메뉴 건너뛰기




Volumn 289, Issue 46, 2014, Pages 32316-32326

Loss of vacuolar H+-ATPase activity in organelles signals ubiquitination and endocytosis of the yeast plasma membrane proton pump Pma1p

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME ACTIVITY; MEMBRANES; MOLECULAR BIOLOGY; PHYSIOLOGY; PROTONS; PUMPS; YEAST;

EID: 84911164053     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.574442     Document Type: Article
Times cited : (33)

References (51)
  • 2
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007) Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 6
    • 50649120655 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast
    • Martínez-Muñoz, G. A., and Kane, P. (2008) Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast. J. Biol. Chem. 283, 20309-20319
    • (2008) J. Biol. Chem. , vol.283 , pp. 20309-20319
    • Martínez-Muñoz, G.A.1    Kane, P.2
  • 7
    • 80051532058 scopus 로고    scopus 로고
    • Consequences of loss of Vph1 protein-containing vacuolar ATPases (V-ATPases) for overall cellular pH homeostasis
    • Tarsio, M., Zheng, H., Smardon, A. M., Martínez-Muñoz, G. A., and Kane, P. M. (2011) Consequences of loss of Vph1 protein-containing vacuolar ATPases (V-ATPases) for overall cellular pH homeostasis. J. Biol. Chem. 286, 28089-28096
    • (2011) J. Biol. Chem. , vol.286 , pp. 28089-28096
    • Tarsio, M.1    Zheng, H.2    Smardon, A.M.3    Martínez-Muñoz, G.A.4    Kane, P.M.5
  • 8
    • 79953171488 scopus 로고    scopus 로고
    • PH-dependent cargo sorting from the Golgi
    • Huang, C., and Chang, A. (2011) pH-dependent cargo sorting from the Golgi. J. Biol. Chem. 286, 10058-10065
    • (2011) J. Biol. Chem. , vol.286 , pp. 10058-10065
    • Huang, C.1    Chang, A.2
  • 9
    • 39649119621 scopus 로고    scopus 로고
    • The pH of the secretory pathway: Measurement, determinants, and regulation
    • Paroutis, P., Touret, N., and Grinstein, S. (2004) The pH of the secretory pathway: measurement, determinants, and regulation. Physiology 19, 207-215
    • (2004) Physiology , vol.19 , pp. 207-215
    • Paroutis, P.1    Touret, N.2    Grinstein, S.3
  • 11
    • 70649112359 scopus 로고    scopus 로고
    • Arrestin-mediated endocytosis of yeast plasma membrane transporters
    • Nikko, E., and Pelham, H. R. (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.2
  • 12
    • 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., and 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
  • 13
    • 77958046490 scopus 로고    scopus 로고
    • α-Arrestins Aly1 and Aly2 regulate intracellular trafficking in response to nutrient signaling
    • O'Donnell, A. F., Apffel, A., Gardner, R. G., and Cyert, M. S. (2010) α-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
  • 14
    • 81855183664 scopus 로고    scopus 로고
    • TORC1 regulates endocytosis via Npr1-mediated phosphoinhibition of a ubiquitin ligase adaptor
    • MacGurn, J. A., Hsu, P. C., Smolka, M. B., and Emr, S. D. (2011) TORC1 regulates endocytosis via Npr1-mediated phosphoinhibition of a ubiquitin ligase adaptor. Cell 147, 1104-1117
    • (2011) Cell , vol.147 , pp. 1104-1117
    • MacGurn, J.A.1    Hsu, P.C.2    Smolka, M.B.3    Emr, S.D.4
  • 16
    • 57049101734 scopus 로고    scopus 로고
    • Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1
    • Nikko, E., Sullivan, J. A., and Pelham, H. R. (2008) Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1. EMBO Rep. 9, 1216-1221
    • (2008) EMBO Rep , vol.9 , pp. 1216-1221
    • Nikko, E.1    Sullivan, J.A.2    Pelham, H.R.3
  • 17
    • 80052416211 scopus 로고    scopus 로고
    • Endocytosis of the aspartic acid/glutamic acid transporter Dip5 is triggered by substrate-dependent recruitment of the Rsp5 ubiquitin ligase via the arrestinlike protein Aly2
