메뉴 건너뛰기




Volumn 32, Issue 1, 2008, Pages 32-42

Bimodal Protein Targeting through Activation of Cryptic Mitochondrial Targeting Signals by an Inducible Cytosolic Endoprotease

Author keywords

CELLBIO; PROTEINS

Indexed keywords

CYTOCHROME P450 1A1; GLUCOCORTICOID RECEPTOR; PROTEIN P53; PROTEIN SUBUNIT; RETINOID X RECEPTOR; SERINE PROTEINASE;

EID: 53149085250     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2008.09.008     Document Type: Article
Times cited : (43)

References (47)
  • 2
    • 0033525755 scopus 로고    scopus 로고
    • Physiological role of the N-terminal processed P4501A1 targeted to mitochondria in erythromycin metabolism and reversal of erythromycin-mediated inhibition of mitochondrial protein synthesis
    • Anandatheerthavarada H.K., Vijayasarathy C., Bhagwat S.V., Biswas G., Mullick J., and Avadhani N.G. Physiological role of the N-terminal processed P4501A1 targeted to mitochondria in erythromycin metabolism and reversal of erythromycin-mediated inhibition of mitochondrial protein synthesis. J. Biol. Chem. 274 (1999) 6617-6625
    • (1999) J. Biol. Chem. , vol.274 , pp. 6617-6625
    • Anandatheerthavarada, H.K.1    Vijayasarathy, C.2    Bhagwat, S.V.3    Biswas, G.4    Mullick, J.5    Avadhani, N.G.6
  • 3
    • 50349099993 scopus 로고    scopus 로고
    • An unusual TOM20/TOM22 bypass mechanism for the mitochondrial targeting of cytochrome P450 proteins containing N-terminal chimeric signals
    • Anandatheerthavarada H.K., Sepuri N.B., Biswas G., and Avadhani N.G. An unusual TOM20/TOM22 bypass mechanism for the mitochondrial targeting of cytochrome P450 proteins containing N-terminal chimeric signals. J. Biol. Chem. 283 (2008) 19769-19780
    • (2008) J. Biol. Chem. , vol.283 , pp. 19769-19780
    • Anandatheerthavarada, H.K.1    Sepuri, N.B.2    Biswas, G.3    Avadhani, N.G.4
  • 4
    • 0034863016 scopus 로고    scopus 로고
    • Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease
    • Batra R., Khayat R., and Tong L. Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease. Nat. Struct. Biol. 8 (2001) 810-817
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 810-817
    • Batra, R.1    Khayat, R.2    Tong, L.3
  • 5
    • 0038392751 scopus 로고    scopus 로고
    • The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity
    • Bell J.K., Goetz D.H., Mahrus S., Harris J.L., Fletterick R.J., and Craik C.S. The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity. Nat. Struct. Biol. 10 (2003) 527-534
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 527-534
    • Bell, J.K.1    Goetz, D.H.2    Mahrus, S.3    Harris, J.L.4    Fletterick, R.J.5    Craik, C.S.6
  • 6
    • 0033588378 scopus 로고    scopus 로고
    • Dual Targeting Property of the N-terminal Signal Sequence of P4501A1. Targeting of heterologous proteins to endoplasmic reticulum and mitochondria
    • Bhagwat S.V., Biswas G., Anandatheerthavarada H.K., Addya S., Pandak W., and Avadhani N.G. Dual Targeting Property of the N-terminal Signal Sequence of P4501A1. Targeting of heterologous proteins to endoplasmic reticulum and mitochondria. J. Biol. Chem. 274 (1999) 24014-24022
    • (1999) J. Biol. Chem. , vol.274 , pp. 24014-24022
    • Bhagwat, S.V.1    Biswas, G.2    Anandatheerthavarada, H.K.3    Addya, S.4    Pandak, W.5    Avadhani, N.G.6
  • 7
  • 8
    • 0034602392 scopus 로고    scopus 로고
    • Accumulation of mitochondrial P450MT2, NH(2)-terminal truncated cytochrome P4501A1 in rat brain during chronic treatment with beta-naphthoflavone. A role in the metabolism of neuroactive drugs
