DRS2/YAL026C Literature Guide Help

Other names published for DRS2: FUN38, SWA3, aminophospholipid-translocating P4-type ATPase DRS2, YAL026C

DRS2 - Function/Process (23)

ReferenceOther Genes Addressed
Stone A, et al.  (2012) Biochemical characterization of P4-ATPase mutations identified in patients with progressive familial intrahepatic cholestasis. J Biol Chem 287(49):41139-51
Anand VC, et al.  (2009) Genome-wide analysis of AP-3-dependent protein transport in yeast. Mol Biol Cell 20(5):1592-604
Natarajan P, et al.  (2009) Regulation of a Golgi flippase by phosphoinositides and an ArfGEF. Nat Cell Biol 11(12):1421-6
Zhou X and Graham TR  (2009) Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast. Proc Natl Acad Sci U S A 106(39):16586-91
Fei W, et al.  (2008) Genome-wide analysis of sterol-lipid storage and trafficking in Saccharomyces cerevisiae. Eukaryot Cell 7(2):401-14
Liu K, et al.  (2008) P4-ATPase Requirement for AP-1/Clathrin Function in Protein Transport from the trans-Golgi Network and Early Endosomes. Mol Biol Cell 19(8):3526-35
Stevens HC, et al.  (2008) The Putative Aminophospholipid Translocases, DNF1 and DNF2, Are Not Required for 7-Nitrobenz-2-oxa-1,3-diazol-4-yl-phosphatidylserine Flip across the Plasma Membrane of Saccharomyces cerevisiae. J Biol Chem 283(50):35060-9
Alder-Baerens N, et al.  (2006) Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol Biol Cell 17(4):1632-42
Chen S, et al.  (2006) Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane. Traffic 7(11):1503-17
Reiner S, et al.  (2006) A genomewide screen reveals a role of mitochondria in anaerobic uptake of sterols in yeast. Mol Biol Cell 17(1):90-103
Samanta MP, et al.  (2006) Global identification of noncoding RNAs in Saccharomyces cerevisiae by modulating an essential RNA processing pathway. Proc Natl Acad Sci U S A 103(11):4192-7
Sciorra VA, et al.  (2005) Synthetic genetic array analysis of the PtdIns 4-kinase Pik1p identifies components in a Golgi-specific Ypt31/rab-GTPase signaling pathway. Mol Biol Cell 16(2):776-93
Chantalat S, et al.  (2004) The Arf activator Gea2p and the P-type ATPase Drs2p interact at the Golgi in Saccharomyces cerevisiae. J Cell Sci 117(Pt 5):711-22
Natarajan P, et al.  (2004) Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function. Proc Natl Acad Sci U S A 101(29):10614-9
Saito K, et al.  (2004) Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae. Mol Biol Cell 15(7):3418-32
Enyenihi AH and Saunders WS  (2003) Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163(1):47-54
Pomorski T, et al.  (2003) Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis. Mol Biol Cell 14(3):1240-54
Gall WE, et al.  (2002) Drs2p-dependent formation of exocytic clathrin-coated vesicles in vivo. Curr Biol 12(18):1623-7
Hua Z, et al.  (2002) An essential subfamily of Drs2p-related P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system. Mol Biol Cell 13(9):3162-77
Chen CY, et al.  (1999) Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function. J Cell Biol 147(6):1223-36
Marx U, et al.  (1999) Rapid transbilayer movement of fluorescent phospholipid analogues in the plasma membrane of endocytosis-deficient yeast cells does not require the Drs2 protein. Eur J Biochem 263(1):254-63
Siegmund A, et al.  (1998) Loss of Drs2p does not abolish transfer of fluorescence-labeled phospholipids across the plasma membrane of Saccharomyces cerevisiae. J Biol Chem 273(51):34399-405
Tang X, et al.  (1996) A subfamily of P-type ATPases with aminophospholipid transporting activity. Science 272(5267):1495-7