MOMEFAST

Molecular Mechanisms Employed by the Newly Assigned RNA-binding Protein FASTKD2

Coordinatore	EUROPEAN MOLECULAR BIOLOGY LABORATORY    more  Organization address address: Meyerhofstrasse 1 city: HEIDELBERG postcode: 69117 contact info Titolo: Ms. Nome: Jillian Cognome: Rowe Email: send email Telefono: +49 6221 387 8239 Fax: +49 6221 3878575
Nazionalità Coordinatore	Germany [DE]
Totale costo	161˙968 €
EC contributo	161˙968 €
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-2013-IEF
Funding Scheme	MC-IEF
Anno di inizio	2015
Periodo (anno-mese-giorno)	2015-01-01   -   2016-12-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	EUROPEAN MOLECULAR BIOLOGY LABORATORY  Organization address address: Meyerhofstrasse 1 city: HEIDELBERG postcode: 69117 contact info Titolo: Ms. Nome: Jillian Cognome: Rowe Email: send email Telefono: +49 6221 387 8239 Fax: +49 6221 3878575	DE (HEIDELBERG)	coordinator	161˙968.80

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 Obiettivo del progetto (Objective)

Posttranscriptional gene regulation is an essential process exerted by a multitude of RNA-binding proteins (RBPs) and allows for rapid adaptation of the cellular proteome to environmental perturbations. Previously, only in a limited number of instructive cases, the RNA networks targeted by individual RBPs had been elucidated. The recent proteome-wide unbiased identification of RBPs yielded a comprehensive catalogue of RBPs acting in human cells and has assigned an RNA-binding activity to over 300 orphan proteins, however without revealing their biological function. FASTKD (FAS-activated serine/threonine kinase domain-containing) proteins constitute an entire family of newly assigned RBPs with poorly defined functions and lack classical RNA binding domains. A loss of function mutation within FASTKD2 has been associated with a lethal form of infantile encephalomyopathy. FASTKD2 localizes to mitochondria and appears to regulate mitochondrial homeostasis by entirely undefined mechanisms. To address to which extent and how RNA binding contributes to the evidently vital functions of FASTKD2 I will extensively characterize the FASTKD2-RNA interface. I will determine the regions of FASTKD2 that interact with RNA making use of a novel and unprecedented technique termed RBDmap. The results of this analysis will guide systematic tests of RNA binding mutants of FASTKD2 in RNA interference based complementation assays. To obtain a comprehensive picture of the factors mediating the effects associated with a loss of function of FASTKD2 I will analyze the network of proteins and RNA motifs associating with FASTKD2 at the systems level. The models derived from the obtained data will be validated in cell-based assays. The required interdisciplinary approach is unique and will yield valuable insights into the molecular actions and interconnections of an entirely new type of RNA binding proteins in mitochondrial homeostasis in health and disease.