Nuts and bolts of the salt-inducible kinases (SIKs).
AMPK-related kinase
CREB
CREB-regulated transcriptional co-activator (CRTC)
histone deacetylase (HDAC)
myocyte enhancer factor 2 (MEF2)
salt-inducible kinase (SIK)
Journal
The Biochemical journal
ISSN: 1470-8728
Titre abrégé: Biochem J
Pays: England
ID NLM: 2984726R
Informations de publication
Date de publication:
16 04 2021
16 04 2021
Historique:
received:
01
03
2021
revised:
29
03
2021
accepted:
31
03
2021
entrez:
16
4
2021
pubmed:
17
4
2021
medline:
14
9
2021
Statut:
ppublish
Résumé
The salt-inducible kinases, SIK1, SIK2 and SIK3, most closely resemble the AMP-activated protein kinase (AMPK) and other AMPK-related kinases, and like these family members they require phosphorylation by LKB1 to be catalytically active. However, unlike other AMPK-related kinases they are phosphorylated by cyclic AMP-dependent protein kinase (PKA), which promotes their binding to 14-3-3 proteins and inactivation. The most well-established substrates of the SIKs are the CREB-regulated transcriptional co-activators (CRTCs), and the Class 2a histone deacetylases (HDAC4/5/7/9). Phosphorylation by SIKs promotes the translocation of CRTCs and Class 2a HDACs to the cytoplasm and their binding to 14-3-3s, preventing them from regulating their nuclear binding partners, the transcription factors CREB and MEF2. This process is reversed by PKA-dependent inactivation of the SIKs leading to dephosphorylation of CRTCs and Class 2a HDACs and their re-entry into the nucleus. Through the reversible regulation of these substrates and others that have not yet been identified, the SIKs regulate many physiological processes ranging from innate immunity, circadian rhythms and bone formation, to skin pigmentation and metabolism. This review summarises current knowledge of the SIKs and the evidence underpinning these findings, and discusses the therapeutic potential of SIK inhibitors for the treatment of disease.
Identifiants
pubmed: 33861845
pii: 228393
doi: 10.1042/BCJ20200502
pmc: PMC8057676
doi:
Substances chimiques
Protein Kinase Inhibitors
0
Protein Serine-Threonine Kinases
EC 2.7.11.1
SIK1 protein, human
EC 2.7.11.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
1377-1397Subventions
Organisme : Medical Research Council
ID : MR/R021406/1
Pays : United Kingdom
Informations de copyright
© 2021 The Author(s).
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