메뉴 건너뛰기




Volumn 33, Issue 5, 2011, Pages 368-376

Making new out of old: Recycling and modification of an ancient protein translocation system during eukaryotic evolution

Author keywords

ERAD; Evolution of protein translocation; Peroxisomal importomer; Secondary plastid; SELMA

Indexed keywords

ADENOSINE TRIPHOSPHATASE; UBIQUITIN PROTEIN LIGASE;

EID: 79954779971     PISSN: 02659247     EISSN: 15211878     Source Type: Journal    
DOI: 10.1002/bies.201100007     Document Type: Review
Times cited : (32)

References (94)
  • 2
    • 77955663100 scopus 로고    scopus 로고
    • The evolution of protein targeting and translocation systems
    • Bohnsack MT, Schleiff E. 2010. The evolution of protein targeting and translocation systems. Biochim Biophys Acta 1803: 1115-30.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 1115-1130
    • Bohnsack, M.T.1    Schleiff, E.2
  • 3
    • 73749085583 scopus 로고    scopus 로고
    • Comparative and evolutionary aspects of macromolecular translocation across membranes
    • Tartakoff AM, Tao T. 2010. Comparative and evolutionary aspects of macromolecular translocation across membranes. Int J Biochem Cell Biol 42: 214-29.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 214-229
    • Tartakoff, A.M.1    Tao, T.2
  • 4
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen AJ, Nouwen N. 2008. Protein translocation across the bacterial cytoplasmic membrane. Annu Rev Biochem 77: 643-67.
    • (2008) Annu Rev Biochem , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 6
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport TA. 2007. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450: 663-9.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 8
    • 0033582158 scopus 로고    scopus 로고
    • The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog
    • Reumann S, Davila-Aponte J, Keegstra K. 1999. The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog. Proc Natl Acad Sci USA 96: 784-9.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 784-789
    • Reumann, S.1    Davila-Aponte, J.2    Keegstra, K.3
  • 9
    • 58149513082 scopus 로고    scopus 로고
    • Revaluating the evolution of the Toc and Tic protein translocons
    • Gross J, Bhattacharya D. 2009. Revaluating the evolution of the Toc and Tic protein translocons. Trends Plant Sci 14: 13-20.
    • (2009) Trends Plant Sci , vol.14 , pp. 13-20
    • Gross, J.1    Bhattacharya, D.2
  • 10
    • 0033179289 scopus 로고    scopus 로고
    • The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes
    • Reumann S, Keegstra K. 1999. The endosymbiotic origin of the protein import machinery of chloroplastic envelope membranes. Trends Plant Sci 4: 302-7.
    • (1999) Trends Plant Sci , vol.4 , pp. 302-307
    • Reumann, S.1    Keegstra, K.2
  • 11
    • 30944458601 scopus 로고    scopus 로고
    • Toc, Tic, Tat structure and function of protein transport machineries in chloroplasts
    • Gutensohn M, Fan E, Frielingsdorf S, Hanner P, et al. 2006. Toc, Tic, Tat et al.: structure and function of protein transport machineries in chloroplasts. J Plant Physiol 163: 333-47.
    • (2006) J Plant Physiol , vol.163 , pp. 333-347
    • Gutensohn, M.1    Fan, E.2    Frielingsdorf, S.3    Hanner, P.4
  • 12
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal P, Likic V, Tachezy J, Lithgow T. 2006. Evolution of the molecular machines for protein import into mitochondria. Science 313: 314-8.
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 13
    • 77953811604 scopus 로고    scopus 로고
    • Structure and evolution of mitochondrial outer membrane proteins of beta-barrel topology
    • Zeth K. 2010. Structure and evolution of mitochondrial outer membrane proteins of beta-barrel topology. Biochim Biophys Acta 1797: 1292-9.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1292-1299
    • Zeth, K.1
  • 16
    • 43149096666 scopus 로고    scopus 로고
    • The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum
    • Nakatsukasa K, Brodsky JL. 2008. The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic 9: 861-70.
