Olfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1.

Hdl Handle:
http://hdl.handle.net/10147/127203
Title:
Olfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1.
Authors:
Dooley, Ruth; Baumgart, Sabrina; Rasche, Sebastian; Hatt, Hanns; Neuhaus, Eva M
Affiliation:
Molecular Medicine Lab RCSI, Beaumont Hospital, Dublin, Republic of Ireland.
Citation:
Olfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1. 2009, 276 (24):7279-90 FEBS J.
Journal:
The FEBS journal
Issue Date:
Dec-2009
URI:
http://hdl.handle.net/10147/127203
DOI:
10.1111/j.1742-4658.2009.07435.x
PubMed ID:
19909339
Abstract:
The unique ability of mammals to detect and discriminate between thousands of different odorant molecules is governed by the diverse array of olfactory receptors expressed by olfactory sensory neurons in the nasal epithelium. Olfactory receptors consist of seven transmembrane domain G protein-coupled receptors and comprise the largest gene superfamily in the mammalian genome. We found that approximately 30% of olfactory receptors possess a classical post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) domain binding motif in their C-termini. PDZ domains have been established as sites for protein-protein interaction and play a central role in organizing diverse cell signaling assemblies. In the present study, we show that multi-PDZ domain protein 1 (MUPP1) is expressed in the apical compartment of olfactory sensory neurons. Furthermore, on heterologous co-expression with olfactory sensory neurons, MUPP1 was shown to translocate to the plasma membrane. We found direct interaction of PDZ domains 1 + 2 of MUPP1 with the C-terminus of olfactory receptors in vitro. Moreover, the odorant-elicited calcium response of OR2AG1 showed a prolonged decay in MUPP1 small interfering RNA-treated cells. We have therefore elucidated the first building blocks of the putative 'olfactosome', brought together by the scaffolding protein MUPP1, a possible central nucleator of the olfactory response.
Item Type:
Article
Language:
en
MeSH:
Animals; Calcium Signaling; Carrier Proteins; Humans; Mice; Olfactory Receptor Neurons; PDZ Domains; Protein Transport; Receptors, Odorant; Signal Transduction
ISSN:
1742-4658

Full metadata record

DC FieldValue Language
dc.contributor.authorDooley, Ruthen
dc.contributor.authorBaumgart, Sabrinaen
dc.contributor.authorRasche, Sebastianen
dc.contributor.authorHatt, Hannsen
dc.contributor.authorNeuhaus, Eva Men
dc.date.accessioned2011-04-05T14:31:58Z-
dc.date.available2011-04-05T14:31:58Z-
dc.date.issued2009-12-
dc.identifier.citationOlfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1. 2009, 276 (24):7279-90 FEBS J.en
dc.identifier.issn1742-4658-
dc.identifier.pmid19909339-
dc.identifier.doi10.1111/j.1742-4658.2009.07435.x-
dc.identifier.urihttp://hdl.handle.net/10147/127203-
dc.description.abstractThe unique ability of mammals to detect and discriminate between thousands of different odorant molecules is governed by the diverse array of olfactory receptors expressed by olfactory sensory neurons in the nasal epithelium. Olfactory receptors consist of seven transmembrane domain G protein-coupled receptors and comprise the largest gene superfamily in the mammalian genome. We found that approximately 30% of olfactory receptors possess a classical post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) domain binding motif in their C-termini. PDZ domains have been established as sites for protein-protein interaction and play a central role in organizing diverse cell signaling assemblies. In the present study, we show that multi-PDZ domain protein 1 (MUPP1) is expressed in the apical compartment of olfactory sensory neurons. Furthermore, on heterologous co-expression with olfactory sensory neurons, MUPP1 was shown to translocate to the plasma membrane. We found direct interaction of PDZ domains 1 + 2 of MUPP1 with the C-terminus of olfactory receptors in vitro. Moreover, the odorant-elicited calcium response of OR2AG1 showed a prolonged decay in MUPP1 small interfering RNA-treated cells. We have therefore elucidated the first building blocks of the putative 'olfactosome', brought together by the scaffolding protein MUPP1, a possible central nucleator of the olfactory response.-
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshCalcium Signaling-
dc.subject.meshCarrier Proteins-
dc.subject.meshHumans-
dc.subject.meshMice-
dc.subject.meshOlfactory Receptor Neurons-
dc.subject.meshPDZ Domains-
dc.subject.meshProtein Transport-
dc.subject.meshReceptors, Odorant-
dc.subject.meshSignal Transduction-
dc.titleOlfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1.en
dc.typeArticleen
dc.contributor.departmentMolecular Medicine Lab RCSI, Beaumont Hospital, Dublin, Republic of Ireland.en
dc.identifier.journalThe FEBS journalen
dc.description.provinceLeinster-

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