메뉴 건너뛰기




Volumn 439, Issue 1, 2011, Pages 113-128

Disrupted in renal carcinoma 2 (DIRC2), a novel transporter of the lysosomal membrane, is proteolytically processed by cathepsin L

Author keywords

Carcinogenesis; Cathepsin L.; Disrupted in renal carcinoma 2 (DIRC2); Lysosomal membrane; Major facilitator superfamily; Proteolysis

Indexed keywords

CATHEPSIN L; DISRUPTED IN RENAL CARCINOMA 2; UNCLASSIFIED DRUG; XENOPUS PROTEIN;

EID: 80052701566     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110166     Document Type: Article
Times cited : (29)

References (51)
  • 1
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function
    • Saftig, P. and Klumperman, J. (2009) Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat. Rev. Mol. Cell Biol. 10, 623-635
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 3
    • 43149104361 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of lysosomal membrane transporters
    • Sagne, C. and Gasnier, B. (2008) Molecular physiology and pathophysiology of lysosomal membrane transporters. J. Inherit. Metab. Dis. 31, 258-266
    • (2008) J. Inherit. Metab. Dis. , vol.31 , pp. 258-266
    • Sagne, C.1    Gasnier, B.2
  • 5
    • 53849119555 scopus 로고    scopus 로고
    • Ins and outs of major facilitator superfamily antiporters
    • Law, C. J., Maloney, P. C. and Wang, D. N. (2008) Ins and outs of major facilitator superfamily antiporters. Annu. Rev. Microbiol. 62, 289-305
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 289-305
    • Law, C.J.1    Maloney, P.C.2    Wang, D.N.3
  • 7
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R. and Iwata, S. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-615
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 8
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol 3-phosphate transporter from Escherichia coli
    • Huang, Y., Lemieux, M. J., Song, J., Auer, M. and Wang, D. N. (2003) Structure and mechanism of the glycerol 3-phosphate transporter from Escherichia coli. Science 301, 616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 11
    • 0021269154 scopus 로고
    • Enhanced degradation of cathepsin D synthesized in the presence of the threonine analog β-hydroxynorvaline
    • Hentze, M., Hasilik, A. and von Figura, K. (1984) Enhanced degradation of cathepsin D synthesized in the presence of the threonine analog β-hydroxynorvaline. Arch. Biochem. Biophys. 230, 375-382
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 375-382
    • Hentze, M.1    Hasilik, A.2    Von Figura, K.3
  • 12
    • 0030033235 scopus 로고    scopus 로고
    • Purification of lysosomal membrane proteins from human placenta
    • Diettrich, O., Gallert, F. and Hasilik, A. (1996) Purification of lysosomal membrane proteins from human placenta. Eur. J. Cell Biol. 69, 99-106
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 99-106
    • Diettrich, O.1    Gallert, F.2    Hasilik, A.3
  • 14
    • 15744405825 scopus 로고    scopus 로고
    • Identification of mammalian proline transporter SIT1 (SLC6A20) with characteristics of classical system Imino
    • Takanaga, H., Mackenzie, B., Suzuki, Y. and Hediger, M. A. (2005) Identification of mammalian proline transporter SIT1 (SLC6A20) with characteristics of classical system Imino. J. Biol. Chem. 280, 8974-8984
    • (2005) J. Biol. Chem. , vol.280 , pp. 8974-8984
    • Takanaga, H.1    Mackenzie, B.2    Suzuki, Y.3    Hediger, M.A.4
  • 17
    • 33746255613 scopus 로고    scopus 로고
    • Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice
    • Sevenich, L., Pennacchio, L. A., Peters, C. and Reinheckel, T. (2006) Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Biol. Chem. 387, 885-891
    • (2006) Biol. Chem. , vol.387 , pp. 885-891
    • Sevenich, L.1    Pennacchio, L.A.2    Peters, C.3    Reinheckel, T.4
  • 18
    • 0029083689 scopus 로고
    • Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells
    • Saftig, P., Hetman, M., Schmahl, W., Weber, K., Heine, L., Mossmann, H., Koster, A., Hess, B., Evers, M. and von Figura, K. (1995) Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells. EMBO J. 14, 3599-3608
    • (1995) EMBO J. , vol.14 , pp. 3599-3608
    • Saftig, P.1    Hetman, M.2    Schmahl, W.3    Weber, K.4    Heine, L.5    Mossmann, H.6    Koster, A.7    Hess, B.8    Evers, M.9    Von Figura, K.10
  • 19
    • 77956646290 scopus 로고    scopus 로고
    • Molecular characterisation of 'transmembrane protein 192' (TMEM192), a novel protein of the lysosomal membrane
