Targeted disruption of PKC from AKAP signaling complexes.
Journal
RSC chemical biology
ISSN: 2633-0679
Titre abrégé: RSC Chem Biol
Pays: England
ID NLM: 101768727
Informations de publication
Date de publication:
05 Aug 2021
05 Aug 2021
Historique:
received:
12
05
2021
accepted:
16
07
2021
entrez:
30
8
2021
pubmed:
31
8
2021
medline:
31
8
2021
Statut:
epublish
Résumé
Protein Kinase C (PKC) is a member of the AGC subfamily of kinases and regulates a wide array of signaling pathways and physiological processes. Protein-protein interactions involving PKC and its scaffolding partners dictate the spatiotemporal dynamics of PKC activity, including its access to activating second messenger molecules and potential substrates. While the A Kinase Anchoring Protein (AKAP) family of scaffold proteins universally bind PKA, several were also found to scaffold PKC, thereby serving to tune its catalytic output. Targeting these scaffolding interactions can further shed light on the effect of subcellular compartmentalization on PKC signaling. Here we report the development of two hydrocarbon stapled peptides, CSTAD5 and CSTAD6, that are cell permeable and bind PKC to disrupt PKC
Identifiants
pubmed: 34458835
doi: 10.1039/d1cb00106j
pii: d1cb00106j
pmc: PMC8341804
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1227-1231Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM134168
Pays : United States
Informations de copyright
This journal is © The Royal Society of Chemistry.
Déclaration de conflit d'intérêts
There are no conflicts to declare.
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