Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs.
Biochem J
; 479(1): 1-22, 2022 01 14.
Article
en En
| MEDLINE
| ID: mdl-34989786
ABSTRACT
Cellular function is based on protein-protein interactions. A large proportion of these interactions involves the binding of short linear motifs (SLiMs) by folded globular domains. These interactions are regulated by post-translational modifications, such as phosphorylation, that create and break motif binding sites or tune the affinity of the interactions. In addition, motif-based interactions are involved in targeting serine/threonine kinases and phosphatases to their substrate and contribute to the specificity of the enzymatic actions regulating which sites are phosphorylated. Here, we review how SLiM-based interactions assist in determining the specificity of serine/threonine kinases and phosphatases, and how phosphorylation, in turn, affects motif-based interactions. We provide examples of SLiM-based interactions that are turned on/off, or are tuned by serine/threonine phosphorylation and exemplify how this affects SLiM-based protein complex formation.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Serina
/
Treonina
/
Dominios y Motivos de Interacción de Proteínas
Límite:
Humans
Idioma:
En
Revista:
Biochem J
Año:
2022
Tipo del documento:
Article
País de afiliación:
Suecia