메뉴 건너뛰기




Volumn 383, Issue 2, 2004, Pages 237-248

Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes

Author keywords

Caveolae; Human adipocyte; MS; PEST sequence; Polymerase I and transcript release factor (PTRF); Proteolysis

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; CELLS; CYTOLOGY; FLUORESCENCE; MASS SPECTROMETRY; MICROSCOPIC EXAMINATION;

EID: 7444221690     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040647     Document Type: Article
Times cited : (136)

References (51)
  • 1
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: From cell biology to animal physiology
    • Razani, B., Woodman, S. E. and Lisanti, M. P. (2002) Caveolae: from cell biology to animal physiology. Pharmacol. Rev. 54, 431-467
    • (2002) Pharmacol. Rev. , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 4
    • 0031765341 scopus 로고    scopus 로고
    • Role of plasmalemmal caveolae in signal transduction
    • Shaul, P. W. and Anderson, R. G. (1998) Role of plasmalemmal caveolae in signal transduction. Am. J. Physiol. 275, 843-851
    • (1998) Am. J. Physiol. , vol.275 , pp. 843-851
    • Shaul, P.W.1    Anderson, R.G.2
  • 9
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin
    • Fra, A. M., Williamson, E., Simons, K. and Parton, R. G. (1995) De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin. Proc. Natl. Acad. Sci. U.S.A. 92, 8655-8659
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8655-8659
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 12
    • 0028820041 scopus 로고
    • A detergent-free method for purifying caveolae membrane from tissue culture cells
    • Smart, E. J., Ying, Y. S., Mineo, C. and Anderson, R. G. (1995) A detergent-free method for purifying caveolae membrane from tissue culture cells. Proc. Natl. Acad. Sci. U.S.A. 92, 10104-10108
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.S.2    Mineo, C.3    Anderson, R.G.4
  • 13
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains
    • Song, K. S., Li, S., Okamoto, T., Quilliam, L. A., Sargiacomo, M. and Lisanti, M. P. (1996) Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains. J. Biol. Chem. 271, 9690-9697
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 14
    • 0037705362 scopus 로고    scopus 로고
    • Immunopurification and characterization of rat adipocyte caveolae suggest their dissociation from insulin signaling
    • Souto, R. P., Vallega, G., Wharton, J., Vinten, J., Tranum-Jensen, J. and Pilch, P. F. (2003) Immunopurification and characterization of rat adipocyte caveolae suggest their dissociation from insulin signaling. J. Biol. Chem. 278, 18321-18329
    • (2003) J. Biol. Chem. , vol.278 , pp. 18321-18329
    • Souto, R.P.1    Vallega, G.2    Wharton, J.3    Vinten, J.4    Tranum-Jensen, J.5    Pilch, P.F.6
  • 15
    • 0035433580 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains
    • von Haller, P. D., Donohoe, S., Goodlett, D. R., Aebersold, R. and Watts, J. D. (2001) Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains. Proteomics 1, 1010-1021
    • (2001) Proteomics , vol.1 , pp. 1010-1021
    • Von Haller, P.D.1    Donohoe, S.2    Goodlett, D.R.3    Aebersold, R.4    Watts, J.D.5
  • 16
    • 0347298692 scopus 로고    scopus 로고
    • Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering
    • Bini, L., Pacini, S., Liberatori, S., Valensin, S., Pellegrini, M., Raggiaschi, R., Pallini, V. and Baldari, C. T. (2003) Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering. Biochem. J. 369, 301-309
    • (2003) Biochem. J. , vol.369 , pp. 301-309
    • Bini, L.1    Pacini, S.2    Liberatori, S.3    Valensin, S.4    Pellegrini, M.5    Raggiaschi, R.6    Pallini, V.7    Baldari, C.T.8
  • 17
    • 1042291979 scopus 로고    scopus 로고
    • Comparative proteomics of human endothelial cell caveolae and rafts using two-dimensional gel electrophoresis and mass spectrometry