    • Hatakeyama, R., Kamiya, M., Takahara, T., and Maeda, T. (2010) Endocytosis of the aspartic acid/glutamic acid transporter Dip5 is triggered by substrate-dependent recruitment of the Rsp5 ubiquitin ligase via the arrestinlike protein Aly2. Mol. Cell. Biol. 30, 5598-5607
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 5598-5607
    • Hatakeyama, R.1    Kamiya, M.2    Takahara, T.3    Maeda, T.4
  • 18
    • 75749137330 scopus 로고    scopus 로고
    • Recruitment of the ESCRT machinery to a putative seven-transmembrane-domain receptor is mediated by an arrestin-related protein
    • Herrador, A., Herranz, S., Lara, D., and Vincent, O. (2010) Recruitment of the ESCRT machinery to a putative seven-transmembrane-domain receptor is mediated by an arrestin-related protein. Mol. Cell. Biol. 30, 897-907
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 897-907
    • Herrador, A.1    Herranz, S.2    Lara, D.3    Vincent, O.4
  • 19
    • 84878762528 scopus 로고    scopus 로고
    • A mechanism for protein monoubiquitination dependent on a trans-acting ubiquitin binding domain
    • Herrador, A., Léon, S., Haguenauer-Tsapis, R., and Vincent, O. (2013) A mechanism for protein monoubiquitination dependent on a trans-acting ubiquitin binding domain. J. Biol. Chem. 288, 16206-16211
    • (2013) J. Biol. Chem. , vol.288 , pp. 16206-16211
    • Herrador, A.1    Léon, S.2    Haguenauer-Tsapis, R.3    Vincent, O.4
  • 20
    • 84859561083 scopus 로고    scopus 로고
    • The signaling mechanism of ambient pH sensing and adaptation in yeast and fungi
    • Maeda, T. (2012) The signaling mechanism of ambient pH sensing and adaptation in yeast and fungi. FEBS J. 279, 1407-1413
    • (2012) FEBS J. , vol.279 , pp. 1407-1413
    • Maeda, T.1
  • 21
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991) Getting started with yeast. Methods Enzymol. 194, 3-21
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 22
    • 0035149694 scopus 로고    scopus 로고
    • Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis
    • Dunn, R., and 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
  • 23
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., St Jean, A., Woods, R. A., and Schiestl, R. H. (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20, 1425
    • (1992) Nucleic Acids Res , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 24
    • 77649335931 scopus 로고    scopus 로고
    • ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation
    • Teis, D., Saksena, S., Judson, B. L., and Emr, S. D. (2010) ESCRT-II coordinates the assembly of ESCRT-III filaments for cargo sorting and multivesicular body vesicle formation. EMBO J. 29, 871-883
    • (2010) EMBO J. , vol.29 , pp. 871-883
    • Teis, D.1    Saksena, S.2    Judson, B.L.3    Emr, S.D.4
  • 25
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, A., 3rd, Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J. R. (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, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 26
    • 34249959075 scopus 로고
    • A quick method for estimating the percentage of viable cells in a yeast population, using methylene blue staining
    • Painting, K., and Kirsop, B. (1990) A quick method for estimating the percentage of viable cells in a yeast population, using methylene blue staining. World J. Microbiol. Biotechnol. 6, 346-347
    • (1990) World J. Microbiol. Biotechnol. , vol.6 , pp. 346-347
    • Painting, K.1    Kirsop, B.2
  • 27
    • 0026039784 scopus 로고
    • +]ATPase involves phosphorylation during intracellular transport
    • +]ATPase involves phosphorylation during intracellular transport. J. Cell Biol. 115, 289-295
    • (1991) J. Cell Biol. , vol.115 , pp. 289-295
    • Chang, A.1    Slayman, C.W.2
  • 28
