메뉴 건너뛰기




Volumn 9, Issue 4, 2010, Pages 592-601

Npr2, Yeast homolog of the human tumor suppressor NPRL2, Is a target of Grr1 required for adaptation to growth on diverse nitrogen sources

Author keywords

[No Author keywords available]

Indexed keywords

F BOX PROTEIN; GRR1 PROTEIN, S CEREVISIAE; NITROGEN; NPR2 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SIGNAL PEPTIDE; TUMOR SUPPRESSOR PROTEIN; TUSC4 PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE; NPRL2 PROTEIN, HUMAN;

EID: 77950523750     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00192-09     Document Type: Article
Times cited : (20)

References (33)
  • 1
    • 7644241534 scopus 로고    scopus 로고
    • Amino acid signaling in yeast: Casein kinase I and the Ssy5 endoprotease are key determinants of endoproteolytic activation of the membranebound Stp1 transcription factor
    • Abdel-Sater, F., M. El Bakkoury, A. Urrestarazu, S. Vissers, and B. Andre. 2004. Amino acid signaling in yeast: casein kinase I and the Ssy5 endoprotease are key determinants of endoproteolytic activation of the membranebound Stp1 transcription factor. Mol. Cell. Biol. 24:9771-9785.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 9771-9785
    • Abdel-Sater, F.1    El Bakkoury, M.2    Urrestarazu, A.3    Vissers, S.4    Andre, B.5
  • 2
    • 33745165630 scopus 로고    scopus 로고
    • Regulation of transcription factor latency by receptor-activated proteolysis
    • Andréasson, C., S. Heessen, and P. O. Ljungdahl. 2006. Regulation of transcription factor latency by receptor-activated proteolysis. Genes Dev. 20:1563-1568.
    • (2006) Genes Dev , vol.20 , pp. 1563-1568
    • Andréasson, C.1    Heessen, S.2    Ljungdahl, P.O.3
  • 3
    • 10644233929 scopus 로고    scopus 로고
    • Platinum-intercalator conjugates: From DNA-targeted cisplatin derivatives to adenine binding complexes as potential modulators of gene regulation
    • Baruah, H., C. G. Barry, and U. Bierbach. 2004. Platinum-intercalator conjugates: from DNA-targeted cisplatin derivatives to adenine binding complexes as potential modulators of gene regulation. Curr. Top. Med. Chem. 4:1537-1549.
    • (2004) Curr. Top. Med. Chem , vol.4 , pp. 1537-1549
    • Baruah, H.1    Barry, C.G.2    Bierbach, U.3
  • 4
    • 34848817448 scopus 로고    scopus 로고
    • A proteomic screen reveals SCFGrr1 targets that regulate the glycolytic-gluconeogenic switch
    • Benanti, J. A., S. K. Cheung, M. C. Brady, and D. P. Toczyski. 2007. A proteomic screen reveals SCFGrr1 targets that regulate the glycolytic-gluconeogenic switch. Nat. Cell Biol. 9:1184-1191.
    • (2007) Nat. Cell Biol , vol.9 , pp. 1184-1191
    • Benanti, J.A.1    Cheung, S.K.2    Brady, M.C.3    Toczyski, D.P.4
  • 5
    • 34247338962 scopus 로고    scopus 로고
    • The yeast ammonium transport protein Mep2 and its positive regulator, the Npr1 kinase, play an important role in normal and pseudohyphal growth on various nitrogen media through retrieval of excreted ammonium
    • Boeckstaens, M., B. Andre, and A. M. Marini. 2007. The yeast ammonium transport protein Mep2 and its positive regulator, the Npr1 kinase, play an important role in normal and pseudohyphal growth on various nitrogen media through retrieval of excreted ammonium. Mol. Microbiol. 64:534-546.
    • (2007) Mol. Microbiol , vol.64 , pp. 534-546
    • Boeckstaens, M.1    Andre, B.2    Marini, A.M.3
  • 6
    • 0033573016 scopus 로고    scopus 로고
    • The TOR signaling cascade regulates gene expression in response to nutrients
    • Cardenas, M. E., N. S. Cutler, M. C. Lorenz, C. J. Di Como, and J. Heitman. 1999. The TOR signaling cascade regulates gene expression in response to nutrients. Genes Dev. 13:3271-3279.
    • (1999) Genes Dev , vol.13 , pp. 3271-3279
    • Cardenas, M.E.1    Cutler, N.S.2    Lorenz, M.C.3    Di Como, C.J.4    Heitman, J.5
  • 9
    • 0035941266 scopus 로고    scopus 로고
    • The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast Gap1 permease
    • De Craene, J. O., O. Soetens, and B. Andre. 2001. The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast Gap1 permease. J. Biol. Chem. 276:43939-43948.
    • (2001) J. Biol. Chem , vol.276 , pp. 43939-43948
