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J Cell Sci ; 132(8)2019 04 25.
Artigo em Inglês | MEDLINE | ID: mdl-30872454

RESUMO

The elaboration of polarity is central to organismal development and to the maintenance of functional epithelia. Among the controls determining polarity are the PAR proteins, PAR6, aPKCι and PAR3, regulating both known and unknown effectors. Here, we identify FARP2 as a 'RIPR' motif-dependent partner and substrate of aPKCι that is required for efficient polarisation and junction formation. Binding is conferred by a FERM/FA domain-kinase domain interaction and detachment promoted by aPKCι-dependent phosphorylation. FARP2 is shown to promote GTP loading of Cdc42, which is consistent with it being involved in upstream regulation of the polarising PAR6-aPKCι complex. However, we show that aPKCι acts to promote the localised activity of FARP2 through phosphorylation. We conclude that this aPKCι-FARP2 complex formation acts as a positive feedback control to drive polarisation through aPKCι and other Cdc42 effectors.This article has an associated First Person interview with the first author of the paper.


Assuntos
Células Epiteliais/citologia , Fatores de Troca do Nucleotídeo Guanina/metabolismo , Proteína Quinase C/metabolismo , Junções Íntimas/metabolismo , Proteína cdc42 de Ligação ao GTP/metabolismo , Células CACO-2 , Polaridade Celular , Fatores de Troca do Nucleotídeo Guanina/genética , Células HCT116 , Humanos , Fosforilação
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