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2013 ; 118
(ä): 57-92
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Structural determinants of arrestin functions
#MMPMID23764050
Gurevich VV
; Gurevich EV
Prog Mol Biol Transl Sci
2013[]; 118
(ä): 57-92
PMID23764050
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Arrestins are a small protein family with only four members in mammals. Arrestins
demonstrate an amazing versatility, interacting with hundreds of different G
protein-coupled receptor (GPCR) subtypes, numerous nonreceptor signaling
proteins, and components of the internalization machinery, as well as
cytoskeletal elements, including regular microtubules and centrosomes. Here, we
focus on the structural determinants that mediate various arrestin functions. The
receptor-binding elements in arrestins were mapped fairly comprehensively, which
set the stage for the construction of mutants targeting particular GPCRs. The
elements engaged by other binding partners are only now being elucidated and in
most cases we have more questions than answers. Interestingly, even very limited
and imprecise identification of structural requirements for the interaction with
very few other proteins has enabled the development of signaling-biased arrestin
mutants. More comprehensive understanding of the structural underpinning of
different arrestin functions will pave the way for the construction of arrestins
that can link the receptor we want to the signaling pathway of our choosing.
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