메뉴 건너뛰기




Volumn 14, Issue 2, 2004, Pages 207-219

A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE; CATHEPSIN L; ISOPROTEIN; PYRIMIDINE NUCLEOTIDE; TRANSCRIPTION FACTOR;

EID: 1942470581     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00209-6     Document Type: Article
Times cited : (317)

References (37)
  • 1
    • 0037136311 scopus 로고    scopus 로고
    • Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation
    • Balaji K.N., Schaschke N., Machleidt W., Catalfamo M., Henkart P.A. Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation. J. Exp. Med. 196:2002;493-503.
    • (2002) J. Exp. Med. , vol.196 , pp. 493-503
    • Balaji, K.N.1    Schaschke, N.2    MacHleidt, W.3    Catalfamo, M.4    Henkart, P.A.5
  • 2
    • 0023663120 scopus 로고
    • Transformation of sensory organs by mutations of the cut locus of D. melanogaster
    • Bodmer R., Barbel S., Shepherd S., Jack J.W., Jan L.Y., Jan Y.N. Transformation of sensory organs by mutations of the cut locus of D. melanogaster. Cell. 51:1987;293-307.
    • (1987) Cell , vol.51 , pp. 293-307
    • Bodmer, R.1    Barbel, S.2    Shepherd, S.3    Jack, J.W.4    Jan, L.Y.5    Jan, Y.N.6
  • 3
    • 0034054576 scopus 로고    scopus 로고
    • Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs
    • Bogyo M., Verhelst S., Bellingard-Dubouchaud V., Toba S., Greenbaum D. Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs. Chem. Biol. 7:2000;27-38.
    • (2000) Chem. Biol. , vol.7 , pp. 27-38
    • Bogyo, M.1    Verhelst, S.2    Bellingard-Dubouchaud, V.3    Toba, S.4    Greenbaum, D.5
  • 4
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • a
    • Chapman H.A., Riese R.J., Shi G.P. Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol. 59:1997;63-88. a.
    • (1997) Annu. Rev. Physiol. , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 5
    • 0030888604 scopus 로고    scopus 로고
    • Abnormal glycosylation of procathepsin L due to N-terminal point mutations correlates with failure to sort to lysosomes
    • b
    • Chapman R.L., Kane S.E., Erickson A.H. Abnormal glycosylation of procathepsin L due to N-terminal point mutations correlates with failure to sort to lysosomes. J. Biol. Chem. 272:1997;8808-8816. b.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8808-8816
    • Chapman, R.L.1    Kane, S.E.2    Erickson, A.H.3
  • 6
    • 0032541492 scopus 로고    scopus 로고
    • The mammalian Cut homeodomain protein functions as a cell-cycle dependent transcriptional repressor which downmodulates p21WAF1/CIP1/SDI1 in S phase
    • Coqueret O., Berube G., Nepveu A. The mammalian Cut homeodomain protein functions as a cell-cycle dependent transcriptional repressor which downmodulates p21WAF1/CIP1/SDI1 in S phase. EMBO J. 17:1998;4680-4694.
    • (1998) EMBO J. , vol.17 , pp. 4680-4694
    • Coqueret, O.1    Berube, G.2    Nepveu, A.3
  • 7
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S., Cygler M. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15:1996;5492-5503.
    • (1996) EMBO J. , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Menard, R.4    Mort, J.S.5    Cygler, M.6
  • 9
    • 0024312845 scopus 로고
    • Biosynthesis of lysosomal endopeptidases
    • Erickson A.H. Biosynthesis of lysosomal endopeptidases. J. Cell. Biochem. 40:1989;31-41.
    • (1989) J. Cell. Biochem. , vol.40 , pp. 31-41
    • Erickson, A.H.1
  • 10
    • 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. 70:2001;603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 11
    • 0042329761 scopus 로고    scopus 로고
    • Development of an in vitro assay for the proteolytic processing of the CDP/Cux transcription factor
    • Hebert S., Bérubé G., Nepveu A. Development of an in vitro assay for the proteolytic processing of the CDP/Cux transcription factor. J. Biochem. Mol. Biol. 36:2003;390-398.
