메뉴 건너뛰기




Volumn 24, Issue 11, 2013, Pages 1793-1805

Proteome-wide measurement of protein half-lives and translation rates in vasopressin-sensitive collecting duct cells

Author keywords

[No Author keywords available]

Indexed keywords

17BETA HYDROXYSTEROID DEHYDROGENASE 4; AQUAPORIN 2; DESMOPRESSIN; GELSOLIN; GLUTATHIONE TRANSFERASE; HEAT SHOCK PROTEIN 70; LIPOCORTIN 2; MYOSIN LIGHT CHAIN KINASE; NISCHARIN; NUCLEAR RNA EXPORT FACTOR 1; PROTEIN; PROTEIN AKAP12; PROTEIN MAL2; PROTEOME; RNA BINDING PROTEIN; STABLE ISOTOPE; TESTOSTERONE 17BETA DEHYDROGENASE; UNCLASSIFIED DRUG; VASOPRESSIN;

EID: 84887052100     PISSN: 10466673     EISSN: 15333450     Source Type: Journal    
DOI: 10.1681/ASN.2013030279     Document Type: Article
Times cited : (94)

References (40)
  • 1
    • 0028889112 scopus 로고
    • Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane
    • Nielsen S, Chou CL, Marples D, Christensen E.I., Kishore BK, Knepper MA: Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. Proc Natl Acad Sci U S A 92: 1013-1017, 1995
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1013-1017
    • Nielsen, S.1    Chou, C.L.2    Marples, D.3    Christensen, E.I.4    Kishore, B.K.5    Knepper, M.A.6
  • 2
    • 0026637836 scopus 로고
    • Kinetics of urea and water permeability activation by vasopressin in rat terminal IMCD
    • Wall SM, Han JS, Chou C.L., Knepper MA: Kinetics of urea and water permeability activation by vasopressin in rat terminal IMCD. Am J Physiol 262: F989-F998, 1992
    • (1992) Am J Physiol , vol.262
    • Wall, S.M.1    Han, J.S.2    Chou, C.L.3    Knepper, M.A.4
  • 3
  • 4
    • 0029775026 scopus 로고    scopus 로고
    • Quantitation of aquaporin-2 abundance in microdissected collecting ducts: Axial distribution and control by AVP
    • Kishore BK, Terris JM, Knepper MA: Quantitation of aquaporin-2 abundance in microdissected collecting ducts: Axial distribution and control by AVP. Am J Physiol 271: F62-F70, 1996
    • (1996) Am J Physiol , vol.271
    • Kishore, B.K.1    Terris, J.M.2    Knepper, M.A.3
  • 8
    • 33645491677 scopus 로고    scopus 로고
    • Adenylate cyclase-coupled vasopressin receptor activates AQP2 promoter via a dual effect on CRE and AP1 elements
    • Yasui M, Zelenin SM, Celsi G, Aperia A: Adenylate cyclase-coupled vasopressin receptor activates AQP2 promoter via a dual effect on CRE and AP1 elements. Am J Physiol 272: F443-F450, 1997
    • (1997) Am J Physiol , vol.272
    • Yasui, M.1    Zelenin, S.M.2    Celsi, G.3    Aperia, A.4
  • 9
    • 0029785780 scopus 로고    scopus 로고
    • CAMP motifs regulating transcription in the aquaporin 2 gene
    • Hozawa S, Holtzman EJ, Ausiello DA: cAMP motifs regulating transcription in the aquaporin 2 gene. Am J Physiol 270: C1695-C1702, 1996
    • (1996) Am J Physiol , vol.270
    • Hozawa, S.1    Holtzman, E.J.2    Ausiello, D.A.3
  • 13
    • 78651066261 scopus 로고    scopus 로고
    • Quantitative protein and mRNA profiling shows selective post-transcriptional control of protein expression by vasopressin in kidney cells
    • Khositseth S, Pisitkun T, Slentz D.H., Wang G., Hoffert JD, Knepper MA, Yu MJ: Quantitative protein and mRNA profiling shows selective post-transcriptional control of protein expression by vasopressin in kidney cells. Mol Cell Proteomics 10: 004036, 2011
    • (2011) Mol Cell Proteomics , vol.10 , pp. 004036
    • Khositseth, S.1    Pisitkun, T.2    Slentz, D.H.3    Wang, G.4    Hoffert, J.D.5    Knepper, M.A.6    Yu, M.J.7
  • 14
    • 60849097304 scopus 로고    scopus 로고
    • Turnover of the human proteome: Determination of protein intracellular stability by dynamic SILAC
