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

Organisation/Company: Università degli studi di Bari
Research Field: Biological sciences
Researcher Profile: Recognised Researcher (R2), Leading Researcher (R4), First Stage Researcher (R1), Established Researcher (R3)
Country: Italy
Application Deadline: 15 Jan 2025 - 23:59 (UTC)
Type of Contract: To be defined
Job Status: Not Applicable
Is the job funded through the EU Research Framework Programme?
Not funded by a EU programme
Is the Job related to staff position within a Research Infrastructure?
No
Offer 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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