How Human Cells Form And Deliver The Redox Cofactor Fad In Health And Diseases Lazio

How Human Cells Form And Deliver The Redox Cofactor Fad In Health And Diseases
Roma
Lazio, Lazio

Organisation/Company: Università degli studi di BariResearch Field: Biological sciencesResearcher Profile: Recognised Researcher (R2), Leading Researcher (R4), First Stage Researcher (R1), Established Researcher (R3)Country: ItalyApplication Deadline: 15 Jan 2025 - 23:59 (UTC)Type of Contract: To be definedJob Status: Not ApplicableIs the job funded through the EU Research Framework Programme?

Not funded by a EU programmeIs the Job related to staff position within a Research Infrastructure?

NoOffer DescriptionThis project deals with investigations on the alterations of FAD synthase (FADS), the last enzyme in FAD biosynthesis, coded by the FLAD1 gene, whose mutations are causative of a mitochondria-affecting neuro-muscular derangement, named LSMFLAD.

Therapeutic strategies are needed to treat severe LSMFLAD phenotype.

Additionally, increased expression of FLAD1 has been associated with different kinds of tumors, thus prompting research on FADS. To date, three different protein isoforms, generated by FLAD1 alternative splicing, have been characterized: isoform 1, which is destined to mitochondria; isoform 2, localized in the cytosol; and a shortest isoform, an emergency protein crucial for LSMFLAD patients' survival.

The latter enzyme, a single domain protein, is responsible for FAD synthesis; isoforms 1 and 2 consist of two principal domains and a smaller interdomain region involved in protein dimerization.

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