title: [ABC transporters of pathogenic fungi: recent advances in functional analyses].
abstract: ABC (ATP binding cassette) transporters consist of transmembrane domains which confer specificity, and structurally conserved nucleotide binding domains that contain highly conserved amino acid motifs. They act not only as transporters but also as receptors or channels that use energy generated by ATP hydrolysis. ABC transporters are widely dispersed in nature. They are found in cells ranging from prokaryotes (bacteria) to eukaryotes (including humans) and several are considered to play crucial roles in cellular homeostasis. Defects in ABC transporters in humans are associated with severe diseases such as type 2 diabetes and cystic fibrosis. Some ABC transporters extrude xenobiotics and confer resistance to chemotherapeutics on microbial pathogens and cancer cells. Thus ABC transporters are of considerable medical importance. Structure-function analysis of ABC transporters has begun to elucidate their mechanisms of substrate recognition, the functional regulation of ATP-binding and hydrolysis and to identify intrinsic physiological functions. In pathogenic fungi, ABC transporters contribute to the clinical problem of drug resistance. The application of new technologies to the examination of fungal ABC transporter function is providing new insights into the use of antifungal drugs in medical mycology and contributing to a better understanding of these important membrane proteins.
authors.affiliation: Department of Bioactive Molecules, National Institute of Infectious Diseases, Tokyo, Japan.
authors.forename: Masakazu
authors.initials: M
authors.lastname: Niimi
authors.forename: Koichi
authors.initials: K
authors.lastname: Tanabe
authors.forename: Shun-ichi
authors.initials: S
authors.lastname: Wada
authors.forename: Akiko
authors.initials: A
authors.lastname: Yamazaki
authors.forename: Yoshimasa
authors.initials: Y
authors.lastname: Uehara
authors.forename: Kyoko
authors.initials: K
authors.lastname: Niimi
authors.forename: Erwin
authors.initials: E
authors.lastname: Lamping
authors.forename: Ann R
authors.initials: AR
authors.lastname: Holmes
authors.forename: Brian C
authors.initials: BC
authors.lastname: Monk
authors.forename: Richard D
authors.initials: RD
authors.lastname: Cannon
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000032:analysis / Q000235:genetics / Q000502:physiology*; D002175:Candida / Q000166:cytology; D018432:Drug Resistance, Multiple; D005656:Fungal Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D005658:Fungi / Q000472:pathogenicity*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000378:metabolism; D010766:Phosphorylation; D013379:Substrate Specificity; D014157:Transcription Factors / Q000032:analysis
chemical_list: D018528:ATP-Binding Cassette Transporters; C094693:CDR1 protein, Candida albicans; D005656:Fungal Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D014157:Transcription Factors