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 390-398
    • Hebert, S.1    Bérubé, G.2    Nepveu, A.3
  • 12
    • 0030724422 scopus 로고    scopus 로고
    • Roles of ubiquitin-mediated proteolysis in cell cycle control
    • Hershko A. Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr. Opin. Cell Biol. 9:1997;788-799.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 788-799
    • Hershko, A.1
  • 15
    • 0036481454 scopus 로고    scopus 로고
    • Signal sequences control gating of the protein translocation channel in a substrate-specific manner
    • Kim S.J., Mitra D., Salerno J.R., Hegde R.S. Signal sequences control gating of the protein translocation channel in a substrate-specific manner. Dev. Cell. 2:2002;207-217.
    • (2002) Dev. Cell , vol.2 , pp. 207-217
    • Kim, S.J.1    Mitra, D.2    Salerno, J.R.3    Hegde, R.S.4
  • 16
    • 0036569798 scopus 로고    scopus 로고
    • Deregulated expression of the homeobox gene Cux-1 in transgenic mice results in downregulation of p27(kip1) expression during nephrogenesis, glomerular abnormalities, and multiorgan hyperplasia
    • Ledford A.W., Brantley J.G., Kemeny G., Foreman T.L., Quaggin S.E., Igarashi P., Oberhaus S.M., Rodova M., Calvet J.P., Vanden Heuvel G.B. Deregulated expression of the homeobox gene Cux-1 in transgenic mice results in downregulation of p27(kip1) expression during nephrogenesis, glomerular abnormalities, and multiorgan hyperplasia. Dev. Biol. 245:2002;157-171.
    • (2002) Dev. Biol. , vol.245 , pp. 157-171
    • Ledford, A.W.1    Brantley, J.G.2    Kemeny, G.3    Foreman, T.L.4    Quaggin, S.E.5    Igarashi, P.6    Oberhaus, S.M.7    Rodova, M.8    Calvet, J.P.9    Vanden Heuvel, G.B.10
  • 17
    • 0023895357 scopus 로고
    • A small-scale procedure for preparation of nuclear extracts that support efficient transcription and pre-mRNA splicing
    • Lee K.A.W., Bindereif A., Green M.R. A small-scale procedure for preparation of nuclear extracts that support efficient transcription and pre-mRNA splicing. Gene Anal. Tech. 5:1988;22-31.
    • (1988) Gene Anal. Tech. , vol.5 , pp. 22-31
    • Lee, K.A.W.1    Bindereif, A.2    Green, M.R.3
  • 18
    • 0025966568 scopus 로고
    • Four distinct regulatory regions of the cut locus and their effect on cell type specification in Drosophila
    • Liu S., McLeod E., Jack J. Four distinct regulatory regions of the cut locus and their effect on cell type specification in Drosophila. Genetics. 127:1991;151-159.
    • (1991) Genetics , vol.127 , pp. 151-159
    • Liu, S.1    McLeod, E.2    Jack, J.3
  • 20
    • 0032557529 scopus 로고    scopus 로고
    • In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B. Subcellular distribution of the truncated enzyme in COS cells
    • Mehtani S., Gong Q., Panella J., Subbiah S., Peffley D.M., Frankfater A. In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B. Subcellular distribution of the truncated enzyme in COS cells. J. Biol. Chem. 273:1998;13236-13244.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13236-13244
    • Mehtani, S.1    Gong, Q.2    Panella, J.3    Subbiah, S.4    Peffley, D.M.5    Frankfater, A.6
  • 21
    • 0031591699 scopus 로고    scopus 로고
    • Evidence for participation of a calpain-like cysteine protease in cell cycle progression through late G1 phase
    • Mellgren R.L. Evidence for participation of a calpain-like cysteine protease in cell cycle progression through late G1 phase. Biochem. Biophys. Res. Commun. 236:1997;555-558.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 555-558
    • Mellgren, R.L.1
  • 22
    • 0242452190 scopus 로고    scopus 로고
    • Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro
    • Menard R., Carmona E., Takebe S., Dufour E., Plouffe C., Mason P., Mort J.S. Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro. J. Biol. Chem. 273:1998;4478-4484.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4478-4484
    • Menard, R.1    Carmona, E.2    Takebe, S.3    Dufour, E.4    Plouffe, C.5    Mason, P.6    Mort, J.S.7
  • 24
    • 0034613176 scopus 로고    scopus 로고
