A novel mechanism of P-type ATPase autoinhibition involving both termini of the protein

Kira Ekberg, Michael Palmgren, Bjarke Veierskov, Morten Jeppe Buch-Pedersen

    42 Citations (Scopus)

    Abstract

    The activity of many P-type ATPases is found to be regulated by interacting proteins or autoinhibitory elements located in N- or C-terminal extensions. An extended C terminus of fungal and plant P-type plasma membrane H+-ATPases has long been recognized to be part of a regulatory apparatus involving an autoinhibitory domain. Here we demonstrate that both the N and the C termini of the plant plasma membrane H+-ATPase are directly involved in controlling the pump activity state and that N-terminal displacements are coupled to secondary modifications taking place at the C-terminal end. This identifies the first group of P-type ATPases for which both ends of the polypeptide chain constitute regulatory domains, which together contribute to the autoinhibitory apparatus. This suggests an intricate mechanism of cis-regulation with both termini of the protein communicating to obtain the necessary control of the enzyme activity state.
    Original languageEnglish
    JournalJournal of Biological Chemistry
    Volume285
    Issue number10
    Pages (from-to)7344-7350
    Number of pages7
    ISSN0021-9258
    DOIs
    Publication statusPublished - 5 Mar 2010

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