메뉴 건너뛰기




Volumn 18, Issue 6, 2013, Pages 459-475

Phosphorylation of a conserved Thr357 in yeast Nedd4-like ubiquitin ligase Rsp5 is involved in down-regulation of the general amino acid permease Gap1

Author keywords

[No Author keywords available]

Indexed keywords

AZETIDINE 2 CARBOXYLIC ACID; GAP1 PROTEIN; LIGASE; NITROGEN; PERMEASE; PROLINE; RSP5 PROTEIN; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG;

EID: 84878347483     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/gtc.12049     Document Type: Article
Times cited : (22)

References (49)
  • 1
    • 35349022993 scopus 로고    scopus 로고
    • A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae
    • Alberti, S., Gitler, A.D. & Lindquist, S. (2007) A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae. Yeast 24, 913-919.
    • (2007) Yeast , vol.24 , pp. 913-919
    • Alberti, S.1    Gitler, A.D.2    Lindquist, S.3
  • 2
    • 0037115602 scopus 로고    scopus 로고
    • Receptor-mediated endoproteolytic activation of two transcription factors in yeast
    • Andréasson, C. & Ljungdahl, P.O. (2002) Receptor-mediated endoproteolytic activation of two transcription factors in yeast. Genes Dev. 16, 3158-3172.
    • (2002) Genes Dev. , vol.16 , pp. 3158-3172
    • Andréasson, C.1    Ljungdahl, P.O.2
  • 3
    • 1342333128 scopus 로고    scopus 로고
    • Four permeases import proline and the toxic proline analogue azetidine-2-carboxylate into yeast
    • Andréasson, C., Neve, E.P. & Ljungdahl, P.O. (2004) Four permeases import proline and the toxic proline analogue azetidine-2-carboxylate into yeast. Yeast 21, 193-199.
    • (2004) Yeast , vol.21 , pp. 193-199
    • Andréasson, C.1    Neve, E.P.2    Ljungdahl, P.O.3
  • 4
    • 0035941266 scopus 로고    scopus 로고
    • The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast Gap1 permease
    • De Craene, J.O., Soetens, O. & André, B. (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    André, B.3
  • 5
    • 0035149694 scopus 로고    scopus 로고
    • Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis
    • Dunn, R. & Hicke, L. (2001) Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis. Mol. Biol. Cell 12, 421-435.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 421-435
    • Dunn, R.1    Hicke, L.2
  • 6
  • 7
    • 0020774482 scopus 로고
    • Inactivation-reactivation process and repression of permease formation regulate several ammonia-sensitive permeases in the yeast Saccharomyces cerevisiae
    • Grenson, M. (1983) Inactivation-reactivation process and repression of permease formation regulate several ammonia-sensitive permeases in the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 133, 135-139.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 135-139
    • Grenson, M.1
  • 8
    • 0029994841 scopus 로고    scopus 로고
    • A new efficient gene disruption cassette for repeated use in budding yeast
    • Guldener, U., Heck, S., Fielder, T., Beinhauer, J. & Hegemann, J.H. (1996) A new efficient gene disruption cassette for repeated use in budding yeast. Nucleic Acids Res. 24, 2519-2524.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2519-2524
    • Guldener, U.1    Heck, S.2    Fielder, T.3    Beinhauer, J.4    Hegemann, J.H.5
  • 9
    • 58149328668 scopus 로고    scopus 로고
    • Engineering of the yeast ubiquitin ligase Rsp5: isolation of a new variant that induces constitutive inactivation of the general amino acid permease Gap1
    • Haitani, Y., Nakata, M., Sasaki, T., Uchida, A. & Takagi, H. (2009) Engineering of the yeast ubiquitin ligase Rsp5: isolation of a new variant that induces constitutive inactivation of the general amino acid permease Gap1. FEMS Yeast Res. 9, 73-86.
    • (2009) FEMS Yeast Res. , vol.9 , pp. 73-86
    • Haitani, Y.1    Nakata, M.2    Sasaki, T.3    Uchida, A.4    Takagi, H.5
  • 10
    • 33746406889 scopus 로고    scopus 로고
    • Rsp5 regulates expression of stress proteins via post-translational modification of Hsf1 and Msn4 in Saccharomyces cerevisiae
    • Haitani, Y., Shimoi, H. & Takagi, H. (2006) Rsp5 regulates expression of stress proteins via post-translational modification of Hsf1 and Msn4 in Saccharomyces cerevisiae. FEBS Lett. 580, 3433-3438.
    • (2006) FEBS Lett. , vol.580 , pp. 3433-3438
    • Haitani, Y.1    Shimoi, H.2    Takagi, H.3
