Solo vs. Chorus: Monomers and Oligomers of Arrestin Proteins

Three out of four subtypes of arrestin proteins expressed in mammals self-associate, each forming oligomers of a distinct kind. Monomers and oligomers have different subcellular localization and distinct biological functions. Here we summarize existing evidence regarding arrestin oligomerization and...

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Bibliographic Details
Published in:International journal of molecular sciences 2022-06, Vol.23 (13), p.7253
Main Authors: Gurevich, Vsevolod V, Gurevich, Eugenia V
Format: Article
Language:English
Subjects:
Adrenergic receptors
Animals
Arrestin
Arrestin - genetics
Arrestin - metabolism
Arrestins - metabolism
beta-Arrestins - metabolism
conformation
Cytotoxicity
Equilibrium
Homology
Kinases
Light
Localization
Mammals - metabolism
Mutation
Oligomerization
Phosphorylation
Photoreceptors
Proteins
Review
signaling
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Summary:Three out of four subtypes of arrestin proteins expressed in mammals self-associate, each forming oligomers of a distinct kind. Monomers and oligomers have different subcellular localization and distinct biological functions. Here we summarize existing evidence regarding arrestin oligomerization and discuss specific functions of monomeric and oligomeric forms, although too few of the latter are known. The data on arrestins highlight biological importance of oligomerization of signaling proteins. Distinct modes of oligomerization might be an important contributing factor to the functional differences among highly homologous members of the arrestin protein family.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms23137253