    • Schröder, B., Wrocklage, C., Hasilik, A. and Saftig, P. (2010) Molecular characterisation of 'transmembrane protein 192' (TMEM192), a novel protein of the lysosomal membrane. Biol. Chem. 391, 695-704
    • (2010) Biol. Chem. , vol.391 , pp. 695-704
    • Schröder, B.1    Wrocklage, C.2    Hasilik, A.3    Saftig, P.4
  • 20
    • 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
  • 21
    • 0023520131 scopus 로고
    • Neutral endopeptidase-24.11 (enkephalinase). Biosynthesis and localization in human fibroblasts
    • Lorkowski, G., Zijderhand-Bleekemolen, J. E., Erdos, E. G., von Figura, K. and Hasilik, A. (1987) Neutral endopeptidase-24.11 (enkephalinase). Biosynthesis and localization in human fibroblasts. Biochem. J. 248, 345-350
    • (1987) Biochem. J. , vol.248 , pp. 345-350
    • Lorkowski, G.1    Zijderhand-Bleekemolen, J.E.2    Erdos, E.G.3    Von Figura, K.4    Hasilik, A.5
  • 22
  • 23
    • 0017698250 scopus 로고
    • Human α-N-acetylglucosaminidase. 1. Purification and properties
    • von Figura, K. (1977) Human α-N-acetylglucosaminidase. 1. Purification and properties. Eur. J. Biochem. 80, 523-533
    • (1977) Eur. J. Biochem. , vol.80 , pp. 523-533
    • Von Figura, K.1
  • 25
    • 0025989238 scopus 로고
    • Multiple targets for brefeldin A
    • Pelham, H. R. (1991) Multiple targets for brefeldin A. Cell 67, 449-451
    • (1991) Cell , vol.67 , pp. 449-451
    • Pelham, H.R.1
  • 26
    • 0018903866 scopus 로고
    • Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight
    • Hasilik, A. and Neufeld, E. F. (1980) Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight. J. Biol. Chem. 255, 4937-4945
    • (1980) J. Biol. Chem. , vol.255 , pp. 4937-4945
    • Hasilik, A.1    Neufeld, E.F.2
  • 27
    • 0020445847 scopus 로고
    • The slow, tight-binding inhibition of cathepsin B by leupeptin. A hysteretic effect
    • Baici, A. and Gyger-Marazzi, M. (1982) The slow, tight-binding inhibition of cathepsin B by leupeptin. A hysteretic effect. Eur. J. Biochem. 129, 33-41
    • (1982) Eur. J. Biochem. , vol.129 , pp. 33-41
    • Baici, A.1    Gyger-Marazzi, M.2
  • 29
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett, A. J., Kembhavi, A. A., Brown, M. A., Kirschke, H., Knight, C. G., Tamai, M. and Hanada, K. (1982) L-trans-Epoxysuccinyl-leucylamido(4- guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 201, 189-198
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 30
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: Cellular roadmap to different functions
    • Brix, K., Dunkhorst, A., Mayer, K. and Jordans, S. (2008) Cysteine cathepsins: cellular roadmap to different functions. Biochimie 90, 194-207
    • (2008) Biochimie , vol.90 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 32
    • 0036661078 scopus 로고    scopus 로고
    • CA-074, but not its methyl ester CA-074Me, is a selective inhibitor of cathepsin B within living cells
    • Montaser, M., Lalmanach, G. and Mach, L. (2002) CA-074, but not its methyl ester CA-074Me, is a selective inhibitor of cathepsin B within living cells. Biol. Chem. 383, 1305-1308
    • (2002) Biol. Chem. , vol.383 , pp. 1305-1308
    • Montaser, M.1    Lalmanach, G.2    Mach, L.3
  • 33
    • 0037025342 scopus 로고    scopus 로고
    • Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells
    • Ebert, D. H., Deussing, J., Peters, C. and Dermody, T. S. (2002) Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells. J. Biol. Chem. 277, 24609-24617
    • (2002) J. Biol. Chem. , vol.277 , pp. 24609-24617
    • Ebert, D.H.1    Deussing, J.2    Peters, C.3    Dermody, T.S.4
  • 36
    • 10644257949 scopus 로고    scopus 로고
    • Functional characterization of wild-type and mutant human sialin
    • Morin, P., Sagne, C. and Gasnier, B. (2004) Functional characterization of wild-type and mutant human sialin. EMBO J. 23, 4560-4570
    • (2004) EMBO J. , vol.23 , pp. 4560-4570
    • Morin, P.1    Sagne, C.2    Gasnier, B.3
  • 37
    • 33947154383 scopus 로고    scopus 로고
    • Scanning N-glycosylation mutagenesis of membrane proteins
    • Cheung, J. C. and Reithmeier, R. A. (2007) Scanning N-glycosylation mutagenesis of membrane proteins. Methods 41, 451-459
    • (2007) Methods , vol.41 , pp. 451-459
    • Cheung, J.C.1    Reithmeier, R.A.2
  • 38
    • 0031656594 scopus 로고    scopus 로고
    • The extent of polylactosamine glycosylation of MDCK LAMP-2 is determined by its Golgi residence time
