[ABC transporters of pathogenic fungi: recent advances in functional analyses].
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.
Niimi
Masakazu
M
Department of Bioactive Molecules, National Institute of Infectious Diseases, Tokyo, Japan.
Tanabe
Koichi
K
Wada
Shun-ichi
S
Yamazaki
Akiko
A
Uehara
Yoshimasa
Y
Niimi
Kyoko
K
Lamping
Erwin
E
Holmes
Ann R
AR
Monk
Brian C
BC
Cannon
Richard D
RD
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
D018528:ATP-Binding Cassette Transporters; C094693:CDR1 protein, Candida albicans; D005656:Fungal Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D014157:Transcription Factors