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat Methods 9, 671-675
    • (2012) Nat Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 30
    • 84876474749 scopus 로고    scopus 로고
    • Measurement of vacuolar and cytosolic pH in vivo in yeast cell suspensions
    • Diakov, T. T., Tarsio, M., and Kane, P. M. (2013) Measurement of vacuolar and cytosolic pH in vivo in yeast cell suspensions. J. Vis. Exp. 74, 50261
    • (2013) J. Vis. Exp. , vol.74 , pp. 50261
    • Diakov, T.T.1    Tarsio, M.2    Kane, P.M.3
  • 31
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin, D., and 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
  • 32
    • 84860332365 scopus 로고    scopus 로고
    • The β-arrestin-like protein Rim8 is hyperphosphorylated and complexes with Rim21 and Rim101 to promote adaptation to neutral-alkaline pH
    • Gomez-Raja, J., and Davis, D. A. (2012) The β-arrestin-like protein Rim8 is hyperphosphorylated and complexes with Rim21 and Rim101 to promote adaptation to neutral-alkaline pH. Eukaryot. Cell 11, 683-693
    • (2012) Eukaryot. Cell. , vol.11 , pp. 683-693
    • Gomez-Raja, J.1    Davis, D.A.2
  • 34
    • 0027455339 scopus 로고
    • End3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., Rohrer, J., Crausaz, F., and Riezman, H. (1993) end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120, 55-65
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 35
    • 0027997975 scopus 로고
    • +-ATPase-defective yeast: Identification of six new END genes
    • +-ATPase-defective yeast: identification of six new END genes. J. Cell Biol. 127, 373-386
    • (1994) J. Cell Biol. , vol.127 , pp. 373-386
    • Munn, A.L.1    Riezman, H.2
  • 36
    • 84879049031 scopus 로고    scopus 로고
    • The ART-Rsp5 ubiquitin ligase network comprises a plasma membrane quality control system that protects yeast cells from proteotoxic stress
    • Zhao, Y., Macgurn, J. A., Liu, M., and Emr, S. (2013) The ART-Rsp5 ubiquitin ligase network comprises a plasma membrane quality control system that protects yeast cells from proteotoxic stress. Elife 2, e00459
    • (2013) Elife , vol.2 , pp. e00459
    • Zhao, Y.1    Macgurn, J.A.2    Liu, M.3    Emr, S.4
  • 37
    • 0028117116 scopus 로고
    • Metabolic instability and constitutive endocytosis of STE6, the a-factor transporter of Saccharomyces cerevisiae
    • Berkower, C., Loayza, D., and Michaelis, S. (1994) Metabolic instability and constitutive endocytosis of STE6, the a-factor transporter of Saccharomyces cerevisiae. Mol. Biol. Cell 5, 1185-1198
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 1185-1198
    • Berkower, C.1    Loayza, D.2    Michaelis, S.3
  • 38
    • 0035979185 scopus 로고    scopus 로고
    • A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface
    • Gong, X., and Chang, A. (2001) A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface. Proc. Natl. Acad. Sci. U. S. A. 98, 9104-9109
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9104-9109
    • Gong, X.1    Chang, A.2
  • 39
    • 33845996190 scopus 로고    scopus 로고
    • Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, PMA1
    • Liu, Y., Sitaraman, S., and Chang, A. (2006) Multiple degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, PMA1. J. Biol. Chem. 281, 31457-31466
    • (2006) J. Biol. Chem. , vol.281 , pp. 31457-31466
    • Liu, Y.1    Sitaraman, S.2    Chang, A.3
  • 40
    • 2342450002 scopus 로고    scopus 로고
    • Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast
    • Pizzirusso, M., and Chang, A. (2004) Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast. Mol. Biol. Cell 15, 2401-2409
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 2401-2409
    • Pizzirusso, M.1    Chang, A.2
  • 41
    • 84891608907 scopus 로고    scopus 로고
