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Volumn 9, Issue 3, 2010, Pages 1510-1521

Proteomic identification of Hsc70 as a mediator of RGS9-2 degradation by in vivo interactome analysis

Author keywords

Basal ganglia; Drug addiction; Heat shock proteins; Neuronal signaling; Protein degradation; Protein protein interactions; Quantitative proteomics; Regulator of G protein signaling

Indexed keywords

HEAT SHOCK COGNATE PROTEIN 70; OPIATE; RGS2 PROTEIN;

EID: 77949866108     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr901022m     Document Type: Article
Times cited : (12)

References (51)
  • 1
    • 68549106027 scopus 로고    scopus 로고
    • The R7 RGS protein family: Multi-subunit regulators of neuronal G protein signaling
    • Anderson, G. R.; Posokhova, E.; Martemyanov, K. A. The R7 RGS protein family: multi-subunit regulators of neuronal G protein signaling. Cell Biochem. Biophys. 2009, 54, 33-46.
    • (2009) Cell Biochem. Biophys. , vol.54 , pp. 33-46
    • Anderson, G.R.1    Posokhova, E.2    Martemyanov, K.A.3
  • 3
    • 61349171291 scopus 로고    scopus 로고
    • RGS9-2: Probing an intracellular modulator of behavior as a drug target
    • Traynor, J. R.; Terzi, D.; Caldarone, B. J.; Zachariou, V. RGS9-2: probing an intracellular modulator of behavior as a drug target. Trends Pharmacol. Sci. 2009, 30, 105-111
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 105-111
    • Traynor, J.R.1    Terzi, D.2    Caldarone, B.J.3    Zachariou, V.4
  • 4
    • 0034602868 scopus 로고    scopus 로고
    • Co-expression of Gbeta5 enhances the function of two Ggamma subunit-like domain-containing regulators of G protein signaling proteins
    • Kovoor, A.; Chen, C. K.; He, W.; Wensel, T. G.; Simon, M. I.; Lester, H. A. Co-expression of Gbeta5 enhances the function of two Ggamma subunit-like domain-containing regulators of G protein signaling proteins. J. Biol. Chem. 2000, 275, 3397-3402
    • (2000) J. Biol. Chem. , vol.275 , pp. 3397-3402
    • Kovoor, A.1    Chen, C.K.2    He, W.3    Wensel, T.G.4    Simon, M.I.5    Lester, H.A.6
  • 5
    • 14044273637 scopus 로고    scopus 로고
    • R7BP, a novel neuronal protein interacting with RGS proteins of the R7 family
    • Martemyanov, K. A.; Yoo, P. J.; Skiba, N. P.; Arshavsky, V. Y. R7BP, a novel neuronal protein interacting with RGS proteins of the R7 family. J. Biol. Chem. 2005, 280, 5133-5136.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5133-5136
    • Martemyanov, K.A.1    Yoo, P.J.2    Skiba, N.P.3    Arshavsky, V.Y.4
  • 7
    • 22344431893 scopus 로고    scopus 로고
    • Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family
    • Drenan, R. M.; Doupnik, C. A.; Boyle, M. P.; Muglia, L. J.; Huettner, J. E.; Linder, M. E.; Blumer, K. J. Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family. J. Cell Biol. 2005, 169, 623-633.
    • (2005) J. Cell Biol. , vol.169 , pp. 623-633
    • Drenan, R.M.1    Doupnik, C.A.2    Boyle, M.P.3    Muglia, L.J.4    Huettner, J.E.5    Linder, M.E.6    Blumer, K.J.7
  • 8
    • 33947492531 scopus 로고    scopus 로고
    • The membrane anchor R7BP controls the proteolytic stability of the striatal specific RGS protein, RGS9-2
    • Anderson, G. R.; Semenov, A.; Song, J. H.; Martemyanov, K. A. The membrane anchor R7BP controls the proteolytic stability of the striatal specific RGS protein, RGS9-2. J. Biol. Chem. 2007, 282, 4772-4781.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4772-4781
    • Anderson, G.R.1    Semenov, A.2    Song, J.H.3    Martemyanov, K.A.4
  • 9
    • 38449085211 scopus 로고    scopus 로고
    • Expression and localization of RGS9-2/G 5/R7BP complex in vivo is set by dynamic control of its constitutive degradation by cellular cysteine proteases
    • Anderson, G. R.; Lujan, R.; Semenov, A.; Pravetoni, M.; Posokhova, E. N.; Song, J. H.; Uversky, V.; Chen, C. K.; Wickman, K.; Martemyanov, K. A. Expression and localization of RGS9-2/G 5/R7BP complex in vivo is set by dynamic control of its constitutive degradation by cellular cysteine proteases. J. Neurosci. 2007, 27, 14117-14127.
