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Into the fold: advances in understanding aPKC membrane dynamics.
Cobbaut, Mathias; Parker, Peter J; McDonald, Neil Q.
  • Cobbaut M; Signalling and Structural Biology Laboratory, The Francis Crick Institute, NW1 1AT London, U.K.
  • Parker PJ; Protein Phosphorylation Laboratory, The Francis Crick Institute, NW1 1AT London, U.K.
  • McDonald NQ; School of Cancer and Pharmaceutical Sciences, King's College London, London, U.K.
Biochem J ; 480(24): 2037-2044, 2023 12 20.
Article en En | MEDLINE | ID: mdl-38100320
ABSTRACT
Atypical protein kinase Cs (aPKCs) are part of the PKC family of protein kinases and are atypical because they don't respond to the canonical PKC activators diacylglycerol (DAG) and Ca2+. They are central to the organization of polarized cells and are deregulated in several cancers. aPKC recruitment to the plasma membrane compartment is crucial to their encounter with substrates associated with polarizing functions. However, in contrast with other PKCs, the mechanism by which atypical PKCs are recruited there has remained elusive until recently. Here, we bring aPKC into the fold, summarizing recent reports on the direct recruitment of aPKC to membranes, providing insight into seemingly discrepant findings and integrating them with existing literature.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteína Quinasa C Idioma: En Año: 2023 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteína Quinasa C Idioma: En Año: 2023 Tipo del documento: Article