  • 11
    • 38849086867 scopus 로고    scopus 로고
    • Rsp5 is required for the nuclear export of mRNA of HSF1 and MSN2/4 under stress conditions in Saccharomyces cerevisiae
    • Haitani, Y. & Takagi, H. (2008) Rsp5 is required for the nuclear export of mRNA of HSF1 and MSN2/4 under stress conditions in Saccharomyces cerevisiae. Genes Cells 13, 105-116.
    • (2008) Genes Cells , vol.13 , pp. 105-116
    • Haitani, Y.1    Takagi, H.2
  • 12
    • 0035858866 scopus 로고    scopus 로고
    • Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease
    • Helliwell, S.B., Losko, S. & Kaiser, C.A. (2001) Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease. J. Cell Biol. 153, 649-662.
    • (2001) J. Cell Biol. , vol.153 , pp. 649-662
    • Helliwell, S.B.1    Losko, S.2    Kaiser, C.A.3
  • 13
    • 33745037938 scopus 로고    scopus 로고
    • Comparative analysis of Saccharomyces cerevisiae WW domains and their interacting proteins
    • doi:10.1186/gb-2006-7-4-r30
    • Hesselberth, J.R., Miller, J.P., Golob, A., Stajich, J.E., Michaud, G.A. & Fields, S. (2006) Comparative analysis of Saccharomyces cerevisiae WW domains and their interacting proteins. Genome Biol. 7, R30. doi:10.1186/gb-2006-7-4-r30.
    • (2006) Genome Biol. , vol.7
    • Hesselberth, J.R.1    Miller, J.P.2    Golob, A.3    Stajich, J.E.4    Michaud, G.A.5    Fields, S.6
  • 14
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L. & Riezman, H. (1996) Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84, 277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 15
    • 69449102285 scopus 로고    scopus 로고
    • The yeast ubiquitin ligase Rsp5 downregulates the alpha subunit of nascent polypeptide-associated complex Egd2 under stress conditions
    • Hiraishi, H., Shimada, T., Ohtsu, I., Sato, T. & Takagi, H. (2009) The yeast ubiquitin ligase Rsp5 downregulates the alpha subunit of nascent polypeptide-associated complex Egd2 under stress conditions. FEBS J. 276, 5287-5297.
    • (2009) FEBS J. , vol.276 , pp. 5287-5297
    • Hiraishi, H.1    Shimada, T.2    Ohtsu, I.3    Sato, T.4    Takagi, H.5
  • 16
    • 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., Auld, K., Gygi, S.P. & Silver, P.A. (2003) A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery. Proc. Natl Acad. Sci. USA 100, 12735-12740.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12735-12740
    • Hitchcock, A.L.1    Auld, K.2    Gygi, S.P.3    Silver, P.A.4
  • 17
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe, T., Matuschewski, K., Rape, M., Schlenker, S., Ulrich, H.D. & Jentsch, S. (2000) Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102, 577-586.
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 18
    • 0141816772 scopus 로고    scopus 로고
    • A nonconserved Ala401 in the yeast Rsp5 ubiquitin ligase is involved in degradation of Gap1 permease and stress-induced abnormal proteins
    • Hoshikawa, C., Shichiri, M., Nakamori, S. & Takagi, H. (2003) A nonconserved Ala401 in the yeast Rsp5 ubiquitin ligase is involved in degradation of Gap1 permease and stress-induced abnormal proteins. Proc. Natl Acad. Sci. USA 100, 11505-11510.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 11505-11510
    • Hoshikawa, C.1    Shichiri, M.2    Nakamori, S.3    Takagi, H.4
  • 19
    • 0030888109 scopus 로고    scopus 로고
    • The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase
    • Huibregtse, J.M., Yang, J.C. & Beaudenon, S.L. (1997) The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase. Proc. Natl Acad. Sci. USA 94, 3656-3661.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3656-3661
    • Huibregtse, J.M.1    Yang, J.C.2    Beaudenon, S.L.3
  • 21
    • 22744456248 scopus 로고    scopus 로고
    • The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme
    • Kee, Y., Lyon, N. & Huibregtse, J.M. (2005) The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme. EMBO J. 24, 2414-2424.
    • (2005) EMBO J. , vol.24 , pp. 2414-2424
    • Kee, Y.1    Lyon, N.2    Huibregtse, J.M.3
  • 22
    • 12144251018 scopus 로고    scopus 로고
    • Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER
    • Kota, J. & Ljungdahl, P.O. (2005) Specialized membrane-localized chaperones prevent aggregation of polytopic proteins in the ER. J. Cell Biol. 168, 79-88.
