Gene Symbol: YBT1
Description: bile acid-transporting ATPase YBT1
Alias: BAT1, bile acid-transporting ATPase YBT1
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Ortiz D, St Pierre M, Abdulmessih A, Arias I. A yeast ATP-binding cassette-type protein mediating ATP-dependent bile acid transport. J Biol Chem. 1997;272:15358-65 pubmed
    ..The BAT1 (bile acid transporter) gene was isolated from yeast DNA by polymerase chain reaction amplification using ..
  2. Gulshan K, Moye Rowley W. Vacuolar import of phosphatidylcholine requires the ATP-binding cassette transporter Ybt1. Traffic. 2011;12:1257-68 pubmed publisher
    ..are found on the limiting membrane of the yeast vacuole and loss of one of these vacuolar ABC transporters, Ybt1, caused a major defect in the normal delivery of the phosphatidylcholine (PC) analog NBD-PC (7-nitro-2,1,3-..
  3. Sharma K, Kaur R, Bachhawat A. The glutathione-mediated detoxification pathway in yeast: an analysis using the red pigment that accumulates in certain adenine biosynthetic mutants of yeasts reveals the involvement of novel genes. Arch Microbiol. 2003;180:108-17 pubmed
    ..By contrast, two other previously characterized genes, the oxidative stress transcription factor gene, SKN7, and the yeast caesin protein kinase gene, YCK1, of S. cerevisiae do participate in this pathway. ..
  4. Dosil M. Ribosome synthesis-unrelated functions of the preribosomal factor Rrp12 in cell cycle progression and the DNA damage response. Mol Cell Biol. 2011;31:2422-38 pubmed publisher
    ..I propose that the functional duality of Rrp12 may couple the control of ribosome production to the regulation of other cellular processes during cell cycle progression. ..
  5. Sasser T, Padolina M, Fratti R. The yeast vacuolar ABC transporter Ybt1p regulates membrane fusion through Ca2+ transport modulation. Biochem J. 2012;448:365-72 pubmed publisher
    ..In the present study we found that deletion of YBT1 enhanced in vitro homotypic vacuole fusion by up to 50% relative to wild-type vacuoles...