    • +-ATPase have major impacts on protein conformation, trafficking, quality control, and function
    • +-ATPase have major impacts on protein conformation, trafficking, quality control, and function. Eukaryot. Cell 13, 43-52
    • (2014) Eukaryot. Cell. , vol.13 , pp. 43-52
    • Mason, A.B.1    Allen, K.E.2    Slayman, C.W.3
  • 42
    • 0036714075 scopus 로고    scopus 로고
    • Regulation of gene expression by ambient pH in filamentous fungi and yeasts
    • Peñalva, M. A., and Arst, H. N., Jr. (2002) Regulation of gene expression by ambient pH in filamentous fungi and yeasts. Microbiol. Mol. Biol. Rev. 66, 426-446
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 426-446
    • Peñalva, M.A.1    Arst, H.N.2
  • 43
    • 44949242315 scopus 로고    scopus 로고
    • Ambient pH gene regulation in fungi: Making connections
    • Peñalva, M. A., Tilburn, J., Bignell, E., and Arst, H. N., Jr. (2008) Ambient pH gene regulation in fungi: making connections. Trends Microbiol. 16, 291-300
    • (2008) Trends Microbiol , vol.16 , pp. 291-300
    • Peñalva, M.A.1    Tilburn, J.2    Bignell, E.3    Arst, H.N.4
  • 44
    • 9444284398 scopus 로고    scopus 로고
    • Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans
    • Xu, W., Smith, F. J., Jr., Subaran, R., and Mitchell, A. P. (2004) Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans. Mol. Biol. Cell 15, 5528-5537
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 5528-5537
    • Xu, W.1    Smith, F.J.2    Subaran, R.3    Mitchell, A.P.4
  • 46
    • 84876305060 scopus 로고    scopus 로고
    • A novel single-cell screening platform reveals proteome plasticity during yeast stress responses
    • Breker, M., Gymrek, M., and Schuldiner, M. (2013) A novel single-cell screening platform reveals proteome plasticity during yeast stress responses. J. Cell Biol. 200, 839-850
    • (2013) J. Cell Biol. , vol.200 , pp. 839-850
    • Breker, M.1    Gymrek, M.2    Schuldiner, M.3
  • 47
    • 84902660212 scopus 로고    scopus 로고
    • Specific α-arrestins negatively regulate Saccharomyces cerevisiae pheromone response by down-modulating the G-protein-coupled receptor Ste2
    • Alvaro, C. G., O'Donnell, A. F., Prosser, D. C., Augustine, A. A., Goldman, A., Brodsky, J. L., Cyert, M. S., Wendland, B., and Thorner, J. (2014) Specific α-arrestins negatively regulate Saccharomyces cerevisiae pheromone response by down-modulating the G-protein-coupled receptor Ste2. Mol. Cell. Biol. 34, 2660-2681
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 2660-2681
    • Alvaro, C.G.1    O'Donnell, A.F.2    Prosser, D.C.3    Augustine, A.A.4    Goldman, A.5    Brodsky, J.L.6    Cyert, M.S.7    Wendland, B.8    Thorner, J.9
  • 48
    • 34147107933 scopus 로고    scopus 로고
    • Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress
    • Milgrom, E., Diab, H., Middleton, F., and Kane, P. M. (2007) Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. J. Biol. Chem. 282, 7125-7136
    • (2007) J. Biol. Chem. , vol.282 , pp. 7125-7136
    • Milgrom, E.1    Diab, H.2    Middleton, F.3    Kane, P.M.4
  • 50
    • 84863289864 scopus 로고    scopus 로고
    • +-ATPase works in parallel with the HOG pathway to adapt Saccharomyces cerevisiae cells to osmotic stress
    • +-ATPase works in parallel with the HOG pathway to adapt Saccharomyces cerevisiae cells to osmotic stress. Eukaryot Cell 11, 282-291
    • (2012) Eukaryot Cell , vol.11 , pp. 282-291
    • Li, S.C.1    Diakov, T.T.2    Rizzo, J.M.3    Kane, P.M.4
  • 51
    • 78649673808 scopus 로고    scopus 로고
    • + exchanger 1 ubiquitylation, endocytosis, and function
    • + exchanger 1 ubiquitylation, endocytosis, and function. J. Biol. Chem. 285, 38293-38303
    • (2010) J. Biol. Chem. , vol.285 , pp. 38293-38303
    • Simonin, A.1    Fuster, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.