    • de Craene, J.O.1    Soetens, O.2    Andre, B.3
  • 11
    • 12244262808 scopus 로고    scopus 로고
    • Cisplatin biochemical mechanism of action: From cytotoxicity to induction of cell death through interconnections between apoptotic and necrotic pathways
    • Fuertesa, M. A., J. Castillab, C. Alonsoa, and J. M. Perez. 2003. Cisplatin biochemical mechanism of action: from cytotoxicity to induction of cell death through interconnections between apoptotic and necrotic pathways. Curr. Med. Chem. 10:257-266.
    • (2003) Curr. Med. Chem , vol.10 , pp. 257-266
    • Fuertesa, M.A.1    Castillab, J.2    Alonsoa, C.3    Perez, J.M.4
  • 12
    • 0242300110 scopus 로고    scopus 로고
    • A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery
    • Hitchcock, A. L., K. Auld, S. P. Gygi, and P. A. Silver. 2003. A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc. Natl. Acad. Sci. U. S. A. 100:12735-12740.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 12735-12740
    • Hitchcock, A.L.1    Auld, K.2    Gygi, S.P.3    Silver, P.A.4
  • 14
    • 0035106567 scopus 로고    scopus 로고
    • F-box protein Grr1 interacts with phosphorylated targets via the cationic surface of its leucine-rich repeat
    • Hsiung, Y. G., H. C. Chang, J. L. Pellequer, R. La Valle, S. Lanker, and C. Wittenberg. 2001. F-box protein Grr1 interacts with phosphorylated targets via the cationic surface of its leucine-rich repeat. Mol. Cell. Biol. 21:2506-2520.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 2506-2520
    • Hsiung, Y.G.1    Chang, H.C.2    Pellequer, J.L.3    la Valle, R.4    Lanker, S.5    Wittenberg, C.6
  • 15
    • 1842689859 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of the DNA polymerase epsilon subunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase
    • Kesti, T., W. H. McDonald, J. R. Yates III, and C. Wittenberg. 2004. Cell cycle-dependent phosphorylation of the DNA polymerase epsilon subunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase. J. Biol. Chem. 279: 14245-14255.
    • (2004) J. Biol. Chem , vol.279 , pp. 14245-14255
    • Kesti, T.1    McDonald, W.H.2    Yates III, J.R.3    Wittenberg, C.4
  • 17
    • 34247574716 scopus 로고    scopus 로고
    • Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells
    • Liu, C., J. Apodaca, L. E. Davis, and H. Rao. 2007. Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells. Biotechniques 42:158, 160-162.
    • (2007) Biotechniques 42:158 , pp. 160-162
    • Liu, C.1    Apodaca, J.2    Davis, L.E.3    Rao, H.4
  • 18
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., A. McKenzie III, D. J. Demarini, N. G. Shah, A. Wach, A. Brachat, P. Philippsen, and J. R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 19
    • 0037094434 scopus 로고    scopus 로고
    • Nitrogen regulation in Saccharomyces cerevisiae
    • Magasanik, B., and C. A. Kaiser. 2002. Nitrogen regulation in Saccharomyces cerevisiae. Gene 290:1-18.
    • (2002) Gene , vol.290 , pp. 1-18
    • Magasanik, B.1    Kaiser, C.A.2
  • 20
    • 1442281229 scopus 로고    scopus 로고
    • A genome-wide screen identifies genes required for centromeric cohesion
    • Marston, A. L., W. H. Tham, H. Shah, and A. Amon. 2004. A genome-wide screen identifies genes required for centromeric cohesion. Science 303:1367-1370.
    • (2004) Science , vol.303 , pp. 1367-1370
    • Marston, A.L.1    Tham, W.H.2    Shah, H.3    Amon, A.4
  • 21
    • 0036399228 scopus 로고    scopus 로고
    • Shotgun proteomics and biomarker discovery
    • McDonald, W. H., and J. R. Yates III. 2002. Shotgun proteomics and biomarker discovery. Dis. Markers 18:99-105.
    • (2002) Dis. Markers , vol.18 , pp. 99-105
    • McDonald, W.H.1    Yates III, J.R.2
  • 22
    • 1242274644 scopus 로고    scopus 로고
    • Glucose sensing and signaling in Saccharomyces cerevisiae through the Rgt2 glucose sensor and casein kinase I
    • Moriya, H., and M. Johnston. 2004. Glucose sensing and signaling in Saccharomyces cerevisiae through the Rgt2 glucose sensor and casein kinase I. Proc. Natl. Acad. Sci. U. S. A. 101:1572-1577.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 1572-1577
