Abstract
Fas-activated serine/threonine kinase (FASTK) is a mitochondrial protein, which effectively binds to RNA and known to be a component of cytosolic RNA granules. FASTK is generally activated during Fas-mediated apoptosis by phosphorylating a nuclear RNA-binding protein TIA-1, and thus considered as an effector of apoptosis. A little report is available on the structural and functional aspects of this protein. In this review, we tried to provide comprehensive information on FASTK with a special attention to structure, function and interactions. Structurally, the C-terminal region is consists of two conserved kinase domains named, subdomain-1 and subdomain-2, which is involved in verities of functions and a putative RNA-binding domain (RAP domain). This review covers FASTK gene structure, expression and regulation, interactome and its biological function.
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