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    The Rho-family GEF FARP2 is activated by aPKCiota to control polarity and tight junction formation.

    Elbediwy, A. and Zhang, Y. and Cobbaut, M. and Riou, P. and Tan, R.S. and Roberts, S.K. and Tynan, C. and George, R. and Kjaer, S. and Martin-Fernandez, M.L. and Thompson, B.J. and McDonald, Neil Q. and Parker, P.J. (2019) The Rho-family GEF FARP2 is activated by aPKCiota to control polarity and tight junction formation. Journal of Cell Science 132 (8), jcs223743. ISSN 0021-9533.

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    The elaboration of polarity is central to organismal development and to the maintenance of functional epithelia. Amongst the controls determining polarity are the PAR proteins, PAR6/aPKCiota-PAR3, regulating both known and unknown effectors. Here we identify FARP2 as a "RIPR" motif dependent partner and substrate of aPKCiota that is required for efficient polarisation and junction formation. Binding is conferred by a FERM/FA domain-Kinase domain interaction and detachment promoted by aPKCiota dependent phosphorylation. FARP2 is shown to promote GTP loading of Cdc42 consistent with upstream regulation of the polarising PAR6-aPKCiota complex. However, it is shown that aPKCiota acts to promote the localised activity of FARP2 through phosphorylation. We conclude that this aPKCiota FARP2 complex formation acts as a positive feedback control to drive polarisation through aPKCiota and other Cdc42 effectors. Ahmed , Yixiao , Mathias , Philippe , Ray S. , Selene K. Roberts, Chris Tynan, Roger George, Svend Kjaer, Marisa L. Martin-Fernandez, Barry J. Thompson, Neil Q. McDonald, Peter J. Parker


    Item Type: Article
    Keyword(s) / Subject(s): Cdc42, FARP, Atypical protein kinase C, Polarity
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Neil Mcdonald
    Date Deposited: 29 Mar 2019 14:48
    Last Modified: 02 Aug 2023 17:50


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