    • Moriya, H.1    Johnston, M.2
  • 23
    • 67651235863 scopus 로고    scopus 로고
    • A genome-wide screen for regulators of TORC1 in response to amino acid starvation reveals a conserved Npr2/3 complex
    • Neklesa, T. K., and R. W. Davis. 2009. A genome-wide screen for regulators of TORC1 in response to amino acid starvation reveals a conserved Npr2/3 complex. PLoS Genet. 5:e1000515.
    • (2009) PLoS Genet , vol.5
    • Neklesa, T.K.1    Davis, R.W.2
  • 24
    • 0028840055 scopus 로고
    • A second nitrogen permease regulator in Saccharomyces cerevisiae
    • Rousselet, G., M. Simon, P. Ripoche, and J. M. Buhler. 1995. A second nitrogen permease regulator in Saccharomyces cerevisiae. FEBS Lett. 359: 215-219.
    • (1995) FEBS Lett , vol.359 , pp. 215-219
    • Rousselet, G.1    Simon, M.2    Ripoche, P.3    Buhler, J.M.4
  • 25
    • 0036180524 scopus 로고    scopus 로고
    • Inactivation of the Saccharomyces cerevisiae SKY1 gene induces a specific modification of the yeast anticancer drug sensitivity profile accompanied by a mutator phenotype
    • Schenk, P. W., A. W. Boersma, M. Brok, H. Burger, G. Stoter, and K. Nooter. 2002. Inactivation of the Saccharomyces cerevisiae SKY1 gene induces a specific modification of the yeast anticancer drug sensitivity profile accompanied by a mutator phenotype. Mol. Pharmacol. 61:659-666.
    • (2002) Mol. Pharmacol , vol.61 , pp. 659-666
    • Schenk, P.W.1    Boersma, A.W.2    Brok, M.3    Burger, H.4    Stoter, G.5    Nooter, K.6
  • 26
    • 0042844651 scopus 로고    scopus 로고
    • Anticancer drug resistance induced by disruption of the Saccharomyces cerevisiae NPR2 gene: A novel component involved in cisplatinand doxorubicin-provoked cell kill
    • Schenk, P. W., M. Brok, A. W. Boersma, J. A. Brandsma, H. Den Dulk, H. Burger, G. Stoter, J. Brouwer, and K. Nooter. 2003. Anticancer drug resistance induced by disruption of the Saccharomyces cerevisiae NPR2 gene: a novel component involved in cisplatinand doxorubicin-provoked cell kill. Mol. Pharmacol. 64:259-268.
    • (2003) Mol. Pharmacol , vol.64 , pp. 259-268
    • Schenk, P.W.1    Brok, M.2    Boersma, A.W.3    Brandsma, J.A.4    Den Dulk, H.5    Burger, H.6    Stoter, G.7    Brouwer, J.8    Nooter, K.9
  • 27
    • 0035941194 scopus 로고    scopus 로고
    • Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease
    • Soetens, O., J. O. De Craene, and B. Andre. 2001. Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J. Biol. Chem. 276:43949-43957.
    • (2001) Gap1. J. Biol. Chem , vol.276 , pp. 43949-43957
    • Soetens, O.1    de Craene, J.O.2    Andre, B.3
  • 28
    • 4744373127 scopus 로고    scopus 로고
    • Regulation and recognition of SCFGrr1 targets in the glucose and amino acid signaling pathways
    • Spielewoy, N., K. Flick, T. I. Kalashnikova, J. R. Walker, and C. Wittenberg. 2004. Regulation and recognition of SCFGrr1 targets in the glucose and amino acid signaling pathways. Mol. Cell. Biol. 24:8994-9005.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 8994-9005
    • Spielewoy, N.1    Flick, K.2    Kalashnikova, T.I.3    Walker, J.R.4    Wittenberg, C.5
  • 30
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., A. Brachat, R. Pohlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10:1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 32
    • 0034698665 scopus 로고    scopus 로고
    • Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae
    • Yun, C. Y., and X. D. Fu. 2000. Conserved SR protein kinase functions in nuclear import and its action is counteracted by arginine methylation in Saccharomyces cerevisiae. J. Cell Biol. 150:707-718.
    • (2000) J. Cell Biol , vol.150 , pp. 707-718
    • Yun, C.Y.1    Fu, X.D.2
  • 33
    • 0037037787 scopus 로고    scopus 로고
    • Tumor suppressor genes on chromosome 3p involved in the pathogenesis of lung and other cancers
    • Zabarovsky, E. R., M. I. Lerman, and J. D. Minna. 2002. Tumor suppressor genes on chromosome 3p involved in the pathogenesis of lung and other cancers. Oncogene 21:6915-6935.
    • (2002) Oncogene , vol.21 , pp. 6915-6935
    • Zabarovsky, E.R.1    Lerman, M.I.2    Minna, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.