    • Doherty MK, Hammond DE, Clague M.J., Gaskell SJ, Beynon RJ: Turnover of the human proteome: Determination of protein intracellular stability by dynamic SILAC. J Proteome Res 8: 104-112, 2009
    • (2009) J Proteome Res , vol.8 , pp. 104-112
    • Doherty, M.K.1    Hammond, D.E.2    Clague, M.J.3    Gaskell, S.J.4    Beynon, R.J.5
  • 15
    • 59449085150 scopus 로고    scopus 로고
    • Global analysis of cellularproteintranslationbypulsed SILAC
    • Schwanhäusser B., Gossen M, Dittmar G., Selbach M: Global analysis of cellularproteintranslationbypulsed SILAC. Proteomics 9: 205-209, 2009
    • (2009) Proteomics , vol.9 , pp. 205-209
    • Schwanhäusser, B.1    Gossen, M.2    Dittmar, G.3    Selbach, M.4
  • 17
    • 1642494672 scopus 로고    scopus 로고
    • Glycosylation is important for cell surface expression of the water channel aquaporin-2 but is not essential for tetramerization in the endoplasmic reticulum
    • DOI 10.1074/jbc.M310767200
    • Hendriks G, Koudijs M, van Balkom BW, Oorschot V, Klumperman J, Deen P.M., van der Sluijs P: Glycosylation is important for cell surface expression of the water channel aquaporin-2 but is not essential for tetramerization in the endoplasmic reticulum. J Biol Chem 279: 2975-2983, 2004 (Pubitemid 38114290)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2975-2983
    • Hendriks, G.1    Koudijs, M.2    Van Balkom, B.W.M.3    Oorschot, V.4    Klumperman, J.5    Deen, P.M.T.6    Van Der Sluijs, P.7
  • 20
    • 0037763721 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling gene expression mediated by the antioxidant response element
    • DOI 10.1146/annurev.pharmtox.43.100901.140229
    • Nguyen T, Sherratt PJ, Pickett CB: Regulatory mechanisms controlling gene expression mediated by the antioxidant response element. Annu Rev Pharmacol Toxicol 43: 233-260, 2003 (Pubitemid 37372641)
    • (2003) Annual Review of Pharmacology and Toxicology , vol.43 , pp. 233-260
    • Nguyen, T.1    Sherratt, P.J.2    Pickett, C.B.3
  • 21
    • 0036570346 scopus 로고    scopus 로고
    • Glutamate-cysteine ligase modifier subunit: Mouse Gclm gene structure and regulation by agents that cause oxidative stress
    • DOI 10.1016/S0006-2952(02)00897-3, PII S0006295202008973
    • Solis WA, Dalton TP, Dieter M.Z., Freshwater S., Harrer JM, He L, Shertzer HG, Nebert DW: Glutamate-cysteine ligase modifier subunit: Mouse Gclm gene structure and regulation by agents that cause oxidative stress. Biochem Pharmacol 63: 1739-1754, 2002 (Pubitemid 34458012)
    • (2002) Biochemical Pharmacology , vol.63 , Issue.9 , pp. 1739-1754
    • Solis, W.A.1    Dalton, T.P.2    Dieter, M.Z.3    Freshwater, S.4    Harrer, J.M.5    He, L.6    Shertzer, H.G.7    Nebert, D.W.8
  • 22
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradationto the rescue
    • Brodsky JL: Cleaning up: ER-associated degradationto the rescue. Cell 151: 1163-1167, 2012
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 23
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V, McEwan DG, Novak I, Dikic I: A role for ubiquitin in selective autophagy. Mol Cell 34: 259-269, 2009
    • (2009) Mol Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 24
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D, Kumar S: Physiological functions of the HECT family of ubiquitin ligases. Nat Rev Mol Cell Biol 10: 398-409, 2009
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 25
    • 78649664485 scopus 로고    scopus 로고
    • Structural insights into histone lysine demethylation
    • Hou H, Yu H: Structural insights into histone lysine demethylation. Curr Opin Struct Biol 20: 739-748, 2010
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 739-748
    • Hou, H.1    Yu, H.2
  • 26