    • (2007) J. Neurosci. , vol.27 , pp. 14117-14127
    • Anderson, G.R.1    Lujan, R.2    Semenov, A.3    Pravetoni, M.4    Posokhova, E.N.5    Song, J.H.6    Uversky, V.7    Chen, C.K.8    Wickman, K.9    Martemyanov, K.A.10
  • 10
    • 66349138500 scopus 로고    scopus 로고
    • Changes in striatal signaling induce remodeling of RGS complexes containing Gbeta5 and R7BP subunits
    • Anderson, G. R.; Lujan, R.; Martemyanov, K. A. Changes in striatal signaling induce remodeling of RGS complexes containing Gbeta5 and R7BP subunits. Mol. Cell. Biol. 2009, 29, 3033-3044.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3033-3044
    • Anderson, G.R.1    Lujan, R.2    Martemyanov, K.A.3
  • 11
    • 0033025069 scopus 로고    scopus 로고
    • RGS mRNA expression in rat striatum: Modulation by dopamine receptors and effects of repeated amphetamine administration
    • Burchett, S. A.; Bannon, M. J.; Granneman, J. G. RGS mRNA expression in rat striatum: modulation by dopamine receptors and effects of repeated amphetamine administration. J. Neurochem. 1999, 72, 1529-1533.
    • (1999) J. Neurochem. , vol.72 , pp. 1529-1533
    • Burchett, S.A.1    Bannon, M.J.2    Granneman, J.G.3
  • 14
    • 0035813162 scopus 로고    scopus 로고
    • RGS9-Gbeta5 substrate selectivity in photoreceptors - Opposing effects of constituent domains yield high affinity of RGS interaction with the G proteineffector complex
    • Skiba, N. P.; Martemyanov, K. A.; Elfenbein, A.; Hopp, J. A.; Bohm, A.; Simonds, W. F.; Arshavsky, V. Y. RGS9-Gbeta5 substrate selectivity in photoreceptors - Opposing effects of constituent domains yield high affinity of RGS interaction with the G proteineffector complex. J. Biol. Chem. 2001, 276, 37365-37372.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37365-37372
    • Skiba, N.P.1    Martemyanov, K.A.2    Elfenbein, A.3    Hopp, J.A.4    Bohm, A.5    Simonds, W.F.6    Arshavsky, V.Y.7
  • 15
    • 0038198731 scopus 로고    scopus 로고
    • Specificity of G protein-RGS protein recognition is regulated by affinity adapters
    • Martemyanov, K. A.; Hopp, J. A.; Arshavsky, V. Y. Specificity of G protein-RGS protein recognition is regulated by affinity adapters. Neuron 2003, 38, 857-862.
    • (2003) Neuron , vol.38 , pp. 857-862
    • Martemyanov, K.A.1    Hopp, J.A.2    Arshavsky, V.Y.3
  • 16
    • 0034598728 scopus 로고    scopus 로고
    • Slowed recovery of rod photoresponse in mice lacking the GTPase accelerating protein RGS9-1
    • Chen, C. K.; Burns, M. E.; He, W.; Wensel, T. G.; Baylor, D. A.; Simon, M. I. Slowed recovery of rod photoresponse in mice lacking the GTPase accelerating protein RGS9-1. Nature 2000, 403, 557-560.
    • (2000) Nature , vol.403 , pp. 557-560
    • Chen, C.K.1    Burns, M.E.2    He, W.3    Wensel, T.G.4    Baylor, D.A.5    Simon, M.I.6
  • 17
    • 34548178909 scopus 로고    scopus 로고
    • Ingel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A.; Tomas, H.; Havlis, J.; Olsen, J. V.; Mann, M. Ingel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 2006, 1, 2856-2860.
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 18
    • 30344485673 scopus 로고    scopus 로고
    • Exploiting heterogeneous sequence properties improves prediction of protein disorder
    • Obradovic, Z.; Peng, K.; Vucetic, S.; Radivojac, P.; Dunker, A. K. Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins 2005, 61 (7), 176-182.
    • (2005) Proteins , vol.61 , Issue.7 , pp. 176-182
    • Obradovic, Z.1    Peng, K.2    Vucetic, S.3    Radivojac, P.4    Dunker, A.K.5
  • 20
    • 33646269941 scopus 로고    scopus 로고
    • A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies
    • Zieske, L. R. A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies. J. Exp. Bot. 2006, 57, 1501-1508.
    • (2006) J. Exp. Bot. , vol.57 , pp. 1501-1508
    • Zieske, L.R.1
  • 21