    • (2008) Traffic , vol.9 , pp. 861-870
    • Nakatsukasa, K.1    Brodsky, J.L.2
  • 18
    • 78649403829 scopus 로고    scopus 로고
    • Peroxisomal protein import and ERAD: variations on a common theme
    • Schliebs W, Girzalsky W, Erdmann R. 2010. Peroxisomal protein import and ERAD: variations on a common theme. Nat Rev Mol Cell Biol 11: 885-90.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 885-890
    • Schliebs, W.1    Girzalsky, W.2    Erdmann, R.3
  • 19
    • 33644907201 scopus 로고    scopus 로고
    • The evolutionary origin of peroxisomes: an ER-peroxisome connection
    • Schluter A, Fourcade S, Ripp R, Mandel JL, et al. 2006. The evolutionary origin of peroxisomes: an ER-peroxisome connection. Mol Biol Evol 23: 838-45.
    • (2006) Mol Biol Evol , vol.23 , pp. 838-845
    • Schluter, A.1    Fourcade, S.2    Ripp, R.3    Mandel, J.L.4
  • 21
    • 79954771065 scopus 로고    scopus 로고
    • ERAD components in organisms with complex red plastids suggest recruitment of a preexisting protein transport pathway for the periplastid membrane
    • Felsner G, Sommer MS, Gruenheit N, Hempel F, et al. 2011. ERAD components in organisms with complex red plastids suggest recruitment of a preexisting protein transport pathway for the periplastid membrane. Genome Biol Evol 3: 140-50.
    • (2011) Genome Biol Evol , vol.3 , pp. 140-150
    • Felsner, G.1    Sommer, M.S.2    Gruenheit, N.3    Hempel, F.4
  • 22
    • 67749095912 scopus 로고    scopus 로고
    • ERAD-derived preprotein transport across the second outermost plastid membrane of diatoms
    • Hempel F, Bullmann L, Lau J, Zauner S, et al. 2009. ERAD-derived preprotein transport across the second outermost plastid membrane of diatoms. Mol Biol Evol 26: 1781-90.
    • (2009) Mol Biol Evol , vol.26 , pp. 1781-1790
    • Hempel, F.1    Bullmann, L.2    Lau, J.3    Zauner, S.4
  • 23
    • 68549083618 scopus 로고    scopus 로고
    • Characterization of two putative protein translocation components in the apicoplast of Plasmodium falciparum
    • Kalanon M, Tonkin CJ, McFadden GI. 2009. Characterization of two putative protein translocation components in the apicoplast of Plasmodium falciparum Eukaryot Cell 8: 1146-54.
    • (2009) Eukaryot Cell , vol.8 , pp. 1146-1154
    • Kalanon, M.1    Tonkin, C.J.2    McFadden, G.I.3
  • 24
    • 34047211982 scopus 로고    scopus 로고
    • Der1-mediated preprotein import into the periplastid compartment of chromalveolates?
    • Sommer MS, Gould SB, Lehmann P, Gruber A, et al. 2007. Der1-mediated preprotein import into the periplastid compartment of chromalveolates? Mol Biol Evol 24: 918-28.
    • (2007) Mol Biol Evol , vol.24 , pp. 918-928
    • Sommer, M.S.1    Gould, S.B.2    Lehmann, P.3    Gruber, A.4
  • 25
    • 68549085312 scopus 로고    scopus 로고
    • An unusual ERAD-like complex is targeted to the apicoplast of Plasmodium falciparum
    • Spork S, Hiss JA, Mandel K, Sommer M, et al. 2009. An unusual ERAD-like complex is targeted to the apicoplast of Plasmodium falciparum Eukaryot Cell 8: 1134-45.
    • (2009) Eukaryot Cell , vol.8 , pp. 1134-1145
    • Spork, S.1    Hiss, J.A.2    Mandel, K.3    Sommer, M.4
  • 26
    • 70450251981 scopus 로고    scopus 로고
    • Genetic evidence that an endosymbiont-derived endoplasmic reticulum-associated protein degradation (ERAD) system functions in import of apicoplast proteins
    • Agrawal S, van Dooren GG, Beatty WL, Striepen B. 2009. Genetic evidence that an endosymbiont-derived endoplasmic reticulum-associated protein degradation (ERAD) system functions in import of apicoplast proteins. J Biol Chem 284: 33683-91.