    • Nabi, I. R. and Dennis, J. W. (1998) The extent of polylactosamine glycosylation of MDCK LAMP-2 is determined by its Golgi residence time. Glycobiology 8, 947-953
    • (1998) Glycobiology , vol.8 , pp. 947-953
    • Nabi, I.R.1    Dennis, J.W.2
  • 39
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J. S. and Traub, L. M. (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72, 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 40
    • 0029670903 scopus 로고    scopus 로고
    • Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting
    • Schweizer, A., Kornfeld, S. and Rohrer, J. (1996) Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting. J. Cell Biol. 132, 577-584
    • (1996) J. Cell Biol. , vol.132 , pp. 577-584
    • Schweizer, A.1    Kornfeld, S.2    Rohrer, J.3
  • 41
    • 63149196645 scopus 로고    scopus 로고
    • Principles of lysosomal membrane degradation: Cellular topology and biochemistry of lysosomal lipid degradation
    • Schulze, H., Kolter, T. and Sandhoff, K. (2009) Principles of lysosomal membrane degradation: cellular topology and biochemistry of lysosomal lipid degradation. Biochim. Biophys. Acta 1793, 674-683
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 674-683
    • Schulze, H.1    Kolter, T.2    Sandhoff, K.3
  • 42
    • 77957794731 scopus 로고    scopus 로고
    • Analysis of the biogenesis of heparan sulfate acetyl-CoA:α- glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC
    • Durand, S., Feldhammer, M., Bonneil, E., Thibault, P. and Pshezhetsky, A. V. (2010) Analysis of the biogenesis of heparan sulfate acetyl-CoA:α- glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC. J. Biol. Chem. 285, 31233-31242
    • (2010) J. Biol. Chem. , vol.285 , pp. 31233-31242
    • Durand, S.1    Feldhammer, M.2    Bonneil, E.3    Thibault, P.4    Pshezhetsky, A.V.5
  • 43
    • 33744963797 scopus 로고    scopus 로고
    • Posttranslational cleavage and adaptor protein complex-dependent trafficking of mucolipin-1
    • Miedel, M. T., Weixel, K. M., Bruns, J. R., Traub, L. M. and Weisz, O. A. (2006) Posttranslational cleavage and adaptor protein complex-dependent trafficking of mucolipin-1. J. Biol. Chem. 281, 12751-12759
    • (2006) J. Biol. Chem. , vol.281 , pp. 12751-12759
    • Miedel, M.T.1    Weixel, K.M.2    Bruns, J.R.3    Traub, L.M.4    Weisz, O.A.5
  • 44
    • 56349114913 scopus 로고    scopus 로고
    • Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9
    • Park, B., Brinkmann, M. M., Spooner, E., Lee, C. C., Kim, Y. M. and Ploegh, H. L. (2008) Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9. Nat. Immunol. 9, 1407-1414
    • (2008) Nat. Immunol. , vol.9 , pp. 1407-1414
    • Park, B.1    Brinkmann, M.M.2    Spooner, E.3    Lee, C.C.4    Kim, Y.M.5    Ploegh, H.L.6
  • 45
    • 0036929283 scopus 로고    scopus 로고
    • Processing and activation of lysosomal proteinases
    • Ishidoh, K. and Kominami, E. (2002) Processing and activation of lysosomal proteinases. Biol. Chem. 383, 1827-1831
    • (2002) Biol. Chem. , vol.383 , pp. 1827-1831
    • Ishidoh, K.1    Kominami, E.2
  • 46
    • 0034930528 scopus 로고    scopus 로고
    • Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L
    • Reinheckel, T., Deussing, J., Roth, W. and Peters, C. (2001) Towards specific functions of lysosomal cysteine peptidases: phenotypes of mice deficient for cathepsin B or cathepsin L. Biol. Chem. 382, 735-741
    • (2001) Biol. Chem. , vol.382 , pp. 735-741
    • Reinheckel, T.1    Deussing, J.2    Roth, W.3    Peters, C.4
  • 47
    • 77957855881 scopus 로고    scopus 로고
    • Specialized roles for cysteine cathepsins in health and disease
    • Reiser, J., Adair, B. and Reinheckel, T. (2010) Specialized roles for cysteine cathepsins in health and disease. J. Clin. Invest. 120, 3421-3431
    • (2010) J. Clin. Invest. , vol.120 , pp. 3421-3431
    • Reiser, J.1    Adair, B.2    Reinheckel, T.3
  • 50
    • 0025006452 scopus 로고
    • Reconstitution of an active lactose carrier in vivo by simultaneous synthesis of two complementary protein fragments
    • Wrubel, W., Stochaj, U., Sonnewald, U., Theres, C. and Ehring, R. (1990) Reconstitution of an active lactose carrier in vivo by simultaneous synthesis of two complementary protein fragments. J. Bacteriol. 172, 5374-5381
    • (1990) J. Bacteriol. , vol.172 , pp. 5374-5381
    • Wrubel, W.1    Stochaj, U.2    Sonnewald, U.3    Theres, C.4    Ehring, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.