메뉴 건너뛰기




Volumn 32, Issue 7, 2013, Pages 1036-1051

Structural features within the nascent chain regulate alternative targeting of secretory proteins to mitochondria

Author keywords

endoplasmic reticulum; intrinsically disordered; mitochondria; neurodegeneration; signal peptide

Indexed keywords

AMYLOID PRECURSOR PROTEIN; GLIAL CELL LINE DERIVED NEUROTROPHIC FACTOR RECEPTOR; GLYCOSYLPHOSPHATIDYLINOSITOL; SECRETORY PROTEIN; SIGNAL PEPTIDE; SOMATOSTATIN;

EID: 84875962374     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2013.46     Document Type: Article
Times cited : (32)

References (55)
  • 1
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada HK, Biswas G, Robin MA, Avadhani NG (2003) Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J Cell Biol 161, 41-54
    • (2003) J Cell Biol , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3    Avadhani, N.G.4
  • 2
    • 80255136273 scopus 로고    scopus 로고
    • Bimodal targeting of cytochrome P450s to endoplasmic reticulum and mitochondria: The concept of chimeric signals
    • Avadhani NG, Sangar MC, Bansal S, Bajpai P (2011) Bimodal targeting of cytochrome P450s to endoplasmic reticulum and mitochondria: the concept of chimeric signals. FEBS J 278, 4218-4229
    • (2011) FEBS J , vol.278 , pp. 4218-4229
    • Avadhani, N.G.1    Sangar, M.C.2    Bansal, S.3    Bajpai, P.4
  • 3
    • 81855185408 scopus 로고    scopus 로고
    • A third of the yeast mitochondrial proteome is dual localized: A question of evolution
    • Ben-Menachem R, Tal M, Shadur T, Pines O (2011) A third of the yeast mitochondrial proteome is dual localized: a question of evolution. Proteomics 11, 4468-4476
    • (2011) Proteomics , vol.11 , pp. 4468-4476
    • Ben-Menachem, R.1    Tal, M.2    Shadur, T.3    Pines, O.4
  • 5
    • 60349127044 scopus 로고    scopus 로고
    • Protein transport in organelles: Dual targeting of proteins to mitochondria and chloroplasts
    • Carrie C, Giraud E, Whelan J (2009) Protein transport in organelles: dual targeting of proteins to mitochondria and chloroplasts. FEBS J 276, 1187-1195
    • (2009) FEBS J , vol.276 , pp. 1187-1195
    • Carrie, C.1    Giraud, E.2    Whelan, J.3
  • 6
    • 66449124518 scopus 로고    scopus 로고
    • Functional depletion of mahogunin by cytosolically exposed prion protein contributes to neurode-generation
    • Chakrabarti O, Hegde RS (2009) Functional depletion of mahogunin by cytosolically exposed prion protein contributes to neurode-generation. Cell 137, 1136-1147
    • (2009) Cell , vol.137 , pp. 1136-1147
    • Chakrabarti, O.1    Hegde, R.S.2
  • 9
    • 51049088654 scopus 로고    scopus 로고
    • Control of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome
    • Daniel CJ, Conti B, Johnson AE, Skach WR (2008) Control of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome. J Biol Chem 283, 20864-20873
    • (2008) J Biol Chem , vol.283 , pp. 20864-20873
    • Daniel, C.J.1    Conti, B.2    Johnson, A.E.3    Skach, W.R.4
  • 10
    • 0029015912 scopus 로고
    • How can the products of a single gene be localized to more than one intracellular compartment?
    • Danpure CJ (1995) How can the products of a single gene be localized to more than one intracellular compartment? Trends Cell Biol 5, 230-238
    • (1995) Trends Cell Biol , vol.5 , pp. 230-238
    • Danpure, C.J.1
  • 12
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mito-chondrial dysfunction
    • Devi L, Prabhu BM, Galati DF, Avadhani NG, Anandatheerthavarada HK (2006) Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mito-chondrial dysfunction. J Neurosci 26, 9057-9068
    • (2006) J Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 13
    • 0037007448 scopus 로고    scopus 로고