    • (2009) J Biol Chem , vol.284 , pp. 33683-33691
    • Agrawal, S.1    van Dooren, G.G.2    Beatty, W.L.3    Striepen, B.4
  • 27
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • Carvalho P, Goder V, Rapoport TA. 2006. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 126: 361-73.
    • (2006) Cell , vol.126 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 28
    • 24944583185 scopus 로고    scopus 로고
    • Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen
    • Bhamidipati A, Denic V, Quan EM, Weissman JS. 2005. Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. Mol Cell 19: 741-51.
    • (2005) Mol Cell , vol.19 , pp. 741-751
    • Bhamidipati, A.1    Denic, V.2    Quan, E.M.3    Weissman, J.S.4
  • 29
    • 8844270968 scopus 로고    scopus 로고
    • A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins
    • Buschhorn BA, Kostova Z, Medicherla B, Wolf DH. 2004. A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. FEBS Lett 577: 422-6.
    • (2004) FEBS Lett , vol.577 , pp. 422-426
    • Buschhorn, B.A.1    Kostova, Z.2    Medicherla, B.3    Wolf, D.H.4
  • 30
    • 33746208871 scopus 로고    scopus 로고
    • A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
    • Denic V, Quan EM, Weissman JS. 2006. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126: 349-59.
    • (2006) Cell , vol.126 , pp. 349-359
    • Denic, V.1    Quan, E.M.2    Weissman, J.S.3
  • 31
    • 0034597161 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p
    • Gardner RG, Swarbrick GM, Bays NW, Cronin SR, et al. 2000. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p. J Cell Biol 151: 69-82.
    • (2000) J Cell Biol , vol.151 , pp. 69-82
    • Gardner, R.G.1    Swarbrick, G.M.2    Bays, N.W.3    Cronin, S.R.4
  • 33
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays NW, Gardner RG, Seelig LP, Joazeiro CA, et al. 2001. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol 3: 24-9.
    • (2001) Nat Cell Biol , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4
  • 34
    • 0031885043 scopus 로고    scopus 로고
    • Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins
    • Bordallo J, Plemper RK, Finger A, Wolf DH. 1998. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol Biol Cell 9: 209-22.
    • (1998) Mol Biol Cell , vol.9 , pp. 209-222
    • Bordallo, J.1    Plemper, R.K.2    Finger, A.3    Wolf, D.H.4
  • 35
    • 0035815754 scopus 로고    scopus 로고
    • Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation
    • Deak PM, Wolf DH. 2001. Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J Biol Chem 276: 10663-9.
    • (2001) J Biol Chem , vol.276 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 36
    • 0025967290 scopus 로고
    • UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme
    • McGrath JP, Jentsch S, Varshavsky A. 1991. UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme. EMBO J 10: 227-36.
    • (1991) EMBO J , vol.10 , pp. 227-236
    • McGrath, J.P.1    Jentsch, S.2    Varshavsky, A.3
  • 37
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander R, Jarosch E, Urban J, Volkwein C, et al. 2000. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2: 379-84.
    • (2000) Nat Cell Biol , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4
  • 38
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch C, Gauss R, Horn SC, Neuber O, et al. 2009. The ubiquitylation machinery of the endoplasmic reticulum. Nature 458: 453-60.
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4
  • 39
    • 36248988054 scopus 로고    scopus 로고
    • Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation
    • Kostova Z, Tsai YC, Weissman AM. 2007. Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation. Semin Cell Dev Biol 18: 770-9.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 770-779
    • Kostova, Z.1    Tsai, Y.C.2    Weissman, A.M.3
  • 40
    • 0032540384 scopus 로고    scopus 로고
    • Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome
    • de Virgilio M, Weninger H, Ivessa NE. 1998. Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J Biol Chem 273: 9734-43.
    • (1998) J Biol Chem , vol.273 , pp. 9734-9743
    • de Virgilio, M.1    Weninger, H.2    Ivessa, N.E.3
  • 41
    • 0035167960 scopus 로고    scopus 로고
    • Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol
    • Shamu CE, Flierman D, Ploegh HL, Rapoport TA, et al. 2001. Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol Biol Cell 12: 2546-55.
