U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    DRS2 aminophospholipid-translocating P4-type ATPase DRS2 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851207, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    TRAPPIII requires Drs2 binding to transport Atg9 vesicles at cold temperatures.

    TRAPPIII requires Drs2 binding to transport Atg9 vesicles at cold temperatures.
    Puig-Tintó M, Pazos I, Betancur L, Hernández AC, Gallego O., Free PMC Article

    10/16/2023
    The P4-ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast.

    The P4-ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast.
    Pazos I, Puig-Tintó M, Betancur L, Cordero J, Jiménez-Menéndez N, Abella M, Hernández AC, Duran AG, Adachi-Fernández E, Belmonte-Mateos C, Sabido-Bozo S, Tosi S, Nezu A, Oliva B, Colombelli J, Graham TR, Yoshimori T, Muñiz M, Hamasaki M, Gallego O., Free PMC Article

    05/8/2023
    The Drs2 PS flippase activity is required to support neo1Delta any1Delta viability.

    The PQ-loop protein Any1 segregates Drs2 and Neo1 functions required for viability and plasma membrane phospholipid asymmetry.
    Takar M, Huang Y, Graham TR., Free PMC Article

    08/15/2020
    cryo-electron microscopy structure of the P4-ATPase Drs2p-Cdc50p; three structures are presented that represent the complex in an autoinhibited, an intermediate and a fully activated state

    Structure and autoregulation of a P4-ATPase lipid flippase.
    Timcenko M, Lyons JA, Januliene D, Ulstrup JJ, Dieudonné T, Montigny C, Ash MR, Karlsen JL, Boesen T, Kühlbrandt W, Lenoir G, Moeller A, Nissen P.

    10/12/2019
    activation of the Drs2p-Cdc50p flippase follows a multistep mechanism, with preliminary release of a number of constraints, possibly through the binding of regulatory proteins in the trans-Golgi network, followed by full activation by PI4P

    High phosphatidylinositol 4-phosphate (PI4P)-dependent ATPase activity for the Drs2p-Cdc50p flippase after removal of its N- and C-terminal extensions.
    Azouaoui H, Montigny C, Dieudonné T, Champeil P, Jacquot A, Vázquez-Ibar JL, Le Maréchal P, Ulstrup J, Ash MR, Lyons JA, Nissen P, Lenoir G., Free PMC Article

    07/15/2017
    Deletion of KES1 suppresses plasma membrane-missorting defects and the accumulation of intracellular ergosterol in drs2 mutants.

    Phosphatidylserine translocation at the yeast trans-Golgi network regulates protein sorting into exocytic vesicles.
    Hankins HM, Sere YY, Diab NS, Menon AK, Graham TR., Free PMC Article

    10/1/2016
    we describe the overexpression of a yeast lipid flippase complex, namely the P4-ATPase Drs2p and its associated subunit Cdc50p, in a coordinated manner.

    Coordinated Overexpression in Yeast of a P4-ATPase and Its Associated Cdc50 Subunit: The Case of the Drs2p/Cdc50p Lipid Flippase Complex.
    Azouaoui H, Montigny C, Jacquot A, Barry R, Champeil P, Lenoir G.

    09/24/2016
    Imh1p and Drs2p modulate the activity of Gcs1p by timing its interaction with Arl1p, hence providing feedback regulation of Arl1p activity.

    Mechanism of action of the flippase Drs2p in modulating GTP hydrolysis of Arl1p.
    Hsu JW, Chen ZJ, Liu YW, Lee FJ.

    01/31/2015
    Auto-inhibition of Drs2p, a yeast phospholipid flippase, by its carboxyl-terminal tail.

    Auto-inhibition of Drs2p, a yeast phospholipid flippase, by its carboxyl-terminal tail.
    Zhou X, Sebastian TT, Graham TR., Free PMC Article

    01/4/2014
    results demonstrate that activated Arl1p can promote the spatial modulation of membrane organization at the trans-Golgi network through interacting with the effectors Gea2p and Drs2p

    Arl1p regulates spatial membrane organization at the trans-Golgi network through interaction with Arf-GEF Gea2p and flippase Drs2p.
    Tsai PC, Hsu JW, Liu YW, Chen KY, Lee FJ., Free PMC Article

    04/27/2013
    Phosphatidylinositol-4-phosphate tightly controls Drs2p-catalyzed lipid transport and establish the functional relevance of the Drs2p.Cdc50p complex.

