Protein kinase C: release from quarantine by mTORC2.
Trends Biochem Sci
; 47(6): 518-530, 2022 06.
Article
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| MEDLINE
| ID: mdl-35361526
ABSTRACT
Protein kinase C (PKC) isozymes are maintained in a 'ready-to-go' but 'safe' autoinhibited conformation until second messenger binding unleashes an autoinhibitory pseudosubstrate to allow substrate phosphorylation. However, to gain this 'ready-to-go' conformation, PKC must be processed by a series of complex priming phosphorylations, the mechanism of which was enigmatic until now. Recent findings snapped the pieces of the phosphorylation puzzle into place to unveil a process that involves a newly described motif (TOR interaction motif, TIM), a well-described kinase [mechanistic target of rapamycin complex 2 (mTORC2)], and an often-used mechanism (autophosphorylation) to prime PKC to signal. This review highlights new insights into how phosphorylation controls PKC and discusses them in the context of common mechanisms for AGC kinase regulation by phosphorylation and autophosphorylation.
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1
Bases de datos:
MEDLINE
Asunto principal:
Proteína Quinasa C
/
Cuarentena
Idioma:
En
Revista:
Trends Biochem Sci
Año:
2022
Tipo del documento:
Article
País de afiliación:
Estados Unidos