    • (2001) Mol Biol Cell , vol.12 , pp. 2546-2555
    • Shamu, C.E.1    Flierman, D.2    Ploegh, H.L.3    Rapoport, T.A.4
  • 42
    • 0037076507 scopus 로고    scopus 로고
    • Cdc48-Ufd1-Npl4: stuck in the middle with Ub
    • Bays NW, Hampton RY. 2002. Cdc48-Ufd1-Npl4: stuck in the middle with Ub. Curr Biol 12: R366-71.
    • (2002) Curr Biol , vol.12
    • Bays, N.W.1    Hampton, R.Y.2
  • 43
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E, Taxis C, Volkwein C, Bordallo J, et al. 2002. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4: 134-9.
    • (2002) Nat Cell Biol , vol.4 , pp. 134-139
    • Jarosch, E.1    Taxis, C.2    Volkwein, C.3    Bordallo, J.4
  • 44
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA. 2001. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414: 652-6.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 45
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y, Meyer HH, Rapoport TA. 2003. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162: 71-84.
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 46
    • 0034501375 scopus 로고    scopus 로고
    • A major conformational change in p97 AAA ATPase upon ATP binding
    • Rouiller I, Butel VM, Latterich M, Milligan RA, et al. 2000. A major conformational change in p97 AAA ATPase upon ATP binding. Mol Cell 6: 1485-90.
    • (2000) Mol Cell , vol.6 , pp. 1485-1490
    • Rouiller, I.1    Butel, V.M.2    Latterich, M.3    Milligan, R.A.4
  • 48
    • 35948947822 scopus 로고    scopus 로고
    • AAA+ATPases: achieving diversity of function with conserved machinery
    • White SR, Lauring B. 2007. AAA+ATPases: achieving diversity of function with conserved machinery. Traffic 8: 1657-67.
    • (2007) Traffic , vol.8 , pp. 1657-1667
    • White, S.R.1    Lauring, B.2
  • 49
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer HH, Shorter JG, Seemann J, Pappin D, et al. 2000. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J 19: 2181-92.
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4
  • 50
    • 27144535945 scopus 로고    scopus 로고
    • Ubx2 links the Cdc48 complex to ER-associated protein degradation
    • Neuber O, Jarosch E, Volkwein C, Walter J, et al. 2005. Ubx2 links the Cdc48 complex to ER-associated protein degradation. Nat Cell Biol 7: 993-8.
    • (2005) Nat Cell Biol , vol.7 , pp. 993-998
    • Neuber, O.1    Jarosch, E.2    Volkwein, C.3    Walter, J.4
  • 51
    • 27144539523 scopus 로고    scopus 로고
    • Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation
    • Schuberth C, Buchberger A. 2005. Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. Nat Cell Biol 7: 999-1006.
    • (2005) Nat Cell Biol , vol.7 , pp. 999-1006
    • Schuberth, C.1    Buchberger, A.2
  • 52
    • 0037349250 scopus 로고    scopus 로고
    • Pex8p: an intraperoxisomal organizer of the peroxisomal import machinery
    • Agne B, Meindl NM, Niederhoff K, Einwachter H, et al. 2003. Pex8p: an intraperoxisomal organizer of the peroxisomal import machinery. Mol Cell 11: 635-46.
    • (2003) Mol Cell , vol.11 , pp. 635-646
    • Agne, B.1    Meindl, N.M.2    Niederhoff, K.3    Einwachter, H.4
  • 53
    • 0029010680 scopus 로고
    • Import of stably folded proteins into peroxisomes
    • Walton PA, Hill PE, Subramani S. 1995. Import of stably folded proteins into peroxisomes. Mol Biol Cell 6: 675-83.
