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    SLC36A1 solute carrier family 36 member 1 [ Homo sapiens (human) ]

    Gene ID: 206358, updated on 6-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    SLC36A1-mTORC1 signaling drives acquired resistance to CDK4/6 inhibitors.

    SLC36A1-mTORC1 signaling drives acquired resistance to CDK4/6 inhibitors.
    Yoshida A, Bu Y, Qie S, Wrangle J, Camp ER, Hazard ES, Hardiman G, de Leeuw R, Knudsen KE, Diehl JA., Free PMC Article

    05/2/2020
    Increasing the PAT1 level does not readily increase the mTORC1 activity. The lysosomal PAT1 was increased by starvation and decreased by nutrient replenishment. The lysosomal PAT1 plays a negative role on the mTORC1 activity.

    The amino acid transporter PAT1 regulates mTORC1 in a nutrient-sensitive manner that requires its transport activity.
    Zhao L, Zhang X, Ji X, Jin Y, Liu W.

    02/29/2020
    A mechanism through which amino acids may suppress the expression of PAT1 on lysosomes by inducing protein cleavage to remove a targeting signal.

    Amino acids suppress the expression of PAT1 on lysosomes via inducing the cleavage of a targeting signal.
    Ji X, Zhao L, Luo H, Zhang X, Jin Y, Liu W.

    10/14/2017
    Data indicate that the glycosylation-deficient mutant of amino acid transporter PAT1 (PAT1(3)(NQ) ) is unstable and is degraded mainly via the endoplasmic reticulum-associated degradation pathway in HEK293 cells.

    Glycosylation affects the stability and subcellular distribution of human PAT1 protein.
    Luo H, Zhao L, Ji X, Zhang X, Jin Y, Liu W.

    06/3/2017
    Sertraline is an apparent non-competitive inhibitor of PAT1-mediated transport.

    Sertraline inhibits the transport of PAT1 substrates in vivo and in vitro.
    Nielsen CU, Frølund S, Abdulhadi S, Sari H, Langthaler L, Nøhr MK, Kall MA, Brodin B, Holm R., Free PMC Article

    08/9/2014
    Data suggest that PAT1 in enterocytes is responsible for intestinal absorption of some of the alkaloids from areca nut (i.e., arecaidine, guvacine, isoguvacine).

    Transport of the areca nut alkaloid arecaidine by the human proton-coupled amino acid transporter 1 (hPAT1).
    Voigt V, Laug L, Zebisch K, Thondorf I, Markwardt F, Brandsch M.

    09/21/2013
    estrogen attenuates the activity of PAT1 by directly closing PAT1

    Estradiol inhibits the activity of proton-coupled amino acid transporter PAT1 expressed in Xenopus oocytes.
    Shan L, Yang Y, Wang J, Zuo J, Dong X, Li C, Li D.

    03/23/2013
    In hPAT1 expressing oocytes Gly-Tyr, Gly-Pro, and Gly-Phe inhibited currents induced by drug substances.

    Intestinal drug transport via the proton-coupled amino acid transporter PAT1 (SLC36A1) is inhibited by Gly-X(aa) dipeptides.
    Frølund S, Langthaler L, Kall MA, Holm R, Nielsen CU.

    03/9/2013
    PATs function as part of an amino acid-sensing engine that drives mTORC1 activation from endosomal and lysosomal membranes

    Proton-assisted amino acid transporter PAT1 complexes with Rag GTPases and activates TORC1 on late endosomal and lysosomal membranes.
    Ögmundsdóttir MH, Heublein S, Kazi S, Reynolds B, Visvalingam SM, Shaw MK, Goberdhan DC., Free PMC Article

    09/15/2012
    In human cells, SLC36A1 localized on intracellular membranes is required for amino acid-dependent mTORC1 activation and cell proliferation. SLC36A1 also has similar in vivo growth regulatory activity to fly SLC36 AAAPs when expressed in Drosophila.