    • CCAAT displacement activity involves Cut repeats 1 and 2, not the Cut homeodomain
    • Moon N.S., Berube G., Nepveu A. CCAAT displacement activity involves Cut repeats 1 and 2, not the Cut homeodomain. J. Biol. Chem. 275:2000;31325-31334.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31325-31334
    • Moon, N.S.1    Berube, G.2    Nepveu, A.3
  • 25
    • 0035724764 scopus 로고    scopus 로고
    • S phase-specific proteolytic cleavage is required to activate stable DNA binding by the CDP/Cut homeodomain protein
    • Moon N.S., Premdas P., Truscott M., Leduy L., Berube G., Nepveu A. S phase-specific proteolytic cleavage is required to activate stable DNA binding by the CDP/Cut homeodomain protein. Mol. Cell. Biol. 21:2001;6332-6345.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6332-6345
    • Moon, N.S.1    Premdas, P.2    Truscott, M.3    Leduy, L.4    Berube, G.5    Nepveu, A.6
  • 26
    • 0035972762 scopus 로고    scopus 로고
    • Role of the multifunctional CDP/Cut/Cux homeodomain transcription factor in regulating differentiation, cell growth and development
    • Nepveu A. Role of the multifunctional CDP/Cut/Cux homeodomain transcription factor in regulating differentiation, cell growth and development. Gene. 270:2001;1-15.
    • (2001) Gene , vol.270 , pp. 1-15
    • Nepveu, A.1
  • 27
    • 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., Peters C. Towards specific functions of lysosomal cysteine peptidases. phenotypes of mice deficient for cathepsin B or cathepsin L Biol. Chem. 382:2001;735-741.
    • (2001) Biol. Chem. , vol.382 , pp. 735-741
    • Reinheckel, T.1    Deussing, J.2    Roth, W.3    Peters, C.4
  • 30
    • 0015293356 scopus 로고
    • The synthesis of acidic chromosomal proteins during the cell cycle of HeLa S-3 cells. I. The accelerated accumulation of acidic residual nuclear protein before the initiation of DNA replication
    • Stein G.S., Borun T.W. The synthesis of acidic chromosomal proteins during the cell cycle of HeLa S-3 cells. I. The accelerated accumulation of acidic residual nuclear protein before the initiation of DNA replication. J. Cell Biol. 52:1972;292-307.
    • (1972) J. Cell Biol. , vol.52 , pp. 292-307
    • Stein, G.S.1    Borun, T.W.2
  • 32
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: Unpredicted non-ER locations and functions
    • Turano C., Coppari S., Altieri F., Ferraro A. Proteins of the PDI family. unpredicted non-ER locations and functions J. Cell. Physiol. 193:2002;154-163.
    • (2002) J. Cell. Physiol. , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 33
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk B., Turk V., Turk D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 378:1997;141-150.
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 34
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk B., Turk D., Turk V. Lysosomal cysteine proteases. more than scavengers Biochim. Biophys. Acta. 1477:2000;98-111.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 35
    • 0029859407 scopus 로고    scopus 로고
    • CDP/cut is the DNA-binding subunit of histone gene transcription factor HiNF-D: A mechanism for gene regulation at the G1/S phase cell cycle transition point independent of transcription factor E2F
    • van Wijnen A.J., van Gurp M.F., de Ridder M.C., Tufarelli C., Last T.J., Birnbaum M., Vaughan P.S., Giordano A., Krek W., Neufeld E.J.et al. CDP/cut is the DNA-binding subunit of histone gene transcription factor HiNF-D. a mechanism for gene regulation at the G1/S phase cell cycle transition point independent of transcription factor E2F Proc. Natl. Acad. Sci. USA. 93:1996;11516-11521.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11516-11521
    • Van Wijnen, A.J.1    Van Gurp, M.F.2    De Ridder, M.C.3    Tufarelli, C.4    Last, T.J.5    Birnbaum, M.6    Vaughan, P.S.7    Giordano, A.8    Krek, W.9    Neufeld, E.J.10
  • 37
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • Zheng L., Roeder R.G., Luo Y. S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell. 114:2003;255-266.
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.