Amino acid transport System A resembles System N in sequence but differs in mechanism

被引:158
作者
Reimer, RJ
Chaudhry, FA
Grays, AT
Edwards, RH
机构
[1] Univ Calif San Francisco, Sch Med, Dept Neurol, San Francisco, CA 94143 USA
[2] Univ Calif San Francisco, Sch Med, Dept Physiol, San Francisco, CA 94143 USA
[3] Univ Calif San Francisco, Sch Med, Dept Anesthesia, Grad Program Neurosci, San Francisco, CA 94143 USA
[4] Univ Calif San Francisco, Sch Med, Grad Program Cell Biol, San Francisco, CA 94143 USA
[5] Univ Calif San Francisco, Sch Med, Grad Program Biomed Sci, San Francisco, CA 94143 USA
[6] Univ Oslo, Inst Basic Med Sci, Dept Anat, N-0317 Oslo, Norway
关键词
D O I
10.1073/pnas.140152797
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Classical amino acid transport System A accounts for most of the Na+-dependent neutral amino acid uptake by mammalian cells. System A has also provided a paradigm for short- and long-term regulation by physiological stimuli. We now report the isolation of a cDNA encoding System A that shows close similarity to the recently identified System N transporter (SN1). The System A transporter (SA1) and SN1 share many functional characteristics, including a marked sensitivity to low pH, but, unlike SN1, SA1 does not mediate proton exchange. Transport mediated by SA1 is also electrogenic. Amino acid transport Systems A and N thus appear closely related in function as well as structure, but exhibit important differences in ionic coupling.
引用
收藏
页码:7715 / 7720
页数:6
相关论文
共 44 条
  • [21] KILBERG MS, 1980, J BIOL CHEM, V255, P4011
  • [22] KRISTENSEN LO, 1980, J BIOL CHEM, V255, P5236
  • [23] Loss of BETA2/NeuroD leads to malformation of the dentate gyrus and epilepsy
    Liu, M
    Pleasure, SJ
    Collins, AE
    Noebels, JL
    Naya, FJ
    Tsai, MJ
    Lowenstein, DH
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (02) : 865 - 870
  • [24] Liu YJ, 1997, ANNU REV NEUROSCI, V20, P125
  • [25] REGULATORY AND MOLECULAR ASPECTS OF MAMMALIAN AMINO-ACID-TRANSPORT
    MCGIVAN, JD
    PASTORANGLADA, M
    [J]. BIOCHEMICAL JOURNAL, 1994, 299 : 321 - 334
  • [26] Identification and characterization of the vesicular GABA transporter
    McIntire, SL
    Reimer, RJ
    Schuske, K
    Edwards, RH
    Jorgensen, EM
    [J]. NATURE, 1997, 389 (6653) : 870 - 876
  • [27] REGULATION OF THE A-SYSTEM OF AMINO-ACID-TRANSPORT IN CHINESE-HAMSTER OVARY CELLS, CHO-K1 - THE DIFFERENCE IN SPECIFICITY BETWEEN THE APO-REPRESSOR INACTIVATOR (APO-RI) AND THE TRANSPORTER AND THE CHARACTERIZATION OF THE PROPOSED APO-RI
    MOFFETT, J
    ENGLESBERG, E
    [J]. JOURNAL OF CELLULAR PHYSIOLOGY, 1986, 126 (03) : 421 - 429
  • [28] CONTROL OF A-SYSTEM AMINO-ACID-TRANSPORT BY A 2ND REGULATORY GENE R2 IN CHINESE-HAMSTER OVARY CELLS CHO-K1 AND THE POSSIBLE CONNECTION OF THIS GENE WITH INSULIN ACTIVITY
    MOFFETT, J
    PERIER, F
    JONES, M
    ENGLESBERG, E
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (22) : 8040 - 8043
  • [29] Molecular biology of mammalian plasma membrane amino acid transporters
    Palacin, M
    Estevez, R
    Bertran, J
    Zorzano, A
    [J]. PHYSIOLOGICAL REVIEWS, 1998, 78 (04) : 969 - 1054
  • [30] Identification of a membrane protein, LAT-2, that co-expresses with 4F2 heavy chain, an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids
    Pineda, M
    Fernández, E
    Torrents, D
    Estévez, R
    López, C
    Camps, M
    Lloberas, J
    Zorzano, A
    Palacín, M
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (28) : 19738 - 19744