    Proton-assisted amino-acid transporters are conserved regulators of proliferation and amino-acid-dependent mTORC1 activation.
    Heublein S, Kazi S, Ogmundsdóttir MH, Attwood EV, Kala S, Boyd CA, Wilson C, Goberdhan DC., Free PMC Article

    01/23/2012
    This study is the first to demonstrate both taurine uptake via PAT1 and functional expression of PAT1 at the apical membrane of the intestinal epithelium.

    Taurine uptake across the human intestinal brush-border membrane is via two transporters: H+-coupled PAT1 (SLC36A1) and Na+- and Cl(-)-dependent TauT (SLC6A6).
    Anderson CM, Howard A, Walters JR, Ganapathy V, Thwaites DT., Free PMC Article

    01/21/2010
    a disulfide bridge is essential for the transport function of the human proton-coupled amino acid transporter hPAT1

    Identification of a disulfide bridge essential for transport function of the human proton-coupled amino acid transporter hPAT1.
    Dorn M, Weiwad M, Markwardt F, Laug L, Rudolph R, Brandsch M, Bosse-Doenecke E., Free PMC Article

    01/21/2010
    Data conclude that hPAT1 might be responsible for the intestinal absorption of beta-GPA thereby allowing its oral administration.

    The orally active antihyperglycemic drug beta-guanidinopropionic acid is transported by the human proton-coupled amino acid transporter hPAT1.
    Metzner L, Dorn M, Markwardt F, Brandsch M.

    01/21/2010
    The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1

    The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
    Dorn M, Jaehme M, Weiwad M, Markwardt F, Rudolph R, Brandsch M, Bosse-Doenecke E.

    01/21/2010
    His-55 might be responsible for binding and translocation of H+ in the course of cellular amino acid uptake by PAT1.

    Mutational analysis of histidine residues in the human proton-coupled amino acid transporter PAT1.
    Metzner L, Natho K, Zebisch K, Dorn M, Bosse-Doenecke E, Ganapathy V, Brandsch M.

    01/21/2010
    Amino acid uptake via hPAT1 is inhibited by activators of the cAMP pathway indirectly through inhibition of NHE3 activity.

    Indirect regulation of the intestinal H+-coupled amino acid transporter hPAT1 (SLC36A1).
    Anderson CM, Thwaites DT.

    01/21/2010
    A high-capacity imino acid carrier localized at the small intestinal luminal membrane that transports nutrients and amino acids and imino acids.

    H+/amino acid transporter 1 (PAT1) is the imino acid carrier: An intestinal nutrient/drug transporter in human and rat.
    Anderson CM, Grenade DS, Boll M, Foltz M, Wake KA, Kennedy DJ, Munck LK, Miyauchi S, Taylor PM, Campbell FC, Munck BG, Daniel H, Ganapathy V, Thwaites DT.

    01/21/2010
    PAT1a, which is 99.0% identical to protein interacting with APP tail 1 (PAT1), is a functional link between the transport and processing of beta-amyloid precursor protein APP and its two paralogs APLP1 and APLP2 in vivo.

    PAT1a modulates intracellular transport and processing of amyloid precursor protein (APP), APLP1, and APLP2.
    Kuan YH, Gruebl T, Soba P, Eggert S, Nesic I, Back S, Kirsch J, Beyreuther K, Kins S.

    01/21/2010
    PAT1 expressed exclusively in apical membrane of Caco-2 cells. hPAT1 may be responsible for H(+)-coupled amino acid transport expressed in apical membrane of Caco-2 cells.

    Structure, function and immunolocalization of a proton-coupled amino acid transporter (hPAT1) in the human intestinal cell line Caco-2.
    Chen Z, Fei YJ, Anderson CM, Wake KA, Miyauchi S, Huang W, Thwaites DT, Ganapathy V., Free PMC Article

    01/21/2010
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