    • Boopathi E., Anandatheerthavarada H.K., Bhagwat S.V., Biswas G., Fang J.K., and Avadhani N.G. Accumulation of mitochondrial P450MT2, NH(2)-terminal truncated cytochrome P4501A1 in rat brain during chronic treatment with beta-naphthoflavone. A role in the metabolism of neuroactive drugs. J. Biol. Chem. 275 (2000) 34415-34423
    • (2000) J. Biol. Chem. , vol.275 , pp. 34415-34423
    • Boopathi, E.1    Anandatheerthavarada, H.K.2    Bhagwat, S.V.3    Biswas, G.4    Fang, J.K.5    Avadhani, N.G.6
  • 9
    • 0041923832 scopus 로고    scopus 로고
    • Polyserase-I, a human polyprotease with the ability to generate independent Ser protease domains from a single translation product
    • Cal S., Quesada V., Garabaya C., and Lopez-Otin C. Polyserase-I, a human polyprotease with the ability to generate independent Ser protease domains from a single translation product. Proc. Natl. Acad. Sci. USA 100 (2003) 9185-9190
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9185-9190
    • Cal, S.1    Quesada, V.2    Garabaya, C.3    Lopez-Otin, C.4
  • 10
    • 12544258994 scopus 로고    scopus 로고
    • Human polyserase-2, a novel enzyme with three tandem Ser protease domains in a single polypeptide chain
    • Cal S., Quesada V., Llamazares M., Díaz-Perales A., Garabaya C., and López-Otín C. Human polyserase-2, a novel enzyme with three tandem Ser protease domains in a single polypeptide chain. J. Biol. Chem. 280 (2005) 1953-1961
    • (2005) J. Biol. Chem. , vol.280 , pp. 1953-1961
    • Cal, S.1    Quesada, V.2    Llamazares, M.3    Díaz-Perales, A.4    Garabaya, C.5    López-Otín, C.6
  • 12
    • 14944380621 scopus 로고    scopus 로고
    • Estrogen's effects on mitochondrial gene expression: mechanisms and potential contributions to estrogen carcinogenesis
    • Chen J.Q., and Yager J.D. Estrogen's effects on mitochondrial gene expression: mechanisms and potential contributions to estrogen carcinogenesis. Ann. N Y Acad. Sci. 1028 (2004) 258-272
    • (2004) Ann. N Y Acad. Sci. , vol.1028 , pp. 258-272
    • Chen, J.Q.1    Yager, J.D.2
  • 13
    • 33750041948 scopus 로고    scopus 로고
    • Role of protein kinase C-mediated protein phosphorylation in mitochondrial translocation of mouse CYP1A1, which contains a non-canonical targeting signal
    • Dasari V.R., Anandatheerthavarada H.K., Robin M.A., Boopathi E., Biswas G., Fang J.K., Nebert D.W., and Avadhani N.G. Role of protein kinase C-mediated protein phosphorylation in mitochondrial translocation of mouse CYP1A1, which contains a non-canonical targeting signal. J. Biol. Chem. 281 (2006) 30834-30847
    • (2006) J. Biol. Chem. , vol.281 , pp. 30834-30847
    • Dasari, V.R.1    Anandatheerthavarada, H.K.2    Robin, M.A.3    Boopathi, E.4    Biswas, G.5    Fang, J.K.6    Nebert, D.W.7    Avadhani, N.G.8
  • 14
    • 0030042248 scopus 로고    scopus 로고
    • Internal targeting signal of the BCS1 protein: a novel mechanism of import into mitochondria
    • Fölsch H., Guiard B., Neupert W., and Stuart R.A. Internal targeting signal of the BCS1 protein: a novel mechanism of import into mitochondria. EMBO J. 15 (1996) 479-487
    • (1996) EMBO J. , vol.15 , pp. 479-487
    • Fölsch, H.1    Guiard, B.2    Neupert, W.3    Stuart, R.A.4
  • 15
    • 0034651865 scopus 로고    scopus 로고
    • Proteases in the evaluation of pancreatic function and pancreatic disease
    • Goldberg D.M. Proteases in the evaluation of pancreatic function and pancreatic disease. Clin. Chim. Acta 291 (2000) 201-221
    • (2000) Clin. Chim. Acta , vol.291 , pp. 201-221
    • Goldberg, D.M.1
  • 16
    • 0015889117 scopus 로고
    • The properties of subunits of avidin coupled to sepharose
    • Green N.M., and Toms E.J. The properties of subunits of avidin coupled to sepharose. Biochem. J. 133 (1973) 687-700
