Positive regulation of the Candida albicans multidrug efflux pump Cdr1p function by phosphorylation of its N-terminal extension | Zendy

Sarah Tsao | Zendy; Sandra Weber | Zendy; Christine Cameron | Zendy; Dominic Nehme | Zendy; Elaheh Ahmadzadeh | Zendy; Martine Raymond | Zendy

Open Access

Positive regulation of the Candida albicans multidrug efflux pump Cdr1p function by phosphorylation of its N-terminal extension

Author(s) -

Sarah Tsao,

Sandra Weber,

Christine Cameron,

Dominic Nehme,

Elaheh Ahmadzadeh,

Martine Raymond

Publication year - 2016

Publication title -

journal of antimicrobial chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.124

H-Index - 194

eISSN - 1460-2091

pISSN - 0305-7453

DOI - 10.1093/jac/dkw252

Subject(s) - atp binding cassette transporter , efflux , candida albicans , nile red , biology , multiple drug resistance , mutant , microbiology and biotechnology , biochemistry , drug resistance , transporter , gene , physics , quantum mechanics , fluorescence

Overexpression of ATP-binding cassette (ABC) transporters is a frequent cause of multidrug resistance in cancer cells and pathogenic microorganisms. One example is the Cdr1p transporter from the human fungal pathogen Candida albicans that belongs to the pleiotropic drug resistance (PDR) subfamily of ABC transporters found in fungi and plants. Cdr1p is overexpressed in several azole-resistant clinical isolates, causing azole efflux and treatment failure. Cdr1p appears as a doublet band in western blot analyses, suggesting that the protein is post-translationally modified. We investigated whether Cdr1p is phosphorylated and the function of this modification.

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