    • (1995) Mol Biol Cell , vol.6 , pp. 675-683
    • Walton, P.A.1    Hill, P.E.2    Subramani, S.3
  • 54
    • 0028110118 scopus 로고
    • Saccharomyces cerevisiae peroxisomal thiolase is imported as a dimer
    • Glover JR, Andrews DW, Rachubinski RA. 1994. Saccharomyces cerevisiae peroxisomal thiolase is imported as a dimer. Proc Natl Acad Sci USA 91: 10541-5.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10541-10545
    • Glover, J.R.1    Andrews, D.W.2    Rachubinski, R.A.3
  • 55
    • 0028033934 scopus 로고
    • An oligomeric protein is imported into peroxisomes in vivo
    • McNew JA, Goodman JM. 1994. An oligomeric protein is imported into peroxisomes in vivo. J Cell Biol 127: 1245-57.
    • (1994) J Cell Biol , vol.127 , pp. 1245-1257
    • McNew, J.A.1    Goodman, J.M.2
  • 56
    • 0029912063 scopus 로고    scopus 로고
    • Analysis of the carboxyl-terminal peroxisomal targeting signal 1 in a homologous context in Saccharomyces cerevisiae
    • Elgersma Y, Vos A, van den Berg M, van Roermund CW, et al. 1996. Analysis of the carboxyl-terminal peroxisomal targeting signal 1 in a homologous context in Saccharomyces cerevisiae J Biol Chem 271: 26375-82.
    • (1996) J Biol Chem , vol.271 , pp. 26375-26382
    • Elgersma, Y.1    Vos, A.2    van den Berg, M.3    van Roermund, C.W.4
  • 57
    • 0033664345 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5
    • Gatto GJ, Jr, Geisbrecht BV, Gould SJ, Berg JM. 2000. Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5. Nat Struct Biol 7: 1091-5.
    • (2000) Nat Struct Biol , vol.7 , pp. 1091-1095
    • Gatto Jr., G.J.1    Geisbrecht, B.V.2    Gould, S.J.3    Berg, J.M.4
  • 58
    • 0024521811 scopus 로고
    • A conserved tripeptide sorts proteins to peroxisomes
    • Gould SJ, Keller GA, Hosken N, Wilkinson J, et al. 1989. A conserved tripeptide sorts proteins to peroxisomes. J Cell Biol 108: 1657-64.
    • (1989) J Cell Biol , vol.108 , pp. 1657-1664
    • Gould, S.J.1    Keller, G.A.2    Hosken, N.3    Wilkinson, J.4
  • 59
    • 0032509362 scopus 로고    scopus 로고
    • The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it
    • Lametschwandtner G, Brocard C, Fransen M, Van Veldhoven P, et al. 1998. The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it. J Biol Chem 273: 33635-43.
    • (1998) J Biol Chem , vol.273 , pp. 33635-33643
    • Lametschwandtner, G.1    Brocard, C.2    Fransen, M.3    Van Veldhoven, P.4
  • 60
    • 0025941962 scopus 로고
    • A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase
    • Swinkels BW, Gould SJ, Bodnar AG, Rachubinski RA, et al. 1991. A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase. EMBO J 10: 3255-62.
    • (1991) EMBO J , vol.10 , pp. 3255-3262
    • Swinkels, B.W.1    Gould, S.J.2    Bodnar, A.G.3    Rachubinski, R.A.4
  • 61
    • 27744523622 scopus 로고    scopus 로고
    • Peroxisomal matrix protein import: the transient pore model
    • Erdmann R, Schliebs W. 2005. Peroxisomal matrix protein import: the transient pore model. Nat Rev Mol Cell Biol 6: 738-42.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 738-742
    • Erdmann, R.1    Schliebs, W.2
  • 62
    • 77649267086 scopus 로고    scopus 로고
    • The peroxisomal importomer constitutes a large and highly dynamic pore
    • Meinecke M, Cizmowski C, Schliebs W, Kruger V, et al. 2010. The peroxisomal importomer constitutes a large and highly dynamic pore. Nat Cell Biol 12: 273-7.
    • (2010) Nat Cell Biol , vol.12 , pp. 273-277
    • Meinecke, M.1    Cizmowski, C.2    Schliebs, W.3    Kruger, V.4
  • 63
    • 0037414755 scopus 로고    scopus 로고
    • Characterization of the peroxisomal cycling receptor, Pex5p, using a cell-free in vitro import system
    • Gouveia AM, Guimaraes CP, Oliveira ME, Reguenga C, et al. 2003. Characterization of the peroxisomal cycling receptor, Pex5p, using a cell-free in vitro import system. J Biol Chem 278: 226-32.