    • (1973) Biochem. J. , vol.133 , pp. 687-700
    • Green, N.M.1    Toms, E.J.2
  • 17
    • 34347210331 scopus 로고    scopus 로고
    • Activation of a novel calcineurin-mediated insulin-like growth factor-1 receptor pathway, altered metabolism, and tumor cell invasion in cells subjected to mitochondrial respiratory stress
    • Guha M., Srinivasan S., Biswas G., and Avadhani N.G. Activation of a novel calcineurin-mediated insulin-like growth factor-1 receptor pathway, altered metabolism, and tumor cell invasion in cells subjected to mitochondrial respiratory stress. J. Biol. Chem. 282 (2007) 14536-14546
    • (2007) J. Biol. Chem. , vol.282 , pp. 14536-14546
    • Guha, M.1    Srinivasan, S.2    Biswas, G.3    Avadhani, N.G.4
  • 18
    • 0028948675 scopus 로고
    • The yeast mitochondrial protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence
    • Haucke V., Lithgow T., Rospert S., Hahne K., and Schatz G. The yeast mitochondrial protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence. J. Biol. Chem. 270 (1995) 5565-5570
    • (1995) J. Biol. Chem. , vol.270 , pp. 5565-5570
    • Haucke, V.1    Lithgow, T.2    Rospert, S.3    Hahne, K.4    Schatz, G.5
  • 19
    • 0018791190 scopus 로고
    • An avidin monomer affinity column for the purification of biotin-containing enzymes
    • Henrikson K.P., Allen S., and Maloy H.W.L. An avidin monomer affinity column for the purification of biotin-containing enzymes. Anal. Biochem. 94 (1979) 366-370
    • (1979) Anal. Biochem. , vol.94 , pp. 366-370
    • Henrikson, K.P.1    Allen, S.2    Maloy, H.W.L.3
  • 20
    • 0036499914 scopus 로고    scopus 로고
    • Oviductin, the Oviductal Protease That Mediates Gamete Interaction by Affecting the Vitelline Coat in Bufo japonicus: Its Molecular Cloning and Analyses of Expression and Posttranslational Activation
    • Hiyoshi M., Takamune K., Mita K., Kubo H., Sugimoto Y., and Katagiri C. Oviductin, the Oviductal Protease That Mediates Gamete Interaction by Affecting the Vitelline Coat in Bufo japonicus: Its Molecular Cloning and Analyses of Expression and Posttranslational Activation. Dev. Biol. 243 (2002) 176-184
    • (2002) Dev. Biol. , vol.243 , pp. 176-184
    • Hiyoshi, M.1    Takamune, K.2    Mita, K.3    Kubo, H.4    Sugimoto, Y.5    Katagiri, C.6
  • 21
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosom
    • Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosom. Cell 44 (1986) 283-292
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 22
    • 0242266463 scopus 로고    scopus 로고
    • The dynamic localization of the glucocorticoid receptor in rat C6 glioma cell mitochondria
    • Koufali M.M., Moutsatsou P., Sekeris C.E., and Breen K.C. The dynamic localization of the glucocorticoid receptor in rat C6 glioma cell mitochondria. Mol. Cell. Endocrinol. 209 (2003) 51-60
    • (2003) Mol. Cell. Endocrinol. , vol.209 , pp. 51-60
    • Koufali, M.M.1    Moutsatsou, P.2    Sekeris, C.E.3    Breen, K.C.4
  • 23
    • 0035876166 scopus 로고    scopus 로고
    • Molecular markers of Ser protease evolution
    • Krem M.M., and Cera D.E. Molecular markers of Ser protease evolution. EMBO J. 20 (2001) 3036-3045
    • (2001) EMBO J. , vol.20 , pp. 3036-3045
    • Krem, M.M.1    Cera, D.E.2
  • 24
    • 33646465530 scopus 로고    scopus 로고
    • Purification of liver Ser protease which activates microsomal glutathione S-transferase: possible involvement of hepsin
    • Kunii D., Shimoji M., Nakama S., Ikebe M., Hachiman T., Sato I., Tamaki A., Yamazaki K., and Aniya Y. Purification of liver Ser protease which activates microsomal glutathione S-transferase: possible involvement of hepsin. Biol. Pharm. Bull. 29 (2006) 868-874