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov, I. V.; Seymour, S. L.; Patel, A. A.; Loboda, A.; Tang, W. H.; Keating, S. P.; Hunter, C. L.; Nuwaysir, L. M.; Schaeffer, D. A. The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 2007, 6, 1638-1655.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 22
    • 70449412362 scopus 로고    scopus 로고
    • ITRAQ underestimation in simple and complex mixtures: "The good, the bad and the ugly
    • Ow, S. Y.; Salim, M.; Noirel, J.; Evans, C.; Rehman, I.; Wright, P. C. iTRAQ underestimation in simple and complex mixtures: "the good, the bad and the ugly. J. Proteome Res. 2009, 8, 5347-5355.
    • (2009) J. Proteome Res. , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 23
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice, J. F. Chaperone-mediated autophagy. Autophagy 2007, 3, 295-299.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.F.1
  • 24
    • 1242291789 scopus 로고    scopus 로고
    • A link between the chaperone and proteasome systems
    • McDonough, H.; Patterson, C. CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 2003, 8, 303-308.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Chip, P.C.2
  • 25
    • 33745023775 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy in aging and disease
    • Massey, A. C.; Zhang, C.; Cuervo, A. M. Chaperone-mediated autophagy in aging and disease. Curr. Top. Dev. Biol. 2006, 73, 205-235.
    • (2006) Curr. Top. Dev. Biol. , vol.73 , pp. 205-235
    • Massey, A.C.1    Zhang, C.2    Cuervo, A.M.3
  • 27
    • 33846027092 scopus 로고    scopus 로고
    • The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family
    • Haag Breese, E.; Uversky, V. N.; Georgiadis, M. M.; Harrington, M. A. The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family. DNA Cell Biol 2006, 25, 704-714.
    • (2006) DNA Cell Biol , vol.25 , pp. 704-714
    • Haag Breese, E.1    Uversky, V.N.2    Georgiadis, M.M.3    Harrington, M.A.4
  • 28
    • 40349096246 scopus 로고    scopus 로고
    • Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure
    • Song, J.; Guo, L. W.; Muradov, H.; Artemyev, N. O.; Ruoho, A. E.; Markley, J. L. Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 1505-1510.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1505-1510
    • Song, J.1    Guo, L.W.2    Muradov, H.3    Artemyev, N.O.4    Ruoho, A.E.5    Markley, J.L.6
  • 30
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • Rohde, M.; Daugaard, M.; Jensen, M. H.; Helin, K.; Nylandsted, J.; Jaattela, M. Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev. 2005, 19, 570-582.
    • (2005) Genes Dev. , vol.19 , pp. 570-582
    • Rohde, M.1    Daugaard, M.2    Jensen, M.H.3    Helin, K.4    Nylandsted, J.5    Jaattela, M.6
  • 31
    • 0035799707 scopus 로고    scopus 로고
    • Lethality and centrality in protein networks
    • Jeong, H.; Mason, S. P.; Barabasi, A. L.; Oltvai, Z. N. Lethality and centrality in protein networks. Nature 2001, 411, 41-42
    • (2001) Nature , vol.411 , pp. 41-42
    • Jeong, H.1    Mason, S.P.2    Barabasi, A.L.3    Oltvai, Z.N.4
  • 34
    • 34347368461 scopus 로고    scopus 로고
    • A more complete, complexed and structured interactome
    • Devos, D.; Russell, R. B. A more complete, complexed and structured interactome. Curr. Opin. Struct. Biol. 2007, 17, 370-377
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 370-377
    • Devos, D.1    Russell, R.B.2
  • 35
    • 43849083417 scopus 로고    scopus 로고
    • Sticking together? Falling apart? Exploring the dynamics of the interactome
    • Wilkins, M. R.; Kummerfeld, S. K. Sticking together? Falling apart? Exploring the dynamics of the interactome. Trends Biochem. Sci. 2008, 33, 195-200.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 195-200
    • Wilkins, M.R.1    Kummerfeld, S.K.2
  • 36
    • 69649098398 scopus 로고    scopus 로고
    • Proteomic characterization of the dynamic KSR-2 interactome, a signaling scaffold complex in MAPK pathway