    • (2003) J Biol Chem , vol.278 , pp. 226-232
    • Gouveia, A.M.1    Guimaraes, C.P.2    Oliveira, M.E.3    Reguenga, C.4
  • 64
    • 0034693260 scopus 로고    scopus 로고
    • Characterization of peroxisomal Pex5p from rat liver. Pex5p in the Pex5p-Pex14p membrane complex is a transmembrane protein
    • Gouveia AM, Reguenga C, Oliveira ME, Sa-Miranda C, et al. 2000. Characterization of peroxisomal Pex5p from rat liver. Pex5p in the Pex5p-Pex14p membrane complex is a transmembrane protein. J Biol Chem 275: 32444-51.
    • (2000) J Biol Chem , vol.275 , pp. 32444-32451
    • Gouveia, A.M.1    Reguenga, C.2    Oliveira, M.E.3    Sa-Miranda, C.4
  • 65
    • 0242353302 scopus 로고    scopus 로고
    • Physical interactions of the peroxisomal targeting signal 1 receptor pex5p, studied by fluorescence correlation spectroscopy
    • Wang D, Visser NV, Veenhuis M, van der Klei IJ. 2003. Physical interactions of the peroxisomal targeting signal 1 receptor pex5p, studied by fluorescence correlation spectroscopy. J Biol Chem 278: 43340-5.
    • (2003) J Biol Chem , vol.278 , pp. 43340-43345
    • Wang, D.1    Visser, N.V.2    Veenhuis, M.3    van der Klei, I.J.4
  • 66
    • 35748954927 scopus 로고    scopus 로고
    • Ubiquitination of mammalian Pex5p, the peroxisomal import receptor
    • Carvalho AF, Pinto MP, Grou CP, Alencastre IS, et al. 2007. Ubiquitination of mammalian Pex5p, the peroxisomal import receptor. J Biol Chem 282: 31267-72.
    • (2007) J Biol Chem , vol.282 , pp. 31267-31272
    • Carvalho, A.F.1    Pinto, M.P.2    Grou, C.P.3    Alencastre, I.S.4
  • 67
    • 34547957271 scopus 로고    scopus 로고
    • A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p
    • Williams C, van den Berg M, Sprenger RR, Distel B. 2007. A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p. J Biol Chem 282: 22534-43.
    • (2007) J Biol Chem , vol.282 , pp. 22534-22543
    • Williams, C.1    van den Berg, M.2    Sprenger, R.R.3    Distel, B.4
  • 68
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly H, Rape M, Braun S, Rumpf S, et al. 2005. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120: 73-84.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4
  • 69
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M, Hoppe T, Schlenker S, Ulrich HD, et al. 1999. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96: 635-44.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4
  • 70
    • 34247487864 scopus 로고    scopus 로고
    • Ubiquitination of the peroxisomal import receptor Pex5p is required for its recycling
    • Platta HW, El Magraoui F, Schlee D, Grunau S, et al. 2007. Ubiquitination of the peroxisomal import receptor Pex5p is required for its recycling. J Cell Biol 177: 197-204.
    • (2007) J Cell Biol , vol.177 , pp. 197-204
    • Platta, H.W.1    El Magraoui, F.2    Schlee, D.3    Grunau, S.4
  • 71
    • 12544259938 scopus 로고    scopus 로고
    • Ubiquitination of the peroxisomal targeting signal type 1 receptor, Pex5p, suggests the presence of a quality control mechanism during peroxisomal matrix protein import
    • Kiel JA, Emmrich K, Meyer HE, Kunau WH. 2005. Ubiquitination of the peroxisomal targeting signal type 1 receptor, Pex5p, suggests the presence of a quality control mechanism during peroxisomal matrix protein import. J Biol Chem 280: 1921-30.