    • (2006) Biol. Pharm. Bull. , vol.29 , pp. 868-874
    • Kunii, D.1    Shimoji, M.2    Nakama, S.3    Ikebe, M.4    Hachiman, T.5    Sato, I.6    Tamaki, A.7    Yamazaki, K.8    Aniya, Y.9
  • 25
    • 0033613248 scopus 로고    scopus 로고
    • Ovochymase, a Xenopus laevis egg extracellular protease, is translated as part of an unusual polyprotease
    • Lindsay L.L., Yang J.C., and Hedrick J.L. Ovochymase, a Xenopus laevis egg extracellular protease, is translated as part of an unusual polyprotease. Proc. Natl. Acad. Sci. USA 96 (1999) 11253-11258
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11253-11258
    • Lindsay, L.L.1    Yang, J.C.2    Hedrick, J.L.3
  • 26
    • 45549106857 scopus 로고    scopus 로고
    • A molecular switch for targeting between endoplasmic reticulum (ER) and mitochondria: conversion of a mitochondria-targeted element into ER-Targeting signal in DAKAP1
    • Ma Y., and Taylor S.S. A molecular switch for targeting between endoplasmic reticulum (ER) and mitochondria: conversion of a mitochondria-targeted element into ER-Targeting signal in DAKAP1. J. Biol. Chem. 283 (2008) 11743-11751
    • (2008) J. Biol. Chem. , vol.283 , pp. 11743-11751
    • Ma, Y.1    Taylor, S.S.2
  • 27
    • 0029161894 scopus 로고
    • Biotinylated aprotinin: a versatile probe for the detection of Ser proteinases on western blots
    • Melrose J., Ghosh P., and Patel M. Biotinylated aprotinin: a versatile probe for the detection of Ser proteinases on western blots. Int. J. Biochem. Cell Biol. 27 (1995) 891-904
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 891-904
    • Melrose, J.1    Ghosh, P.2    Patel, M.3
  • 28
    • 0034005954 scopus 로고    scopus 로고
    • Targeting and insertion of nuclear-encoded preproteins into the mitochondrial outer membrane
    • Mihara K. Targeting and insertion of nuclear-encoded preproteins into the mitochondrial outer membrane. Bioessays 22 (2000) 364-391
    • (2000) Bioessays , vol.22 , pp. 364-391
    • Mihara, K.1
  • 30
    • 0022984536 scopus 로고
    • Limited proteolysis of HMW kininogen by plasma kallikrein in man--evidence for a processing mechanism different from the bovine system
    • Müller-Esterl W., Hock H., Rauth G., Kellermann J., Lottspeich F., and Henschen A. Limited proteolysis of HMW kininogen by plasma kallikrein in man--evidence for a processing mechanism different from the bovine system. Adv. Exp. Med. Biol. 198 (1986) 97-103
    • (1986) Adv. Exp. Med. Biol. , vol.198 , pp. 97-103
    • Müller-Esterl, W.1    Hock, H.2    Rauth, G.3    Kellermann, J.4    Lottspeich, F.5    Henschen, A.6
  • 31
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., and Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76 (2007) 723-749
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 32
    • 0021680784 scopus 로고
    • Hepatic mitochondrial cytochrome P-450 system. Distinctive features of cytochrome P-450 involved in the activation of aflatoxin B1 and benzo(a)pyrene
    • Niranjan B.G., Wilson N.M., and Jefcoate C.R. Hepatic mitochondrial cytochrome P-450 system. Distinctive features of cytochrome P-450 involved in the activation of aflatoxin B1 and benzo(a)pyrene. J. Biol. Chem. 259 (1984) 12495-12501
    • (1984) J. Biol. Chem. , vol.259 , pp. 12495-12501
    • Niranjan, B.G.1    Wilson, N.M.2    Jefcoate, C.R.3
  • 33
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the Ser proteases
    • Perona J.J., and Craik C.S. Structural basis of substrate specificity in the Ser proteases. Protein Sci. 4 (1995) 337-360
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 34
    • 0026057311 scopus 로고
    • Mitochondrial import receptors for precursor proteins