    • Folding and intrinsic stability of deletion variants of PrP(121-231), the folded C-terminal domain of the prion protein
    • Eberl H, Glockshuber R (2002) Folding and intrinsic stability of deletion variants of PrP(121-231), the folded C-terminal domain of the prion protein. Biophys Chem 96, 293-303
    • (2002) Biophys Chem , vol.96 , pp. 293-303
    • Eberl, H.1    Glockshuber, R.2
  • 14
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300, 1005-1016
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 15
    • 84859494186 scopus 로고    scopus 로고
    • Fuzzy complexes: A more stochastic view of protein function
    • Fuxreiter M, Tompa P (2012) Fuzzy complexes: a more stochastic view of protein function. Adv Exp Med Biol 725, 1-14
    • (2012) Adv Exp Med Biol , vol.725 , pp. 1-14
    • Fuxreiter, M.1    Tompa, P.2
  • 18
    • 41149144037 scopus 로고    scopus 로고
    • Pathogenic mutations in the glycosylphosphatidylinositol signal peptide of PrP modulate its topology in neuroblastoma cells
    • Gu Y, Singh A, Bose S, Singh N (2008) Pathogenic mutations in the glycosylphosphatidylinositol signal peptide of PrP modulate its topology in neuroblastoma cells. Mol Cell Neurosci 37, 647-656
    • (2008) Mol Cell Neurosci , vol.37 , pp. 647-656
    • Gu, Y.1    Singh, A.2    Bose, S.3    Singh, N.4
  • 19
    • 48249151759 scopus 로고    scopus 로고
    • The concept of translocational regulation
    • Hegde RS, Kang SW (2008) The concept of translocational regulation. J Cell Biol 182, 225-232
    • (2008) J Cell Biol , vol.182 , pp. 225-232
    • Hegde, R.S.1    Kang, S.W.2
  • 20
    • 1242339661 scopus 로고    scopus 로고
    • The C-terminal domain of the prion protein is necessary and sufficient for import into the endoplasmic reticulum
    • Heske J, Heller U, Winklhofer KF, Tatzelt J (2004) The C-terminal domain of the prion protein is necessary and sufficient for import into the endoplasmic reticulum. J Biol Chem 279, 5435-5443
    • (2004) J Biol Chem , vol.279 , pp. 5435-5443
    • Heske, J.1    Heller, U.2    Winklhofer, K.F.3    Tatzelt, J.4
  • 21
    • 79960637590 scopus 로고    scopus 로고
    • Protein targeting and degradation are coupled for elimination of mislocalized proteins
    • Hessa T, Sharma A, Mariappan M, Eshleman HD, Gutierrez E, Hegde RS (2011) Protein targeting and degradation are coupled for elimination of mislocalized proteins. Nature 475, 394-397
    • (2011) Nature , vol.475 , pp. 394-397
    • Hessa, T.1    Sharma, A.2    Mariappan, M.3    Eshleman, H.D.4    Gutierrez, E.5    Hegde, R.S.6
  • 22
    • 0035918202 scopus 로고    scopus 로고
    • Prion protein contains a second endoplasmic reticulum targeting signal sequence located at its C terminus
    • Holscher C, Bach UC, Dobberstein B (2001) Prion protein contains a second endoplasmic reticulum targeting signal sequence located at its C terminus. J Biol Chem 276, 13388-13394
    • (2001) J Biol Chem , vol.276 , pp. 13388-13394
    • Holscher, C.1    Bach, U.C.2    Dobberstein, B.3
  • 23
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang SW, Rane NS, Kim SJ, Garrison JL, Taunton J, Hegde RS (2006) Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127, 999-1013
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1    Rane, N.S.2    Kim, S.J.3    Garrison, J.L.4    Taunton, J.5    Hegde, R.S.6
  • 24
    • 20044387943 scopus 로고    scopus 로고
    • Single translation-dual destination: Mechanisms of dual protein targeting in eukaryotes
    • Karniely S, Pines O (2005) Single translation-dual destination: mechanisms of dual protein targeting in eukaryotes. EMBO Rep 6, 420-425
    • (2005) EMBO Rep , vol.6 , pp. 420-425
    • Karniely, S.1    Pines, O.2
  • 25
    • 0026081504 scopus 로고
