메뉴 건너뛰기




Volumn 4, Issue 2, 2005, Pages 133-143

A proteomic analysis of lysosomal integral membrane proteins reveals the diverse composition of the organelle

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; MEMBRANE PROTEIN; RAB PROTEIN; SNARE PROTEIN; UBIQUITIN;

EID: 14944385370     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M400128-MCP200     Document Type: Article
Times cited : (145)

References (61)
  • 2
    • 0037175388 scopus 로고    scopus 로고
    • Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells
    • Jaiswal, J. K., Andrews, N. W., and Simon, S. M. (2002) Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells. J. Cell Biol. 159, 625-635
    • (2002) J. Cell Biol. , vol.159 , pp. 625-635
    • Jaiswal, J.K.1    Andrews, N.W.2    Simon, S.M.3
  • 4
    • 0036423664 scopus 로고    scopus 로고
    • Formation and function of the ruffled border in osteoclasts
    • Stenbeck, G. (2002) Formation and function of the ruffled border in osteoclasts. Semin. Cell Dev. Biol. 13, 285-292
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 285-292
    • Stenbeck, G.1
  • 6
    • 0037698096 scopus 로고    scopus 로고
    • Presenilin-1, nicastrin, amyloid precursor protein, and γ-secretase activity are colocalized in the lysosomal membrane
    • Pasternak, S. H., Bagshaw, R. D., Guiral, M., Zhang, S., Ackerley, C. A., Pak, B. J., Callahan, J. W., and Mahuran, D. J. (2003) Presenilin-1, nicastrin, amyloid precursor protein, and γ-secretase activity are colocalized in the lysosomal membrane. J. Biol. Chem. 278, 26687-26694
    • (2003) J. Biol. Chem. , vol.278 , pp. 26687-26694
    • Pasternak, S.H.1    Bagshaw, R.D.2    Guiral, M.3    Zhang, S.4    Ackerley, C.A.5    Pak, B.J.6    Callahan, J.W.7    Mahuran, D.J.8
  • 7
    • 1842532328 scopus 로고    scopus 로고
    • The role of the endosomal/lysosomal system in amyloid- production and the pathophysiology of Alzheimer's disease: Reexamining the spatial paradox from a lysosomal perspective
    • Pasternak, S. H., Callahan, J. W., and Mahuran, D. J. (2004) The role of the endosomal/lysosomal system in amyloid-production and the pathophysiology of Alzheimer's disease: reexamining the spatial paradox from a lysosomal perspective. J. Alzheimer's Dis. 6, 53-65
    • (2004) J. Alzheimer's Dis. , vol.6 , pp. 53-65
    • Pasternak, S.H.1    Callahan, J.W.2    Mahuran, D.J.3
  • 12
    • 0014288490 scopus 로고
    • The large-scale separation of peroxisomes, mitochondria, and lysosomes from the livers of rats injected with Triton WR-1339. Improved isolation procedures, automated analysis, biochemical and morphological properties of fractions
    • Leighton, F., Poole, B., Beaufay, H., Baudhuin, P., Coffey, J. W., Fowler, S., and De Duve, C. (1968) The large-scale separation of peroxisomes, mitochondria, and lysosomes from the livers of rats injected with Triton WR-1339. Improved isolation procedures, automated analysis, biochemical and morphological properties of fractions. J. Cell Biol. 37, 482-513
    • (1968) J. Cell Biol. , vol.37 , pp. 482-513
    • Leighton, F.1    Poole, B.2    Beaufay, H.3    Baudhuin, P.4    Coffey, J.W.5    Fowler, S.6    De Duve, C.7
  • 14
    • 0020483301 scopus 로고
    • Characterization of the membrane proteins of rat liver lysosomes. Composition, enzyme activities and turnover
    • Burnside, J., and Schneider, D. L. (1982) Characterization of the membrane proteins of rat liver lysosomes. Composition, enzyme activities and turnover. Biochem. J. 204, 525-534
    • (1982) Biochem. J. , vol.204 , pp. 525-534
    • Burnside, J.1    Schneider, D.L.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0034633294 scopus 로고    scopus 로고
    • Desalting of in-gel-digested protein sample with mini-C18 columns for matrix-assisted laser desorption ionization time of flight peptide mass fingerprinting
