylvie Claeysen1, Wanjin Hong2, Philippe Marin1, Aline Dumuis1 and Joël Bockaert1,*

1 Laboratoire de Génomique Fonctionnelle, CNRS UPR2580, CCIPE, 141 rue de la Cardonille, 34094 Montpellier CEDEX 05, France
2 Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Rep. of Singapore

* Author for correspondence (e-mail: joel.bockaert{at}ccipe.cnrs.fr)

Accepted 24 June 2004

The 5-hydroxytryptamine type 4 receptor (5-HT4R) is involved in learning, feeding, respiratory control and gastrointestinal transit. This receptor is one of the G-protein-coupled receptors for which alternative mRNA splicing generates the most variants that differ in their C-terminal extremities. Some 5-HT4R variants (a, e and f) express canonical PDZ ligands at their C-termini. Here, we have examined whether some mouse 5-HT4R variants associate with specific sets of proteins, using a proteomic approach based on peptide-affinity chromatography, two-dimensional electrophoresis and mass spectrometry. We have identified ten proteins that interact specifically with the 5-HT4(a)R and three that only associate with the 5-HT4(e)R. Most of them are PDZ proteins. Among the proteins that associated specifically with the 5-HT4(a)R variant, NHERF greatly modified its subcellular localization. Moreover, NHERF recruited the 5-HT4(a)R to microvilli, where it localized with activated ezrin, consistent with the role of 5-HT4(a)R in cytoskeleton remodelling. The 5-HT4(a)R also interacted with both the constitutive and inducible (upon methamphetamine treatment) forms of the recently cloned sorting nexin 27 (SNX27a and b, respectively). We found that SNX27a redirected part of 5-HT4(a)R to early endosomes. The interaction of the 5-HT4R splice variants with distinct sets of PDZ proteins might specify their cellular localization as well as their signal transduction properties.

Key words: 5-HT4 Receptor splice variants, PDZ domains, Proteomics, NHERF, Sorting nexin




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