    • A motif found in propeptides and prohormones that may target them to secretory vesicles
    • Kizer JS, Tropsha A (1991) A motif found in propeptides and prohormones that may target them to secretory vesicles. Biochem Biophys Res Commun 174, 586-592
    • (1991) Biochem Biophys Res Commun , vol.174 , pp. 586-592
    • Kizer, J.S.1    Tropsha, A.2
  • 27
    • 80053991771 scopus 로고    scopus 로고
    • Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the translocon
    • Lin PJ, Jongsma CG, Pool MR, Johnson AE (2011) Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the translocon. J Cell Biol 195, 55-70
    • (2011) J Cell Biol , vol.195 , pp. 55-70
    • Lin, P.J.1    Jongsma, C.G.2    Pool, M.R.3    Johnson, A.E.4
  • 28
    • 84859499620 scopus 로고    scopus 로고
    • The measles virus N(TAIL)-XD complex: An illustrative example of fuzziness
    • Longhi S (2012) The measles virus N(TAIL)-XD complex: an illustrative example of fuzziness. Adv Exp Med Biol 725, 126-141
    • (2012) Adv Exp Med Biol , vol.725 , pp. 126-141
    • Longhi, S.1
  • 29
    • 20444430500 scopus 로고    scopus 로고
    • Secondary structure formation of a transmembrane segment in Kv channels
    • Lu J, Deutsch C (2005) Secondary structure formation of a transmembrane segment in Kv channels. Biochemistry 44, 8230-8243
    • (2005) Biochemistry , vol.44 , pp. 8230-8243
    • Lu, J.1    Deutsch, C.2
  • 30
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurode-generation when PrP accumulates in the cytosol
    • Ma J, Wollmann R, Lindquist S (2002) Neurotoxicity and neurode-generation when PrP accumulates in the cytosol. Science 298, 1781-1785
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 33
    • 0012249596 scopus 로고    scopus 로고
    • Different conformations of nascent polypeptides during translocation across the ER membrane
    • Mingarro I, Nilsson I, Whitley P, von Heijne G (2000) Different conformations of nascent polypeptides during translocation across the ER membrane. BMC Cell Biol 1: 3
    • (2000) BMC Cell Biol , vol.1 , pp. 3
    • Mingarro, I.1    Nilsson, I.2    Whitley, P.3    Von Heijne, G.4
  • 34
    • 0027270310 scopus 로고
    • Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein
    • Nuoffer C, Horvath A, Riezman H (1993) Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein. J Biol Chem 268, 10558-10563
    • (1993) J Biol Chem , vol.268 , pp. 10558-10563
    • Nuoffer, C.1    Horvath, A.2    Riezman, H.3
  • 36
    • 0029177168 scopus 로고
    • Processing and intracellular targeting of prosomatostatin-derived peptides: The role of mammalian endoproteases
    • discussion 40-50
    • Patel YC, Galanopoulou A (1995) Processing and intracellular targeting of prosomatostatin-derived peptides: the role of mammalian endoproteases. Ciba Found Symp 190: 26-40 discussion 40-50
    • (1995) Ciba Found Symp , vol.190 , pp. 26-40
    • Patel, Y.C.1    Galanopoulou, A.2
  • 37
    • 55549141494 scopus 로고    scopus 로고
    • Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3
    • Petrova K, Oyadomari S, Hendershot LM, Ron D (2008) Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. EMBO J 27, 2862-2872
    • (2008) EMBO J , vol.27 , pp. 2862-2872
    • Petrova, K.1    Oyadomari, S.2    Hendershot, L.M.3    Ron, D.4
  • 40
    • 79953174915 scopus 로고    scopus 로고
    • Conserved stress-protective activity between prion protein and shadoo
    • Sakthivelu V, Seidel RP, Winklhofer KF, Tatzelt J (2011) Conserved stress-protective activity between prion protein and shadoo. J Biol Chem 286, 8901-8908
    • (2011) J Biol Chem , vol.286 , pp. 8901-8908
    • Sakthivelu, V.1    Seidel, R.P.2    Winklhofer, K.F.3    Tatzelt, J.4
  • 41
    • 26444571807 scopus 로고    scopus 로고