    • Bagshaw, R. D., Callahan, J. W., and Mahuran, D. J. (2000) Desalting of in-gel-digested protein sample with mini-C18 columns for matrix-assisted laser desorption ionization time of flight peptide mass fingerprinting. Anal. Biochem. 284, 432-435
    • (2000) Anal. Biochem. , vol.284 , pp. 432-435
    • Bagshaw, R.D.1    Callahan, J.W.2    Mahuran, D.J.3
  • 19
    • 0019792936 scopus 로고
    • Intracellular hormone receptors: Evidence for insulin and lactogen receptors in a unique vesicle sedimenting in lysosome fractions of rat liver
    • Khan, M. N., Posner, B. I., Verma, A. K., Khan, R. J., and Bergeron, J. J. (1981) Intracellular hormone receptors: evidence for insulin and lactogen receptors in a unique vesicle sedimenting in lysosome fractions of rat liver. Proc. Natl. Acad. Sci. U. S. A. 78, 4980-4984
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 4980-4984
    • Khan, M.N.1    Posner, B.I.2    Verma, A.K.3    Khan, R.J.4    Bergeron, J.J.5
  • 20
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., Hubbard, A. L., Fowler, S., and Lazarow, P. B. (1982) Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93, 97-102
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 22
    • 0037334339 scopus 로고    scopus 로고
    • At the acidic edge: Emerging functions for lysosomal membrane proteins
    • Eskelinen, E. L., Tanaka, Y., and Saftig, P. (2003) At the acidic edge: emerging functions for lysosomal membrane proteins. Trends Cell Biol. 13, 137-145
    • (2003) Trends Cell Biol. , vol.13 , pp. 137-145
    • Eskelinen, E.L.1    Tanaka, Y.2    Saftig, P.3
  • 24
    • 0035865744 scopus 로고    scopus 로고
    • Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts
    • Salzer, U., and Prohaska, R. (2001) Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts. Blood 97, 1141-1143
    • (2001) Blood , vol.97 , pp. 1141-1143
    • Salzer, U.1    Prohaska, R.2
  • 25
    • 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
  • 27
    • 0023924272 scopus 로고
    • Post-Golgi apparatus localization and regional expression of rat intestinal sialyltransferase detected by immunoelectron microscopy with polypeptide epitope-purified antibody
    • Taatjes, D. J., Roth, J., Weinstein, J., and Paulson, J. C. (1988) Post-Golgi apparatus localization and regional expression of rat intestinal sialyltransferase detected by immunoelectron microscopy with polypeptide epitope-purified antibody. J. Biol. Chem. 263, 6302-6309
    • (1988) J. Biol. Chem. , vol.263 , pp. 6302-6309
    • Taatjes, D.J.1    Roth, J.2    Weinstein, J.3    Paulson, J.C.4
  • 31
    • 2342497804 scopus 로고    scopus 로고
    • Golgi targeting of ARF-like GTPase Arl3p requires its Nα-acetylation and the integral membrane protein Sys1p
    • Setty, S. R., Strochlic, T. I., Tong, A. H., Boone, C., and Burd, C. G. (2004) Golgi targeting of ARF-like GTPase Arl3p requires its Nα-acetylation and the integral membrane protein Sys1p. Nat. Cell Biol. 6, 414-419
    • (2004) Nat. Cell Biol. , vol.6 , pp. 414-419
    • Setty, S.R.1    Strochlic, T.I.2    Tong, A.H.3    Boone, C.4    Burd, C.G.5
  • 32
    • 2342546616 scopus 로고    scopus 로고
    • Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p
    • Behnia, R., Panic, B., Whyte, J. R., and Munro, S. (2004) Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p. Nat Cell Biol. 6, 405-413
    • (2004) Nat. Cell Biol. , vol.6 , pp. 405-413
    • Behnia, R.1    Panic, B.2    Whyte, J.R.3    Munro, S.4
  • 33
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman, A. M. (2001) Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2, 169-178
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 34
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • Haglund, K., Sigismund, S., Polo, S., Szymkiewicz, I., Di Fiore, P. P., and Dikic, I. (2003) Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat Cell Biol. 5, 461-466
    • (2003) Nat. Cell Biol. , vol.5 , pp. 461-466
