OLF-STOM

Stomatin proteins and olfactory transduction

 Coordinatore SCUOLA INTERNAZIONALE SUPERIORE DI STUDI AVANZATI 

 Organization address address: VIA BONOMEA 265
city: TRIESTE
postcode: 34136

contact info
Titolo: Mr.
Nome: Gabriele
Cognome: Rizzetto
Email: send email
Telefono: +39 040 3787201

 Nazionalità Coordinatore Italy [IT]
 Totale costo 75˙000 €
 EC contributo 75˙000 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-2012-CIG
 Funding Scheme MC-CIG
 Anno di inizio 2013
 Periodo (anno-mese-giorno) 2013-03-01   -   2016-02-29

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    SCUOLA INTERNAZIONALE SUPERIORE DI STUDI AVANZATI

 Organization address address: VIA BONOMEA 265
city: TRIESTE
postcode: 34136

contact info
Titolo: Mr.
Nome: Gabriele
Cognome: Rizzetto
Email: send email
Telefono: +39 040 3787201

IT (TRIESTE) coordinator 75˙000.00

Mappa


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ion    cilia    osns    proteins    olfactory    stoml    mechanisms    physiological    transduction    sensory    domain    mice    stomatin    protein    clarify    neurons    signal    electrophysiological    odorant   

 Obiettivo del progetto (Objective)

'In vertebrate the initial steps of olfaction occur in olfactory sensory neurons (OSNs), located in the olfactory epithelium in the nasal cavity. OSNs are responsible for the detection of odorant molecules present in the environment and the generation of the neural signal that is transmitted to the brain. OSNs are bipolar neurons with a single dendrite that terminates with a knob, from which protrude several tiny cilia, where the transduction of the olfactory signal takes place. Data obtained from different approaches have shown that several stomatin-proteins (stomatin, STOML-2, STOML-3) are highly expressed by OSNs and are localized on the cilia of OSNs. Proteins of the stomatin family are membrane-associated proteins characterized by the presence of a structurally conserved core domain called stomatin-domain of about 120 residues. They can form oligomers and can modulate ion channel activity, although the precise mechanisms of this regulation are still unclear. Here we will clarify the physiological role of stomatin-proteins in the olfactory system by using different knock-out mouse line for stomatin-proteins genes. We will examine if the lack of stomatin-protein alters the development of the olfactory system and in particular the sensory transduction apparatus. We will evaluate the olfactory sensitivity by using electrophysiological recording of odorant-evoked response by OSNs in the absence of stomatin-proteins and we will test the odorant-driven behaviors in null mice. Moreover, we will analyze the electrophysiological properties of transduction ion channels in mutant mice to test a direct modulation by stomatin-proteins. We will not only contribute to increase the understanding of olfactory transduction at the molecular level, but we will also identify possible new mechanisms of stomatin-protein function useful to clarify the physiological role of these proteins in other cellular systems.'

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