    • Regulation of protein compartmentalization expands the diversity of protein function
    • Shaffer KL, Sharma A, Snapp EL, Hegde RS (2005) Regulation of protein compartmentalization expands the diversity of protein function. Dev Cell 9, 545-554
    • (2005) Dev Cell , vol.9 , pp. 545-554
    • Shaffer, K.L.1    Sharma, A.2    Snapp, E.L.3    Hegde, R.S.4
  • 42
    • 0032168849 scopus 로고    scopus 로고
    • Two birds with one stone: Genes that encode products targeted to two or more compartments
    • Small I, Wintz H, Akashi K, Mireau H (1998) Two birds with one stone: genes that encode products targeted to two or more compartments. Plant Mol Biol 38, 265-277
    • (1998) Plant Mol Biol , vol.38 , pp. 265-277
    • Small, I.1    Wintz, H.2    Akashi, K.3    Mireau, H.4
  • 43
    • 84861329438 scopus 로고
    • The MIA pathway: A tight bond between protein transport and oxidative folding in mitochondria
    • Stojanovski D, Bragoszewski P, Chacinska A (2012) The MIA pathway: A tight bond between protein transport and oxidative folding in mitochondria. Biochim Biophys Acta 1823, 1142-1150
    • (1823) Biochim Biophys Acta , pp. 1142-1150
    • Stojanovski, D.1    Bragoszewski, P.2    Chacinska, A.3
  • 44
    • 65249102824 scopus 로고    scopus 로고
    • Close encounters of the third kind: Disordered domains and the interactions of proteins
    • Tompa P, Fuxreiter M, Oldfield CJ, Simon I, Dunker AK, Uversky VN (2009) Close encounters of the third kind: disordered domains and the interactions of proteins. Bioessays 31, 328-335
    • (2009) Bioessays , vol.31 , pp. 328-335
    • Tompa, P.1    Fuxreiter, M.2    Oldfield, C.J.3    Simon, I.4    Dunker, A.K.5    Uversky, V.N.6
  • 50
    • 0029983258 scopus 로고    scopus 로고
    • A nascent secretory protein may traverse the ribosome endoplasmic reticulum translocase complex as an extended chain
    • Whitley P, Nilsson I, Vonheijne G (1996) A nascent secretory protein may traverse the ribosome endoplasmic reticulum translocase complex as an extended chain. J Biol Chem 271, 6241-6244
    • (1996) J Biol Chem , vol.271 , pp. 6241-6244
    • Whitley, P.1    Nilsson, I.2    Vonheijne, G.3
  • 51
    • 0037665405 scopus 로고    scopus 로고
    • Determinants of the in vivo-folding of the prion protein: A bipartite function of helix 1 in folding and aggregation
    • Winklhofer KF, Heske J, Heller U, Reintjes A, Muranji W, Moarefi I, Tatzelt J (2003) Determinants of the in vivo-folding of the prion protein: a bipartite function of helix 1 in folding and aggregation. J Biol Chem 278, 14961-14970
    • (2003) J Biol Chem , vol.278 , pp. 14961-14970
    • Winklhofer, K.F.1    Heske, J.2    Heller, U.3    Reintjes, A.4    Muranji, W.5    Moarefi, I.6    Tatzelt, J.7
  • 52
    • 33744551950 scopus 로고    scopus 로고
    • Translation arrest requires two-way communication between a nascent polypeptide and the ribosome
    • Woolhead CA, Johnson AE, Bernstein HD (2006) Translation arrest requires two-way communication between a nascent polypeptide and the ribosome. Mol Cell 22, 587-598
    • (2006) Mol Cell , vol.22 , pp. 587-598
    • Woolhead, C.A.1    Johnson, A.E.2    Bernstein, H.D.3
  • 53
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • Woolhead CA, McCormick PJ, Johnson AE (2004) Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 116, 725-736
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 54
    • 80255122737 scopus 로고    scopus 로고
    • Fumarase: A paradigm of dual targeting and dual localized functions
    • Yogev O, Naamati A, Pines O (2011) Fumarase: a paradigm of dual targeting and dual localized functions. FEBS J 278, 4230-4242
    • (2011) FEBS J , vol.278 , pp. 4230-4242
    • Yogev, O.1    Naamati, A.2    Pines, O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.