    • Haglund, K.1    Sigismund, S.2    Polo, S.3    Szymkiewicz, I.4    Di Fiore, P.P.5    Dikic, I.6
  • 35
    • 0037677208 scopus 로고    scopus 로고
    • Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation
    • Mosesson, Y., Shtiegman, K., Katz, M., Zwang, Y., Vereb, G., Szollosi, J., and Yarden, Y. (2003) Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation. J. Biol. Chem. 278, 21323-21326
    • (2003) J. Biol. Chem. , vol.278 , pp. 21323-21326
    • Mosesson, Y.1    Shtiegman, K.2    Katz, M.3    Zwang, Y.4    Vereb, G.5    Szollosi, J.6    Yarden, Y.7
  • 36
    • 0344813707 scopus 로고    scopus 로고
    • Characterization of a 76 kDa endosomal, multispanning membrane protein that is highly conserved throughout evolution
    • Schimmoller, F., Diaz, E., Muhlbauer, B., and Pfeffer, S. R. (1998) Characterization of a 76 kDa endosomal, multispanning membrane protein that is highly conserved throughout evolution. Gene (Amst.) 216, 311-318
    • (1998) Gene (Amst.) , vol.216 , pp. 311-318
    • Schimmoller, F.1    Diaz, E.2    Muhlbauer, B.3    Pfeffer, S.R.4
  • 39
    • 0036668520 scopus 로고    scopus 로고
    • Proteomic analysis of human lysosomes: Application to monocytic and breast cancer cells
    • Journet, A., Chapel, A., Kieffer, S., Roux, F., and Garin, J. (2002) Proteomic analysis of human lysosomes: application to monocytic and breast cancer cells. Proteomics 2, 1026-1040
    • (2002) Proteomics , vol.2 , pp. 1026-1040
    • Journet, A.1    Chapel, A.2    Kieffer, S.3    Roux, F.4    Garin, J.5
  • 40
    • 0037147217 scopus 로고    scopus 로고
    • The vesicle- and target-SNARE proteins that mediate Glut4 vesicle fusion are localized in detergent-insoluble lipid rafts present on distinct intracellular membranes
    • Chamberlain, L. H., and Gould, G. W. (2002) The vesicle- and target-SNARE proteins that mediate Glut4 vesicle fusion are localized in detergent-insoluble lipid rafts present on distinct intracellular membranes. J. Biol. Chem. 277, 49750-49754
    • (2002) J. Biol. Chem. , vol.277 , pp. 49750-49754
    • Chamberlain, L.H.1    Gould, G.W.2
  • 43
    • 0035911147 scopus 로고    scopus 로고
    • A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment
    • Wunderlich, W., Fialka, I., Teis, D., Alpi, A., Pfeifer, A., Parton, R. G., Lottspeich, F., and Huber, L. A. (2001) A novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartment. J. Cell Biol. 152, 765-776
    • (2001) J. Cell Biol. , vol.152 , pp. 765-776
    • Wunderlich, W.1    Fialka, I.2    Teis, D.3    Alpi, A.4    Pfeifer, A.5    Parton, R.G.6    Lottspeich, F.7    Huber, L.A.8
  • 44
    • 0036899420 scopus 로고    scopus 로고
    • Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction
    • Teis, D., Wunderlich, W., and Huber, L. A. (2002) Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction. Dev. Cell 3, 803-814
    • (2002) Dev. Cell , vol.3 , pp. 803-814
    • Teis, D.1    Wunderlich, W.2    Huber, L.A.3
  • 46
    • 0034690194 scopus 로고    scopus 로고
    • The secreted glycoprotein CREG enhances differentiation of NTERA-2 human embryonal carcinoma cells
    • Veal, E., Groisman, R., Eisenstein, M., and Gill, G. (2000) The secreted glycoprotein CREG enhances differentiation of NTERA-2 human embryonal carcinoma cells. Oncogene 19, 2120-2128
    • (2000) Oncogene , vol.19 , pp. 2120-2128
    • Veal, E.1    Groisman, R.2    Eisenstein, M.3    Gill, G.4
  • 47
    • 0041834587 scopus 로고    scopus 로고
    • The secreted glycoprotein CREG inhibits cell growth dependent on the mannose-6-phosphate/insulin-like growth factor II receptor
    • Di Bacco, A., and Gill, G. (2003) The secreted glycoprotein CREG inhibits cell growth dependent on the mannose-6-phosphate/insulin-like growth factor II receptor. Oncogene 22, 5436-5445
    • (2003) Oncogene , vol.22 , pp. 5436-5445
    • Di Bacco, A.1    Gill, G.2
  • 48
    • 0142240338 scopus 로고    scopus 로고