    • Sprenger, R. R., Speijer, D., Back, J. W., De Koster, C. G., Pannekoek, H. and Horrevoets, A. J. (2004) Comparative proteomics of human endothelial cell caveolae and rafts using two-dimensional gel electrophoresis and mass spectrometry. Electrophoresis 25, 156-172
    • (2004) Electrophoresis , vol.25 , pp. 156-172
    • Sprenger, R.R.1    Speijer, D.2    Back, J.W.3    De Koster, C.G.4    Pannekoek, H.5    Horrevoets, A.J.6
  • 18
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L. J., De Hoog, C. L. and Mann, M. (2003) Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl. Acad. Sci. U.S.A. 100, 5813-5818
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 19
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M. and Rogers, S. W. (1996) PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 20
    • 0021244750 scopus 로고
    • Photoaflinity labeling of insulin-sensitive hexose transporters in intact rat adipocytes. Direct evidence that latent transporters become exposed to the extracellular space in response to insulin
    • Oka, Y. and Czech, M. P. (1984) Photoaflinity labeling of insulin-sensitive hexose transporters in intact rat adipocytes. Direct evidence that latent transporters become exposed to the extracellular space in response to insulin. J. Biol. Chem. 259, 8125-8133
    • (1984) J. Biol. Chem. , vol.259 , pp. 8125-8133
    • Oka, Y.1    Czech, M.P.2
  • 21
    • 0028228521 scopus 로고
    • Insulin stimulates phosphorylation of c-Jun, c-Fos, and Fos-related proteins in cultured adipocytes
    • Kim, S. J. and Kahn, C. R. (1994) Insulin stimulates phosphorylation of c-Jun, c-Fos, and Fos-related proteins in cultured adipocytes. J. Biol. Chem. 269, 11887-11892
    • (1994) J. Biol. Chem. , vol.269 , pp. 11887-11892
    • Kim, S.J.1    Kahn, C.R.2
  • 23
    • 0036156753 scopus 로고    scopus 로고
    • 'De novo' sequencing of peptides recovered from in-gel digested proteins by nanoelectrospray tandem mass spectrometry
    • Shevchenko, A., Chernushevic, I., Wilm, M. and Mann, M. (2002) 'De novo' sequencing of peptides recovered from in-gel digested proteins by nanoelectrospray tandem mass spectrometry. Mol. Biotechnol. 20, 107-118
    • (2002) Mol. Biotechnol. , vol.20 , pp. 107-118
    • Shevchenko, A.1    Chernushevic, I.2    Wilm, M.3    Mann, M.4
  • 24
    • 0029853096 scopus 로고    scopus 로고
    • Biochemical isolation of a membrane microdomain from resting platelets highly enriched in the plasma membrane glycoprotein CD36
    • Dorahy, D. J., Lincz, L. F., Meldrum, C. J. and Burns, G. F. (1996) Biochemical isolation of a membrane microdomain from resting platelets highly enriched in the plasma membrane glycoprotein CD36. Biochem. J. 319, 67-72
    • (1996) Biochem. J. , vol.319 , pp. 67-72
    • Dorahy, D.J.1    Lincz, L.F.2    Meldrum, C.J.3    Burns, G.F.4
  • 26
    • 0024512015 scopus 로고
    • Isolation and characterization of platelet glycoprotein IV (CD36)
    • Tandon, N. N., Lipsky, R. H., Burgess, W. H. and Jamieson, G. A. (1989) Isolation and characterization of platelet glycoprotein IV (CD36). J. Biol. Chem. 264, 7570-7575
    • (1989) J. Biol. Chem. , vol.264 , pp. 7570-7575
    • Tandon, N.N.1    Lipsky, R.H.2    Burgess, W.H.3    Jamieson, G.A.4
  • 27
    • 0035422806 scopus 로고    scopus 로고
    • Cell surface monoamine oxidases: Enzymes in search of a function
    • Jalkanen, S. and Salmi, M. (2001) Cell surface monoamine oxidases: enzymes in search of a function. EMBO J. 20, 3893-3901
    • (2001) EMBO J. , vol.20 , pp. 3893-3901
    • Jalkanen, S.1    Salmi, M.2
  • 29
    • 0030909369 scopus 로고    scopus 로고
    • Membrane amine oxidase cloning and identification as a major protein in the adipocyte plasma membrane
    • Morris, N. J., Ducret, A., Aebersold, R., Ross, S. A., Keller, S. R. and Lienhard, G. E. (1997) Membrane amine oxidase cloning and identification as a major protein in the adipocyte plasma membrane. J. Biol. Chem. 272, 9388-9392
    • (1997) J. Biol. Chem. , vol.272 , pp. 9388-9392