    • (2005) J. Cell Biol. , vol.168 , pp. 79-88
    • Kota, J.1    Ljungdahl, P.O.2
  • 23
    • 0036276809 scopus 로고    scopus 로고
    • Assaying protein ubiquitination in Saccharomyces cerevisiae
    • Laney, J.D. & Hochstrasser, M. (2002) Assaying protein ubiquitination in Saccharomyces cerevisiae. Methods Enzymol. 351, 248-257.
    • (2002) Methods Enzymol. , vol.351 , pp. 248-257
    • Laney, J.D.1    Hochstrasser, M.2
  • 25
    • 67349113489 scopus 로고    scopus 로고
    • Ubiquitin ligase adaptors: regulators of ubiquitylation and endocytosis of plasma membrane proteins
    • Léon, S. & Haguenauer-Tsapis, R. (2009) Ubiquitin ligase adaptors: regulators of ubiquitylation and endocytosis of plasma membrane proteins. Exp. Cell Res. 315, 1574-1583.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1574-1583
    • Léon, S.1    Haguenauer-Tsapis, R.2
  • 26
    • 55549102963 scopus 로고    scopus 로고
    • Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface
    • Lin, C.H., MacGurn, J.A., Chu, T., Stefan, C.J. & Emr, S.D. (2008) Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 135, 714-725.
    • (2008) Cell , vol.135 , pp. 714-725
    • Lin, C.H.1    MacGurn, J.A.2    Chu, T.3    Stefan, C.J.4    Emr, S.D.5
  • 27
    • 84868676870 scopus 로고    scopus 로고
    • Internal amino acids promote Gap1 permease ubiquitylation via TORC1/Npr1/14-3-3-dependent control of the Bul arrestin-like adaptors
    • Merhi, A. & André, B. (2012) Internal amino acids promote Gap1 permease ubiquitylation via TORC1/Npr1/14-3-3-dependent control of the Bul arrestin-like adaptors. Mol. Cell. Biol. 32, 4510-4522.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4510-4522
    • Merhi, A.1    André, B.2
  • 29
    • 70649112359 scopus 로고    scopus 로고
    • Arrestin-mediated endocytosis of yeast plasma membrane transporters
    • Nikko, E. & Pelham, H.R.B. (2009) Arrestin-mediated endocytosis of yeast plasma membrane transporters. Traffic 10, 1856-1867.
    • (2009) Traffic , vol.10 , pp. 1856-1867
    • Nikko, E.1    Pelham, H.R.B.2
  • 30
    • 0028953080 scopus 로고
    • Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane
    • Nothwehr, S.F., Conibear, E. & Stevens, T.H. (1995) Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane. J. Cell Biol. 129, 35-46.
    • (1995) J. Cell Biol. , vol.129 , pp. 35-46
    • Nothwehr, S.F.1    Conibear, E.2    Stevens, T.H.3
  • 31
    • 84859128614 scopus 로고    scopus 로고
    • Bul proteins, a non-redundant, antagonistic family of ubiquitin ligase regulatory proteins
    • Novoselova, T.V., Zahira, K., Rose, R.S. & Sullivan, J.A. (2012) Bul proteins, a non-redundant, antagonistic family of ubiquitin ligase regulatory proteins. Eukaryot. Cell 11, 463-470.
    • (2012) Eukaryot. Cell , vol.11 , pp. 463-470
    • Novoselova, T.V.1    Zahira, K.2    Rose, R.S.3    Sullivan, J.A.4
  • 32
    • 77958046490 scopus 로고    scopus 로고
    • Alpha-arrestins Aly1 and Aly2 regulate intracellular trafficking in response to nutrient signaling
    • O'Donnell, A.F., Apffel, A., Gardner, R.G. & Cyert, M.S. (2010) Alpha-arrestins Aly1 and Aly2 regulate intracellular trafficking in response to nutrient signaling. Mol. Biol. Cell 21, 3552-3566.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3552-3566
    • O'Donnell, A.F.1    Apffel, A.2    Gardner, R.G.3    Cyert, M.S.4
  • 34
    • 33749467954 scopus 로고    scopus 로고
    • Activity-dependent reversible inactivation of the general amino acid permease
    • Risinger, A.L., Cain, N.E., Chen, E.J. & Kaiser, C.A. (2006) Activity-dependent reversible inactivation of the general amino acid permease. Mol. Biol. Cell 17, 4411-4419.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4411-4419
    • Risinger, A.L.1    Cain, N.E.2    Chen, E.J.3    Kaiser, C.A.4
  • 35
    • 51349159616 scopus 로고    scopus 로고
    • Different ubiquitin signals act at the Golgi and plasma membrane to direct GAP1 trafficking
    • Risinger, A.L. & Kaiser, C.A. (2008) Different ubiquitin signals act at the Golgi and plasma membrane to direct GAP1 trafficking. Mol. Biol. Cell 19, 2962-2972.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2962-2972
    • Risinger, A.L.1    Kaiser, C.A.2
  • 36
    • 0030809956 scopus 로고    scopus 로고