    • 79955061701 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: Signaling pathways and biological functions
    • Lal M, Caplan M: Regulated intramembrane proteolysis: Signaling pathways and biological functions. Physiology (Bethesda) 26: 34-44, 2011
    • (2011) Physiology (Bethesda) , vol.26 , pp. 34-44
    • Lal, M.1    Caplan, M.2
  • 28
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A, Finley D, Varshavsky A: In vivo half-life of a protein is a function of its amino-terminal residue. Science 234: 179-186, 1986 (Pubitemid 17186094)
    • (1986) Science , vol.234 , Issue.4773 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 29
    • 0024562943 scopus 로고
    • The degradation signal in a short-lived protein
    • DOI 10.1016/0092-8674(89)90635-1
    • Bachmair A, Varshavsky A: The degradation signal in a short-lived protein. Cell 56: 1019-1032, 1989 (Pubitemid 19091014)
    • (1989) Cell , vol.56 , Issue.6 , pp. 1019-1032
    • Bachmair, A.1    Varshavsky, A.2
  • 30
    • 77149120798 scopus 로고    scopus 로고
    • N-terminalacetylation of cellular proteins creates specific degradation signals
    • Hwang CS, Shemorry A, Varshavsky A: N-terminalacetylation of cellular proteins creates specific degradation signals. Science 327: 973-977, 2010
    • (2010) Science , vol.327 , pp. 973-977
    • Hwang, C.S.1    Shemorry, A.2    Varshavsky, A.3
  • 31
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S, Wells R, Rechsteiner M: Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis. Science 234: 364-368, 1986 (Pubitemid 17181385)
    • (1986) Science , vol.234 , Issue.4774 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 32
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JR III: An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5: 976-989, 1994
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 33
    • 27544511899 scopus 로고    scopus 로고
    • InsPecT: Identification of posttranslationally modified peptides from tandem mass spectra
    • DOI 10.1021/ac050102d
    • Tanner S, Shu H, Frank A., Wang LC, Zandi E, Mumby M, Pevzner P.A., Bafna V: InsPecT: Identification of posttranslationally modified peptides from tandem mass spectra. Anal Chem 77: 4626-4639, 2005 (Pubitemid 41542287)
    • (2005) Analytical Chemistry , vol.77 , Issue.14 , pp. 4626-4639
    • Tanner, S.1    Shu, H.2    Frank, A.3    Wang, L.-C.4    Zandi, E.5    Mumby, M.6    Pevzner, P.A.7    Bafna, V.8
  • 35
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • DOI 10.1038/nmeth1019, PII NMETH1019
    • Elias JE, Gygi SP: Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 4: 207-214, 2007 (Pubitemid 46358868)
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 36
    • 76549108580 scopus 로고    scopus 로고
    • Proteomic profiling of nuclei from native renal inner medullary collecting duct cells using LC-MS/MS
    • Tchapyjnikov D, Li Y, Pisitkun T., Hoffert JD, Yu MJ, Knepper MA: Proteomic profiling of nuclei from native renal inner medullary collecting duct cells using LC-MS/MS. Physiol Genomics 40: 167-183, 2010
    • (2010) Physiol Genomics , vol.40 , pp. 167-183
    • Tchapyjnikov, D.1    Li, Y.2    Pisitkun, T.3    Hoffert, J.D.4    Yu, M.J.5    Knepper, M.A.6
  • 39
    • 33845873289 scopus 로고    scopus 로고
    • Interactive Tree Of Life (iTOL): An online tool for phylogenetic tree display and annotation
    • DOI 10.1093/bioinformatics/btl529
    • Letunic I, Bork P: Interactive Tree Of Life (iTOL): An online tool for phylogenetic tree display and annotation. Bioinformatics 23: 127-128, 2007 (Pubitemid 46017867)
    • (2007) Bioinformatics , vol.23 , Issue.1 , pp. 127-128
    • Letunic, I.1    Bork, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.