    • Immune control of tuberculosis by IFN-γ-inducible LRG-47
    • MacMicking, J. D., Taylor, G. A., and McKinney, J. D. (2003) Immune control of tuberculosis by IFN-γ-inducible LRG-47. Science 302, 654-659
    • (2003) Science , vol.302 , pp. 654-659
    • MacMicking, J.D.1    Taylor, G.A.2    McKinney, J.D.3
  • 49
    • 0034407116 scopus 로고    scopus 로고
    • A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function
    • Antonin, W., Holroyd, C., Fasshauer, D., Pabst, S., Von Mollard, G. F., and Jahn, R. (2000) A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function. EMBO J. 19, 6453-6464
    • (2000) EMBO J. , vol.19 , pp. 6453-6464
    • Antonin, W.1    Holroyd, C.2    Fasshauer, D.3    Pabst, S.4    Von Mollard, G.F.5    Jahn, R.6
  • 52
    • 0001425929 scopus 로고
    • Grey-lethal, a new mutation in the house mouse
    • Gruneberg, H. (1936) Grey-lethal, a new mutation in the house mouse. J. Heredity 27, 105-109
    • (1936) J. Heredity , vol.27 , pp. 105-109
    • Gruneberg, H.1
  • 53
    • 0035047413 scopus 로고    scopus 로고
    • The mouse osteopetrotic grey-lethal mutation induces a defect in osteoclast maturation/function
    • Rajapurohitam, V., Chalhoub, N., Benachenhou, N., Neff, L., Baron, R., and Vacher, J. (2001) The mouse osteopetrotic grey-lethal mutation induces a defect in osteoclast maturation/function. Bone 28, 513-523
    • (2001) Bone , vol.28 , pp. 513-523
    • Rajapurohitam, V.1    Chalhoub, N.2    Benachenhou, N.3    Neff, L.4    Baron, R.5    Vacher, J.6
  • 55
    • 0036239516 scopus 로고    scopus 로고
    • Ectopic localizations of Golgi glycosyltransferases
    • Berger, E. G. (2002) Ectopic localizations of Golgi glycosyltransferases. Glycobiology 12, 29R-36R
    • (2002) Glycobiology , vol.12
    • Berger, E.G.1
  • 57
    • 0033591236 scopus 로고    scopus 로고
    • Autolysosomal membrane-associated betaine homocysteine methyltransferase. Limited degradation fragment of a sequestered cytosolic enzyme monitoring autophagy
    • Ueno, T., Ishidoh, K., Mineki, R., Tanida, I., Murayama, K., Kadowaki, M., and Kominami, E. (1999) Autolysosomal membrane-associated betaine homocysteine methyltransferase. Limited degradation fragment of a sequestered cytosolic enzyme monitoring autophagy. J. Biol. Chem. 274, 15222-15229
    • (1999) J. Biol. Chem. , vol.274 , pp. 15222-15229
    • Ueno, T.1    Ishidoh, K.2    Mineki, R.3    Tanida, I.4    Murayama, K.5    Kadowaki, M.6    Kominami, E.7
  • 58
    • 0032532323 scopus 로고    scopus 로고
    • Purification and characterization of autophagosomes from rat hepatocytes
    • Stromhaug, P. E., Berg, T. O., Fengsrud, M., and Seglen, P. O. (1998) Purification and characterization of autophagosomes from rat hepatocytes. Biochem. J. 335, 217-224
    • (1998) Biochem. J. , vol.335 , pp. 217-224
    • Stromhaug, P.E.1    Berg, T.O.2    Fengsrud, M.3    Seglen, P.O.4
  • 59
    • 0026059280 scopus 로고
    • Membrane markers of endoplasmic reticulum preserved in autophagic vacuolar membranes isolated from leupeptin-administered rat liver
    • Ueno, T., Muno, D., and Kominami, E. (1991) Membrane markers of endoplasmic reticulum preserved in autophagic vacuolar membranes isolated from leupeptin-administered rat liver. J. Biol. Chem. 266, 18995-18999
    • (1991) J. Biol. Chem. , vol.266 , pp. 18995-18999
    • Ueno, T.1    Muno, D.2    Kominami, E.3
  • 60
    • 0037459096 scopus 로고    scopus 로고
    • Membrane domains in the secretory and endocytic pathways
    • Pfeffer, S. (2003) Membrane domains in the secretory and endocytic pathways. Cell 112, 507-517
    • (2003) Cell , vol.112 , pp. 507-517
    • Pfeffer, S.1
  • 61
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • Barbero, P., Bittova, L., and Pfeffer, S. R. (2002) Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. J. Cell Biol. 156, 511-518
    • (2002) J. Cell Biol. , vol.156 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.