BIROn - Birkbeck Institutional Research Online

    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 , ISSN 0021-9533. (In Press)

    [img] Text
    jcs.223743.full(1).pdf - Author's Accepted Manuscript
    Restricted to Repository staff only

    Download (5MB) | Request a copy
    [img]
    Preview
    Text
    26969a.pdf - Published Version of Record
    Available under License Creative Commons Attribution.

    Download (9MB) | Preview

    Abstract

    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

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): Cdc42, FARP, Atypical protein kinase C, Polarity
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Neil Mcdonald
    Date Deposited: 29 Mar 2019 14:48
    Last Modified: 09 Oct 2019 18:38
    URI: http://eprints.bbk.ac.uk/id/eprint/26969

    Statistics

    Downloads
    Activity Overview
    12Downloads
    31Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item