    • (2005) J Biol Chem , vol.280 , pp. 1921-1930
    • Kiel, J.A.1    Emmrich, K.2    Meyer, H.E.3    Kunau, W.H.4
  • 72
    • 70350447348 scopus 로고    scopus 로고
    • Pex2 and Pex12 function as protein-ubiquitin ligases in peroxisomal protein import
    • Platta HW, El Magraoui F, Baumer BE, Schlee D, et al. 2009. Pex2 and Pex12 function as protein-ubiquitin ligases in peroxisomal protein import. Mol Cell Biol 29: 5505-16.
    • (2009) Mol Cell Biol , vol.29 , pp. 5505-5516
    • Platta, H.W.1    El Magraoui, F.2    Baumer, B.E.3    Schlee, D.4
  • 73
    • 49449096720 scopus 로고    scopus 로고
    • Pex10p functions as an E3 ligase for the Ubc4p-dependent ubiquitination of Pex5p
    • Williams C, van den Berg M, Geers E, Distel B. 2008. Pex10p functions as an E3 ligase for the Ubc4p-dependent ubiquitination of Pex5p. Biochem Biophys Res Commun 374: 620-4.
    • (2008) Biochem Biophys Res Commun , vol.374 , pp. 620-624
    • Williams, C.1    van den Berg, M.2    Geers, E.3    Distel, B.4
  • 74
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM. 2001. Mechanisms underlying ubiquitination. Annu Rev Biochem 70: 503-33.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 75
    • 28544451220 scopus 로고    scopus 로고
    • Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export
    • Miyata N, Fujiki Y. 2005. Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export. Mol Cell Biol 25: 10822-32.
    • (2005) Mol Cell Biol , vol.25 , pp. 10822-10832
    • Miyata, N.1    Fujiki, Y.2
  • 76
    • 23144446970 scopus 로고    scopus 로고
    • Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol
    • Platta HW, Grunau S, Rosenkranz K, Girzalsky W, et al. 2005. Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol. Nat Cell Biol 7: 817-22.
    • (2005) Nat Cell Biol , vol.7 , pp. 817-822
    • Platta, H.W.1    Grunau, S.2    Rosenkranz, K.3    Girzalsky, W.4
  • 77
    • 0031448780 scopus 로고    scopus 로고
    • Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S. cerevisiae, causes proliferation of the endoplasmic reticulum membrane
    • Elgersma Y, Kwast L, van den Berg M, Snyder WB, et al. 1997. Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S. cerevisiae, causes proliferation of the endoplasmic reticulum membrane. EMBO J 16: 7326-41.
    • (1997) EMBO J , vol.16 , pp. 7326-7341
    • Elgersma, Y.1    Kwast, L.2    van den Berg, M.3    Snyder, W.B.4
  • 78
    • 0038394714 scopus 로고    scopus 로고
    • The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes
    • Matsumoto N, Tamura S, Fujiki Y. 2003. The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes. Nat Cell Biol 5: 454-60.
    • (2003) Nat Cell Biol , vol.5 , pp. 454-460
    • Matsumoto, N.1    Tamura, S.2    Fujiki, Y.3
  • 80
    • 78649629196 scopus 로고    scopus 로고
    • More membranes, more proteins: complex protein import mechanisms into secondary plastids
    • Agrawal S, Striepen B. 2010. More membranes, more proteins: complex protein import mechanisms into secondary plastids. Protist 161: 672-87.
    • (2010) Protist , vol.161 , pp. 672-687
    • Agrawal, S.1    Striepen, B.2
  • 81
    • 0032838597 scopus 로고    scopus 로고
    • Principles of protein and lipid targeting in secondary symbiogenesis: euglenoid, dinoflagellate, and sporozoan plastid origins and the eukaryote family tree
    • Cavalier-Smith T. 1999. Principles of protein and lipid targeting in secondary symbiogenesis: euglenoid, dinoflagellate, and sporozoan plastid origins and the eukaryote family tree. J Eukaryot Microbiol 46: 347-66.
    • (1999) J Eukaryot Microbiol , vol.46 , pp. 347-366
    • Cavalier-Smith, T.1
  • 82
    • 77949906386 scopus 로고    scopus 로고
    • Filling the gap, evolutionarily conserved Omp85 in plastids of chromalveolates
    • Bullmann L, Haarmann R, Mirus O, Bredemeier R, et al. 2010. Filling the gap, evolutionarily conserved Omp85 in plastids of chromalveolates. J Biol Chem 285: 6848-56.