    • Morris, N.J.1    Ducret, A.2    Aebersold, R.3    Ross, S.A.4    Keller, S.R.5    Lienhard, G.E.6
  • 30
    • 0035831456 scopus 로고    scopus 로고
    • Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana
    • Vener, A. V., Harms, A., Sussman, M. R. and Vierstra, R. D. (2001) Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana. J. Biol. Chem. 276, 6959-6966
    • (2001) J. Biol. Chem. , vol.276 , pp. 6959-6966
    • Vener, A.V.1    Harms, A.2    Sussman, M.R.3    Vierstra, R.D.4
  • 32
    • 0029003932 scopus 로고
    • Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe
    • Scherer, P. E., Tang, Z., Chun, M., Sargiacomo, M., Lodish, H. F. and Lisanti, M. P. (1995) Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe. J. Biol. Chem. 270, 16395-16401
    • (1995) J. Biol. Chem. , vol.270 , pp. 16395-16401
    • Scherer, P.E.1    Tang, Z.2    Chun, M.3    Sargiacomo, M.4    Lodish, H.F.5    Lisanti, M.P.6
  • 33
    • 0033551731 scopus 로고    scopus 로고
    • Immunoisolation of caveolae with high affinity antibody binding to the oligomeric caveolin cage. Toward understanding the basis of purification
    • Oh, P. and Schnitzer, J. E. (1999) Immunoisolation of caveolae with high affinity antibody binding to the oligomeric caveolin cage. Toward understanding the basis of purification. J. Biol. Chem. 274, 23144-23154
    • (1999) J. Biol. Chem. , vol.274 , pp. 23144-23154
    • Oh, P.1    Schnitzer, J.E.2
  • 34
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • Li, S., Couet, J. and Lisanti, M. P. (1996) Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. J. Biol. Chem. 271, 29182-29190
    • (1996) J. Biol. Chem. , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 35
    • 0034731376 scopus 로고    scopus 로고
    • Differential targeting of beta-adrenergic receptor subtypes and adenylyl cyclase to cardiomyocyte caveolae. A mechanism to functionally regulate the cAMP signaling pathway
    • Rybin, V. O., Xu, X., Lisanti, M. P. and Steinberg, S. F. (2000) Differential targeting of beta-adrenergic receptor subtypes and adenylyl cyclase to cardiomyocyte caveolae. A mechanism to functionally regulate the cAMP signaling pathway. J. Biol. Chem. 275, 41447-41457
    • (2000) J. Biol. Chem. , vol.275 , pp. 41447-41457
    • Rybin, V.O.1    Xu, X.2    Lisanti, M.P.3    Steinberg, S.F.4
  • 36
    • 0032525134 scopus 로고    scopus 로고
    • Cloning and functional characterization of PTRF, a novel protein which induces dissociation of paused ternary transcription complexes
    • Jansa, P., Mason, S. W., Hoffmann-Rohrer, U. and Grummt, I. (1998) Cloning and functional characterization of PTRF, a novel protein which induces dissociation of paused ternary transcription complexes. EMBO J. 17, 2855-2864
    • (1998) EMBO J. , vol.17 , pp. 2855-2864
    • Jansa, P.1    Mason, S.W.2    Hoffmann-Rohrer, U.3    Grummt, I.4
  • 38
    • 0033118814 scopus 로고    scopus 로고
    • The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein
    • Gustincich, S., Vatta, P., Goruppi, S., Wolf, M., Saccone, S., Della Valle, G., Baggiolini, M. and Schneider, C. (1999) The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein. Genomics 57, 120-129
    • (1999) Genomics , vol.57 , pp. 120-129
    • Gustincich, S.1    Vatta, P.2    Goruppi, S.3    Wolf, M.4    Saccone, S.5    Della Valle, G.6    Baggiolini, M.7    Schneider, C.8
  • 40
    • 0033520911 scopus 로고    scopus 로고
    • Annexin VI participates in the formation of a reversible, membrane-cytoskeleton complex in smooth muscle cells
    • Babiychuk, E. B., Palstra, R. J., Schaller, J., Kampfer, U. and Draeger, A. (1999) Annexin VI participates in the formation of a reversible, membrane-cytoskeleton complex in smooth muscle cells. J. Biol. Chem. 274, 35191-35195
    • (1999) J. Biol. Chem. , vol.274 , pp. 35191-35195
    • Babiychuk, E.B.1    Palstra, R.J.2    Schaller, J.3    Kampfer, U.4    Draeger, A.5
  • 41
    • 0037085452 scopus 로고    scopus 로고