    • Liu, L.; Channavajhala, P. L.; Rao, V. R.; Moutsatsos, I.; Wu, L.; Zhang, Y.; Lin, L. L.; Qiu, Y. Proteomic characterization of the dynamic KSR-2 interactome, a signaling scaffold complex in MAPK pathway. Biochim. Biophys. Acta 2009, 1794, 1485-1495
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1485-1495
    • Liu, L.1    Channavajhala, P.L.2    Rao, V.R.3    Moutsatsos, I.4    Wu, L.5    Zhang, Y.6    Lin, L.L.7    Qiu, Y.8
  • 37
    • 70349976548 scopus 로고    scopus 로고
    • Differential proteomic analysis of STAT6 knockout mice reveals new regulatory function in liver lipid homeostasis
    • Iff, J.; Wang, W.; Sajic, T.; Oudry, N.; Gueneau, E.; Hopfgartner, G.; Varesio, E.; Szanto, I. Differential Proteomic Analysis of STAT6 Knockout Mice Reveals New Regulatory Function in Liver Lipid Homeostasis. J. Proteome Res. 2009, 8, 4511-4524.
    • (2009) J. Proteome Res. , vol.8 , pp. 4511-4524
    • Iff, J.1    Wang, W.2    Sajic, T.3    Oudry, N.4    Gueneau, E.5    Hopfgartner, G.6    Varesio, E.7    Szanto, I.8
  • 38
    • 65249153042 scopus 로고    scopus 로고
    • Proteomic analysis of an 7 nicotinic acetylcholine receptor interactome
    • Paulo, J.; Brucker, W.; Hawrot, E. Proteomic Analysis of an 7 Nicotinic Acetylcholine Receptor Interactome. J Proteome Res 2009, 8, 1849-1858.
    • (2009) J Proteome Res , vol.8 , pp. 1849-1858
    • Paulo, J.1    Brucker, W.2    Hawrot, E.3
  • 43
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • Daugaard, M.; Rohde, M.; Jaattela, M. The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions. FEBS Lett. 2007, 581, 3702-3710.
    • (2007) FEBS Lett. , vol.581 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 44
    • 33644872508 scopus 로고    scopus 로고
    • Characterization of rapidly degraded polypeptides in mammalian cells reveals a novel layer of nascent protein quality control
    • Qian, S. B.; Princiotta, M. F.; Bennink, J. R.; Yewdell, J. W. Characterization of rapidly degraded polypeptides in mammalian cells reveals a novel layer of nascent protein quality control. J. Biol. Chem. 2006, 281, 392-400.
    • (2006) J. Biol. Chem. , vol.281 , pp. 392-400
    • Qian, S.B.1    Princiotta, M.F.2    Bennink, J.R.3    Yewdell, J.W.4
  • 45
    • 4344673498 scopus 로고    scopus 로고
    • Mechanisms of chaperone-mediated autophagy
    • Majeski, A. E.; Dice, J. F. Mechanisms of chaperone-mediated autophagy. Int. J. Biochem. Cell Biol. 2004, 36, 2435-2444.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2435-2444
    • Majeski, A.E.1    Dice, J.F.2
  • 47
    • 66849109240 scopus 로고    scopus 로고
    • The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
    • Kramer, G.; Boehringer, D.; Ban, N.; Bukau, B. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nat. Struct. Mol. Biol. 2009, 16, 589-597.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 589-597
    • Kramer, G.1    Boehringer, D.2    Ban, N.3    Bukau, B.4
  • 48
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 2001, 70, 603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 49
    • 22444438841 scopus 로고    scopus 로고
    • Ribosomes catch Hsp70s
    • Bukau, B. Ribosomes catch Hsp70s. Nat. Struct. Mol. Biol. 2005, 12, 472-473.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 472-473
    • Bukau, B.1
  • 50
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang, P.; MacRae, T. H. Molecular chaperones and the cytoskeleton. J. Cell Sci. 1997, 110 (Pt 13), 1431-1440.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 13 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 51
    • 0030272844 scopus 로고    scopus 로고
    • The compartmentalization of protein synthesis: Importance of cytoskeleton and role in mRNA targeting
    • Hovland, R.; Hesketh, J. E.; Pryme, I. F. The compartmentalization of protein synthesis: importance of cytoskeleton and role in mRNA targeting. Int. J. Biochem. Cell Biol. 1996, 28, 1089-1105.
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 1089-1105
    • Hovland, R.1    Hesketh, J.E.2    Pryme, I.F.3


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