Sensors of extracellular nutrients in Saccharomyces cerevisiae

被引:151
作者
Forsberg, H [1 ]
Ljungdahl, PO [1 ]
机构
[1] Ludwig Inst Canc Res, S-17177 Stockholm, Sweden
关键词
signal transduction; nutrient sensing; metabolite-transport proteins; fungal proteins;
D O I
10.1007/s002940100244
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
It has been known for a long time that yeast are capable of making rapid metabolic adjustments in response to changing extracellular nutrient conditions. Until recently it was thought that yeast, in contrast to mammalian cells, primarily monitored nutrient availability through the activity of intracellular sensors. Recent advances in our understanding of nutrient sensing indicate that yeast cells possess several nutrient-sensing systems localized in the plasma membrane that transduce information regarding the presence of extracellular amino acids, ammonium, and glucose. Strikingly, the transmembrane components of several of these sensors, Ssy1p, Mep2p, Snf3p, and Rgt2p, are unique members of nutrient-transport protein families. Perhaps with the exception of Mep2p, the ability of these transporter homologues to transduce nutrient-(ligand)-induced Signals across the plasma membrane appears to be independent of nutrient uptake; and thus these sensor components may function analogously to traditional ligand-dependent receptors. Additionally, the G protein-coupled receptor Gpr1p has been shown to exhibit properties consistent with it being a sensor. These recent advances indicate that yeast cells obtain information regarding their growth environments using sensing systems that are more similar to those present in mammalian cells than previously thought. The fact that yeast plasma membrane nutrient sensors have only recently been discovered reveals how little is understood regarding the molecular signals that enable eukaryotic cells to adapt to changing environments.
引用
收藏
页码:91 / 109
页数:19
相关论文
共 154 条
  • [41] ISOLATION OF STD1, A HIGH-COPY-NUMBER SUPPRESSOR OF A DOMINANT-NEGATIVE MUTATION IN THE YEAST TATA-BINDING PROTEIN
    GANSTER, RW
    SHEN, WQ
    SCHMIDT, MC
    [J]. MOLECULAR AND CELLULAR BIOLOGY, 1993, 13 (06) : 3650 - 3659
  • [42] Sequence of a putative glucose 6-phosphate translocase, mutated in glycogen storage disease type Ib
    Gerin, I
    Veiga-da-Cunha, M
    Achouri, Y
    Collet, JF
    Van Schaftingen, E
    [J]. FEBS LETTERS, 1997, 419 (2-3): : 235 - 238
  • [43] Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles
    Gilstring, CF
    Melin-Larsson, M
    Ljungdahl, PO
    [J]. MOLECULAR BIOLOGY OF THE CELL, 1999, 10 (11) : 3549 - 3565
  • [44] A method for determining the in vivo topology of yeast polytopic membrane proteins demonstrates that Gap1p fully integrates into the membrane independently of Shr3p
    Gilstring, CF
    Ljungdahl, PO
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (40) : 31488 - 31495
  • [45] UNIPOLAR CELL DIVISIONS IN THE YEAST SACCHAROMYCES-CEREVISIAE LEAD TO FILAMENTOUS GROWTH - REGULATION BY STARVATION AND RAS
    GIMENO, CJ
    LJUNGDAHL, PO
    STYLES, CA
    FINK, GR
    [J]. CELL, 1992, 68 (06) : 1077 - 1090
  • [46] BAP2, A GENE ENCODING A PERMEASE FOR BRANCHED-CHAIN AMINO-ACIDS IN SACCHAROMYCES-CEREVISIAE
    GRAUSLUND, M
    DIDION, T
    KIELLANDBRANDT, MC
    ANDERSEN, HA
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 1995, 1269 (03): : 275 - 280
  • [47] Grenson M, 1992, MOL ASPECTS TRANSPOR, P219
  • [48] Guillemain G, 2000, J CELL SCI, V113, P841
  • [49] Multiplicity and regulation of genes encoding peptide transporters in Saccharomyces cerevisiae
    Hauser, M
    Narita, V
    Donhardt, AM
    Naider, F
    Becker, JM
    [J]. MOLECULAR MEMBRANE BIOLOGY, 2001, 18 (01) : 105 - 112
  • [50] TRANSLATIONAL CONTROL OF GCN4 - AN IN-VIVO BAROMETER OF INITIATION-FACTOR ACTIVITY
    HINNEBUSCH, AG
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1994, 19 (10) : 409 - 414