    • Cholesteryl ester is transported from caveolae to internal membranes as part of a caveolin-annexin II lipid-protein complex
    • Uittenbogaard, A., Everson, W. V., Matveev, S. V. and Smart, E. J. (2002) Cholesteryl ester is transported from caveolae to internal membranes as part of a caveolin-annexin II lipid-protein complex. J. Biol. Chem. 277, 4925-4931
    • (2002) J. Biol. Chem. , vol.277 , pp. 4925-4931
    • Uittenbogaard, A.1    Everson, W.V.2    Matveev, S.V.3    Smart, E.J.4
  • 42
    • 0032893752 scopus 로고    scopus 로고
    • Annexin V and phospholipid metabolism
    • Russo-Marie, F. (1999) Annexin V and phospholipid metabolism. Clin. Chem. Lab. Med. 37, 287-291
    • (1999) Clin. Chem. Lab. Med. , vol.37 , pp. 287-291
    • Russo-Marie, F.1
  • 44
    • 0033611490 scopus 로고    scopus 로고
    • Endocytosis: EH domains lend a hand
    • Mayer, B. J. (1999) Endocytosis: EH domains lend a hand. Curr. Biol. 9, 70-73
    • (1999) Curr. Biol. , vol.9 , pp. 70-73
    • Mayer, B.J.1
  • 45
    • 0030614872 scopus 로고    scopus 로고
    • A protein kinase Cdelta-binding protein SRBC whose expression is induced by serum starvation
    • Izumi, Y., Hirai, S., Tamai, Y., Fujise-Matsuoka, A., Nishimura, Y. and Ohno, S. (1997) A protein kinase Cdelta-binding protein SRBC whose expression is induced by serum starvation. J. Biol. Chem. 272, 7381-7389
    • (1997) J. Biol. Chem. , vol.272 , pp. 7381-7389
    • Izumi, Y.1    Hirai, S.2    Tamai, Y.3    Fujise-Matsuoka, A.4    Nishimura, Y.5    Ohno, S.6
  • 46
    • 0031963681 scopus 로고    scopus 로고
    • Id helix-loop-helix proteins in cell growth and differentiation
    • Norton, J. D., Deed, R. W., Craggs, G. and Sablitzky, F. (1998) Id helix-loop-helix proteins in cell growth and differentiation. Trends Cell Biol. 8, 58-65
    • (1998) Trends Cell Biol. , vol.8 , pp. 58-65
    • Norton, J.D.1    Deed, R.W.2    Craggs, G.3    Sablitzky, F.4
  • 47
    • 0035863852 scopus 로고    scopus 로고
    • The transcript release factor PTRF augments ribosomal gene transcription by facilitating reinitiation of RNA polymerase I
    • Jansa, P., Burek, C., Sander, E. E. and Grummt, I. (2001) The transcript release factor PTRF augments ribosomal gene transcription by facilitating reinitiation of RNA polymerase I. Nucleic Acids Res. 29, 423-429
    • (2001) Nucleic Acids Res. , vol.29 , pp. 423-429
    • Jansa, P.1    Burek, C.2    Sander, E.E.3    Grummt, I.4
  • 48
    • 0034177159 scopus 로고    scopus 로고
    • PTRF (polymerase I and transcript-release factor) is tissue-specific and interacts with the BFCOL1 (binding factor of a type-I collagen promoter) zinc-finger transcription factor which binds to the two mouse type-I collagen gene promoters
    • Hasegawa, T., Takeuchi, A., Miyaishi, O., Xiao, H., Mao, J. and Isobe, K. (2000) PTRF (polymerase I and transcript-release factor) is tissue-specific and interacts with the BFCOL1 (binding factor of a type-I collagen promoter) zinc-finger transcription factor which binds to the two mouse type-I collagen gene promoters. Biochem. J. 347, 55-59
    • (2000) Biochem. J. , vol.347 , pp. 55-59
    • Hasegawa, T.1    Takeuchi, A.2    Miyaishi, O.3    Xiao, H.4    Mao, J.5    Isobe, K.6
  • 49
    • 0037155792 scopus 로고    scopus 로고
    • Determinants of ligand specificity in groups I and IV WW domains as studied by surface plasmon resonance and model building
    • Kato, Y., Ito, M., Kawai, K., Nagata, K. and Tanokura, M. (2002) Determinants of ligand specificity in groups I and IV WW domains as studied by surface plasmon resonance and model building. J. Biol. Chem. 277, 10173-10177
    • (2002) J. Biol. Chem. , vol.277 , pp. 10173-10177
    • Kato, Y.1    Ito, M.2    Kawai, K.3    Nagata, K.4    Tanokura, M.5
  • 50
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. (1996) The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. U.S.A. 93, 12142-12149
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 12142-12149
    • Varshavsky, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.