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A Comprehensive View of the ?-Arrestinome
#MMPMID28321204
Crépieux P
; Poupon A
; Langonné-Gallay N
; Reiter E
; Delgado J
; Schaefer MH
; Bourquard T
; Serrano L
; Kiel C
Front Endocrinol (Lausanne)
2017[]; 8
(?): 32
PMID28321204
show ga
G protein-coupled receptors (GPCRs) are membrane receptors critically involved in
sensing the environment and orchestrating physiological processes. As such, they
transduce extracellular signals such as hormone, neurotransmitters, ions, and
light into an integrated cell response. The intracellular trafficking,
internalization, and signaling ability of ligand-activated GPCRs are controlled
by arrestins, adaptor proteins that they interact with upon ligand binding.
?-arrestins 1 and 2 in particular are now considered as hub proteins assembling
multiprotein complexes to regulate receptor fate and transduce diversified cell
responses. While more than 400 ?-arrestin interaction partners have been
identified so far, much remains to be learnt on how discrimination between so
many binding partners is accomplished. Here, we gathered the interacting partners
of ?-arrestins through database mining and manual curation of the literature to
map the ?-arrestin interactome (?-arrestinome). We discussed several parameters
that determine compatible (AND) or mutually exclusive (XOR) binding of ?-arrestin
interactors, such as structural constraints, intracellular abundance, or binding
affinity.
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