Activity of the Kluyveromyces lactis Pdr5 multidrug transporter is modulated by the Sit4 protein phosphatase.

ABSTRACT: A possible role for posttranslational modifications in regulating the activity of ATP-binding cassette (ABC) transporters has not been well established. In this study, the drug efflux ABC transporter gene KlPDR5 was isolated from the budding yeast Kluyveromyces lactis, and it was found that the encoded KlPdr5 drug pump is posttranslationally regulated by the type 2A-related Ser/Thr protein phosphatase, Sit4p. The KlPdr5 transporter is a protein of 1,525 amino acids sharing 63.8% sequence identity with its Saccharomyces cerevisiae counterpart, ScPdr5p. Overexpression of the KlPDR5 gene confers resistance to oligomycin, antimycin, econazole, and ketoconazole, whereas cells with a disrupted allele of KlPDR5 are hypersensitive to the drugs and have a decreased capacity to carry out efflux of t

SUBMITTER: Chen XJ 

PROVIDER: S-EPMC95276 | biostudies-literature | 2001 Jul

REPOSITORIES: biostudies-literature