    • Control of amino acid permease sorting in the late secretory pathway of Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8
    • Roberg, K.J., Bickel, S., Rowley, N. & Kaiser, C.A. (1997) Control of amino acid permease sorting in the late secretory pathway of Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8. Genetics 147, 1569-1584.
    • (1997) Genetics , vol.147 , pp. 1569-1584
    • Roberg, K.J.1    Bickel, S.2    Rowley, N.3    Kaiser, C.A.4
  • 38
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin, D. & Kumar, S. (2009) Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 10, 398-409.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 39
    • 33745615846 scopus 로고    scopus 로고
    • Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway
    • Rubio-Texeira, M. & Kaiser, C.A. (2006) Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway. Mol. Biol. Cell 17, 3031-3050.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3031-3050
    • Rubio-Texeira, M.1    Kaiser, C.A.2
  • 41
    • 34247573976 scopus 로고    scopus 로고
    • Seven-transmembrane receptors and ubiquitination
    • Shenoy, S.K. (2007) Seven-transmembrane receptors and ubiquitination. Circ. Res. 100, 1142-1154.
    • (2007) Circ. Res. , vol.100 , pp. 1142-1154
    • Shenoy, S.K.1
  • 43
    • 0035941194 scopus 로고    scopus 로고
    • Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1
    • Soetens, O., De Craene, J.O. & André, B. (2001) Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J. Biol. Chem. 276, 43949-43957.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43949-43957
    • Soetens, O.1    De Craene, J.O.2    André, B.3
  • 44
    • 0031867271 scopus 로고    scopus 로고
    • Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae
    • Springael, J.Y. & André, B. (1998) Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae. Mol. Biol. Cell 9, 1253-1263.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1253-1263
    • Springael, J.Y.1    André, B.2
  • 45
    • 84864586867 scopus 로고    scopus 로고
    • Molecular insights into the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1
    • Sudol, M., McDonald, C.B. & Farooq, A. (2012) Molecular insights into the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1. FEBS Lett. 586, 2795-2799.
    • (2012) FEBS Lett. , vol.586 , pp. 2795-2799
    • Sudol, M.1    McDonald, C.B.2    Farooq, A.3
  • 46
    • 0035912730 scopus 로고    scopus 로고
    • Protein misfolding and temperature up-shift cause G1 arrest via a common mechanism dependent on heat shock factor in Saccharomyces cerevisiae
    • Trotter, E.W., Berenfeld, L., Krause, S.A., Petsko, G.A. & Gray, J.V. (2001) Protein misfolding and temperature up-shift cause G1 arrest via a common mechanism dependent on heat shock factor in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 98, 7313-7318.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7313-7318
    • Trotter, E.W.1    Berenfeld, L.2    Krause, S.A.3    Petsko, G.A.4    Gray, J.V.5
  • 47
    • 0038141981 scopus 로고    scopus 로고
    • Construction of a set of Saccharomyces cerevisiae vectors designed for recombinational cloning
    • Van Mullem, V., Wery, M., De Bolle, X. & Vandenhaute, J. (2003) Construction of a set of Saccharomyces cerevisiae vectors designed for recombinational cloning. Yeast 20, 739-746.
    • (2003) Yeast , vol.20 , pp. 739-746
    • Van Mullem, V.1    Wery, M.2    De Bolle, X.3    Vandenhaute, J.4
  • 48
    • 33845671137 scopus 로고    scopus 로고
    • Regulation of G protein and mitogen-activated protein kinase signaling by ubiquitination: insights from model organisms
    • Wang, Y. & Dohlman, H.G. (2006) Regulation of G protein and mitogen-activated protein kinase signaling by ubiquitination: insights from model organisms. Circ. Res. 99, 1305-1314.
    • (2006) Circ. Res. , vol.99 , pp. 1305-1314
    • Wang, Y.1    Dohlman, H.G.2
  • 49
    • 0030006865 scopus 로고    scopus 로고
    • Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae
    • Yashiroda, H., Oguchi, T., Yasuda, Y., Toh-e, A. & Kikuchi, Y. (1996) Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae. Mol. Cell. Biol. 16, 3255-3263.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3255-3263
    • Yashiroda, H.1    Oguchi, T.2    Yasuda, Y.3    Toh-e, A.4    Kikuchi, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.