    • Pfanner N., Söllner T., and Neupert W. Mitochondrial import receptors for precursor proteins. Trends Biochem. Sci. 16 (1991) 63-67
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 63-67
    • Pfanner, N.1    Söllner, T.2    Neupert, W.3
  • 37
    • 0242607644 scopus 로고    scopus 로고
    • Finding the right organelle
    • Rapaport D. Finding the right organelle. EMBO Rep. 4 (2003) 948-952
    • (2003) EMBO Rep. , vol.4 , pp. 948-952
    • Rapaport, D.1
  • 38
    • 0037174926 scopus 로고    scopus 로고
    • Bimodal targeting of microsomal CYP2E1 to mitochondria through activation of an N-terminal chimeric signal by cAMP-mediated phosphorylation
    • Robin M.A., Anandatheerthavarada H.K., Biswas G., Sepuri N.P., Cordon D.M., Pain D., and Avadhani N.G. Bimodal targeting of microsomal CYP2E1 to mitochondria through activation of an N-terminal chimeric signal by cAMP-mediated phosphorylation. J. Biochem. (Tokyo) 277 (2002) 40583-40593
    • (2002) J. Biochem. (Tokyo) , vol.277 , pp. 40583-40593
    • Robin, M.A.1    Anandatheerthavarada, H.K.2    Biswas, G.3    Sepuri, N.P.4    Cordon, D.M.5    Pain, D.6    Avadhani, N.G.7
  • 39
    • 0038482043 scopus 로고    scopus 로고
    • Phosphorylation enhances mitochondrial targeting of GSTA4-4 through increased affinity for binding to cytoplasmic Hsp70
    • Robin M.A., Prabu S.K., Raza H., Anandatheerthavarada H.K., and Avadhani N.G. Phosphorylation enhances mitochondrial targeting of GSTA4-4 through increased affinity for binding to cytoplasmic Hsp70. J. Biol. Chem. 278 (2003) 18960-18970
    • (2003) J. Biol. Chem. , vol.278 , pp. 18960-18970
    • Robin, M.A.1    Prabu, S.K.2    Raza, H.3    Anandatheerthavarada, H.K.4    Avadhani, N.G.5
  • 40
    • 0023920458 scopus 로고
    • Mitochondrial presequences
    • Roise D., and Schatz G. Mitochondrial presequences. J. Biol. Chem. 263 (1988) 4509-4511
    • (1988) J. Biol. Chem. , vol.263 , pp. 4509-4511
    • Roise, D.1    Schatz, G.2
  • 41
    • 0037472685 scopus 로고    scopus 로고
    • Ser proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships
    • Ross J., Jiang H., Kanost M.R., and Wang Y. Ser proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships. Gene 304 (2003) 117-131
    • (2003) Gene , vol.304 , pp. 117-131
    • Ross, J.1    Jiang, H.2    Kanost, M.R.3    Wang, Y.4
  • 44
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne G. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341 (1989) 456-458
    • (1989) Nature , vol.341 , pp. 456-458
    • von Heijne, G.1
  • 45
    • 0022555426 scopus 로고
    • The regulation of Cytochrome P-450 gene expression
    • Whitlock J.P. The regulation of Cytochrome P-450 gene expression. Annu. Rev. Pharmacol. Toxicol. 26 (1986) 333-369
    • (1986) Annu. Rev. Pharmacol. Toxicol. , vol.26 , pp. 333-369
    • Whitlock, J.P.1
  • 46
    • 23344450788 scopus 로고    scopus 로고
    • Induction of phase I, II and III drug metabolism/transport by xenobiotics
    • Xu C., Li C.Y., and Kong A.N. Induction of phase I, II and III drug metabolism/transport by xenobiotics. Arch. Pharm. Res. 28 (2005) 249-268
    • (2005) Arch. Pharm. Res. , vol.28 , pp. 249-268
    • Xu, C.1    Li, C.Y.2    Kong, A.N.3
  • 47
    • 0021771144 scopus 로고
    • Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MC
    • Yabusaki Y., Shimizu M., Murakami H., Nakamura K., Oeda K., and Ohkawa H. Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MC. Nucleic Acids Res. 12 (1984) 2929-2938
    • (1984) Nucleic Acids Res. , vol.12 , pp. 2929-2938
    • Yabusaki, Y.1    Shimizu, M.2    Murakami, H.3    Nakamura, K.4    Oeda, K.5    Ohkawa, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.