    • (2010) J Biol Chem , vol.285 , pp. 6848-6856
    • Bullmann, L.1    Haarmann, R.2    Mirus, O.3    Bredemeier, R.4
  • 84
    • 34547925627 scopus 로고    scopus 로고
    • Transport of nuclear-encoded proteins into secondarily evolved plastids
    • Hempel F, Bozarth A, Sommer MS, Zauner S, et al. 2007. Transport of nuclear-encoded proteins into secondarily evolved plastids. Biol Chem 388: 899-906.
    • (2007) Biol Chem , vol.388 , pp. 899-906
    • Hempel, F.1    Bozarth, A.2    Sommer, M.S.3    Zauner, S.4
  • 85
    • 77951567634 scopus 로고    scopus 로고
    • New mechanistic insights into pre-protein transport across the second outermost plastid membrane of diatoms
    • Hempel F, Felsner G, Maier UG. 2010. New mechanistic insights into pre-protein transport across the second outermost plastid membrane of diatoms. Mol Microbiol 76: 793-801.
    • (2010) Mol Microbiol , vol.76 , pp. 793-801
    • Hempel, F.1    Felsner, G.2    Maier, U.G.3
  • 86
    • 70350564161 scopus 로고    scopus 로고
    • Sec61p is part of the endoplasmic reticulum-associated degradation machinery
    • Schafer A, Wolf DH. 2009. Sec61p is part of the endoplasmic reticulum-associated degradation machinery. EMBO J 28: 2874-84.
    • (2009) EMBO J , vol.28 , pp. 2874-2884
    • Schafer, A.1    Wolf, D.H.2
  • 87
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz EJ, Tortorella D, Bogyo M, Yu J, et al. 1996. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384: 432-8.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4
  • 88
    • 57749114774 scopus 로고    scopus 로고
    • Sec61p is required for ERAD-L: genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY
    • Willer M, Forte GM, Stirling CJ. 2008. Sec61p is required for ERAD-L: genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY. J Biol Chem 283: 33883-8.
    • (2008) J Biol Chem , vol.283 , pp. 33883-33888
    • Willer, M.1    Forte, G.M.2    Stirling, C.J.3
  • 89
    • 77955576219 scopus 로고    scopus 로고
    • Lack of phylogenetic support for a supposed actinobacterial origin of peroxisomes
    • Gabaldón T, Capella-Gutierrez S. 2010. Lack of phylogenetic support for a supposed actinobacterial origin of peroxisomes. Gene 465: 61-5.
    • (2010) Gene , vol.465 , pp. 61-65
    • Gabaldón, T.1    Capella-Gutierrez, S.2
  • 90
    • 22144465170 scopus 로고    scopus 로고
    • Contribution of the endoplasmic reticulum to peroxisome formation
    • Hoepfner D, Schildknegt D, Braakman I, Philippsen P, et al. 2005. Contribution of the endoplasmic reticulum to peroxisome formation. Cell 122: 85-95.
    • (2005) Cell , vol.122 , pp. 85-95
    • Hoepfner, D.1    Schildknegt, D.2    Braakman, I.3    Philippsen, P.4
  • 91
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soding J. 2005. Protein homology detection by HMM-HMM comparison. Bioinformatics 21: 951-60.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 92
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K, Misawa K, Kuma K, Miyata T. 2002. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res 30: 3059-66.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 93
    • 67650757433 scopus 로고    scopus 로고
    • trimAl: a tool for automated alignment trimming in large-scale phylogenetic analyses
    • Capella-Gutierrez S, Silla-Martinez JM, Gabaldón T. 2009. trimAl: a tool for automated alignment trimming in large-scale phylogenetic analyses. Bioinformatics 25: 1972-3.
    • (2009) Bioinformatics , vol.25 , pp. 1972-1973
    • Capella-Gutierrez, S.1    Silla-Martinez, J.M.2    Gabaldón, T.3
  • 94
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon S, Gascuel O. 2003. A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst Biol 52: 696-704.
    • (2003) Syst Biol , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.