    Phosphatidylserine stimulation of Drs2p·Cdc50p lipid translocase dephosphorylation is controlled by phosphatidylinositol-4-phosphate.
    Jacquot A, Montigny C, Hennrich H, Barry R, le Maire M, Jaxel C, Holthuis J, Champeil P, Lenoir G., Free PMC Article

    06/23/2012
    Drs2p can catalyze phospholipid translocation directly through purification and reconstitution of this P4-ATPase into proteoliposomes.

    Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast.
    Zhou X, Graham TR., Free PMC Article

    01/21/2010
    Drs2p, a type IV P-type ATPase required for phospholipid translocase (flippase) activity and transport vesicle budding from the trans-Golgi network, is an effector of phosphatidylinositol-4-phosphate.

    Regulation of a Golgi flippase by phosphoinositides and an ArfGEF.
    Natarajan P, Liu K, Patil DV, Sciorra VA, Jackson CL, Graham TR., Free PMC Article

    01/21/2010
    the affinity of yeast P(4)-ATPase Drs2p for its Cdc50-binding partner fluctuates during the transport cycle, with the strongest interaction occurring at a point where the enzyme is loaded with phospholipid ligand

    Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p.
    Lenoir G, Williamson P, Puts CF, Holthuis JC., Free PMC Article

    01/21/2010
    Potential phospholipid translocases in the Drs2/Dnf family (type IV P-type ATPases [P4-ATPases]) are downstream targets of Kes1p repression.

    Control of protein and sterol trafficking by antagonistic activities of a type IV P-type ATPase and oxysterol binding protein homologue.
    Muthusamy BP, Raychaudhuri S, Natarajan P, Abe F, Liu K, Prinz WA, Graham TR., Free PMC Article

    01/21/2010
    Drs2p acts independently of coat recruitment to facilitate AP-1/clathrin-coated vesicle budding from the TGN

    P4-ATPase requirement for AP-1/clathrin function in protein transport from the trans-Golgi network and early endosomes.
    Liu K, Surendhran K, Nothwehr SF, Graham TR., Free PMC Article

    01/21/2010
    Drs2p is an essential endocytic cargo in cells compromised for Ub-dependent endocytosis.

    Yeast P4-ATPases Drs2p and Dnf1p are essential cargos of the NPFXD/Sla1p endocytic pathway.
    Liu K, Hua Z, Nepute JA, Graham TR., Free PMC Article

    01/21/2010
    These results suggest that Cdc50p-Drs2p plays an important role in the Arf1p/Gcs1-mediated formation of clathrin-coated vesicles for the retrieval pathway from early endosomes to the trans-Golgi network.

    The functional relationship between the Cdc50p-Drs2p putative aminophospholipid translocase and the Arf GAP Gcs1p in vesicle formation in the retrieval pathway from yeast early endosomes to the TGN.
    Sakane H, Yamamoto T, Tanaka K.

    01/21/2010
    Cdc50p, a membrane protein in the endosomal/trans-Golgi network compartments, is a noncatalytic subunit of Drs2p, which is implicated in translocation of phospholipids across lipid bilayers.

    Defects in structural integrity of ergosterol and the Cdc50p-Drs2p putative phospholipid translocase cause accumulation of endocytic membranes, onto which actin patches are assembled in yeast.
    Kishimoto T, Yamamoto T, Tanaka K., Free PMC Article

    01/21/2010
    Drs2 or cdc50 null mutatations cause a loss of plasma membrane PS asymmetry. Loss of plasma membrane asymmetry is a secondary consequence of disrupting protein trafficking.

    Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane.
    Chen S, Wang J, Muthusamy BP, Liu K, Zare S, Andersen RJ, Graham TR.

    01/21/2010
    firstprevious page of 1 nextlast