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Volumn 16, Issue 8, 2015, Pages 832-852

Multiple Domains in PEX16 Mediate Its Trafficking and Recruitment of Peroxisomal Proteins to the ER

Author keywords

ER; Membrane targeting; Organelle biogenesis; Peroxisomal membrane protein; Peroxisomes; PEX16; PEX19; PEX3; Protein targeting signal; Protein trafficking

Indexed keywords

AMINO ACID; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN; PEROXISOMAL MEMBRANE PROTEIN 16; RED FLUORESCENT PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; SIGNAL PEPTIDE; SSE1 PROTEIN, ARABIDOPSIS;

EID: 84935683782     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12292     Document Type: Article
Times cited : (36)

References (63)
  • 1
    • 77953642000 scopus 로고    scopus 로고
    • Protein sorting receptors in the early secretory pathway
    • Dancourt J, Barlowe C. Protein sorting receptors in the early secretory pathway. Annu Rev Biochem 2010;79:777-802.
    • (2010) Annu Rev Biochem , vol.79 , pp. 777-802
    • Dancourt, J.1    Barlowe, C.2
  • 2
    • 84880583267 scopus 로고    scopus 로고
    • Vesicle-mediated export from the ER: COPII coat function and regulation
    • D'Arcangelo JG, Stahmer KR, Miller EA. Vesicle-mediated export from the ER: COPII coat function and regulation. Biochim Biophys Acta 2013;1833:2464-2472.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 2464-2472
    • D'Arcangelo, J.G.1    Stahmer, K.R.2    Miller, E.A.3
  • 4
    • 77953022036 scopus 로고    scopus 로고
    • Protein import into chloroplasts: the Tic complex and its regulation
    • Kovacs-Bogdan E, Soll J, Bolter B. Protein import into chloroplasts: the Tic complex and its regulation. Biochim Biophys Acta 2010;1803:740-747.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 740-747
    • Kovacs-Bogdan, E.1    Soll, J.2    Bolter, B.3
  • 5
    • 84871792997 scopus 로고    scopus 로고
    • Mitochondrial protein import: common principles and physiological networks
    • Dudek J, Rehling P, van der Laan M. Mitochondrial protein import: common principles and physiological networks. Biochim Biophys Acta 2013;1833:274-285.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 274-285
    • Dudek, J.1    Rehling, P.2    van der Laan, M.3
  • 6
    • 84896716062 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria-a regulatory hub in metabolism, stress, and disease
    • Harbauer AB, Zahedi RP, Sickmann A, Pfanner N, Meisinger C. The protein import machinery of mitochondria-a regulatory hub in metabolism, stress, and disease. Cell Metab 2014;19:357-372.
    • (2014) Cell Metab , vol.19 , pp. 357-372
    • Harbauer, A.B.1    Zahedi, R.P.2    Sickmann, A.3    Pfanner, N.4    Meisinger, C.5
  • 7
    • 33845304296 scopus 로고    scopus 로고
    • Peroxisomal disorders: the single peroxisomal enzyme deficiencies
    • Wanders RJ, Waterham HR. Peroxisomal disorders: the single peroxisomal enzyme deficiencies. Biochim Biophys Acta 2006;1763:1707-1720.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 1707-1720
    • Wanders, R.J.1    Waterham, H.R.2
  • 8
    • 77953715734 scopus 로고    scopus 로고
    • Be different--the diversity of peroxisomes in the animal kingdom
    • Islinger M, Cardoso MJ, Schrader M. Be different--the diversity of peroxisomes in the animal kingdom. Biochim Biophys Acta 2010;1803:881-897.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 881-897
    • Islinger, M.1    Cardoso, M.J.2    Schrader, M.3
  • 9
    • 79955505833 scopus 로고    scopus 로고
    • Peroxisome assembly: matrix and membrane protein biogenesis
    • Ma C, Agrawal G, Subramani S. Peroxisome assembly: matrix and membrane protein biogenesis. J Cell Biol 2011;193:7-16.
    • (2011) J Cell Biol , vol.193 , pp. 7-16
    • Ma, C.1    Agrawal, G.2    Subramani, S.3
  • 11
    • 84878954796 scopus 로고    scopus 로고
    • Peroxisome formation and maintenance are dependent on the endoplasmic reticulum
    • Tabak HF, Braakman I, van der Zand A. Peroxisome formation and maintenance are dependent on the endoplasmic reticulum. Annu Rev Biochem 2013;82:723-744.
    • (2013) Annu Rev Biochem , vol.82 , pp. 723-744
    • Tabak, H.F.1    Braakman, I.2    van der Zand, A.3
  • 14
    • 0022253765 scopus 로고
    • Post-translational import of fatty acyl-CoA oxidase and catalase into peroxisomes of rat liver in vitro
    • Fujiki Y, Lazarow PB. Post-translational import of fatty acyl-CoA oxidase and catalase into peroxisomes of rat liver in vitro. J Biol Chem 1985;260:5603-5609.
    • (1985) J Biol Chem , vol.260 , pp. 5603-5609
    • Fujiki, Y.1    Lazarow, P.B.2
  • 15
    • 77953507085 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins insert into the endoplasmic reticulum
    • van der Zand A, Braakman I, Tabak HF. Peroxisomal membrane proteins insert into the endoplasmic reticulum. Mol Biol Cell 2010;21:2057-2065.
    • (2010) Mol Biol Cell , vol.21 , pp. 2057-2065
    • van der Zand, A.1    Braakman, I.2    Tabak, H.F.3
  • 16
    • 84858293115 scopus 로고    scopus 로고
    • Peroxisome formation requires the endoplasmic reticulum channel protein Sec61
    • Thoms S, Harms I, Kalies KU, Gartner J. Peroxisome formation requires the endoplasmic reticulum channel protein Sec61. Traffic 2012;13:599-609.
    • (2012) Traffic , vol.13 , pp. 599-609
    • Thoms, S.1    Harms, I.2    Kalies, K.U.3    Gartner, J.4
  • 17
    • 84964902417 scopus 로고    scopus 로고
    • Intra-ER sorting of the peroxisomal membrane protein Pex3 relies on its luminal domain
    • Fakieh MH, Drake PJ, Lacey J, Munck JM, Motley AM, Hettema EH. Intra-ER sorting of the peroxisomal membrane protein Pex3 relies on its luminal domain. Biol Open 2013;2:829-837.
    • (2013) Biol Open , vol.2 , pp. 829-837
    • Fakieh, M.H.1    Drake, P.J.2    Lacey, J.3    Munck, J.M.4    Motley, A.M.5    Hettema, E.H.6
  • 20
    • 0034972812 scopus 로고    scopus 로고
    • Human pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences
    • Fransen M, Wylin T, Brees C, Mannaerts GP, Van Veldhoven PP. Human pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences. Mol Cell Biol 2001;21:4413-4424.
    • (2001) Mol Cell Biol , vol.21 , pp. 4413-4424
    • Fransen, M.1    Wylin, T.2    Brees, C.3    Mannaerts, G.P.4    Van Veldhoven, P.P.5
  • 21
    • 1642394134 scopus 로고    scopus 로고
    • PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins
    • Fang Y, Morrell JC, Jones JM, Gould SJ. PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins. J Cell Biol 2004;164:863-875.
    • (2004) J Cell Biol , vol.164 , pp. 863-875
    • Fang, Y.1    Morrell, J.C.2    Jones, J.M.3    Gould, S.J.4
  • 22
    • 0345861756 scopus 로고    scopus 로고
    • PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins
    • Jones JM, Morrell JC, Gould SJ. PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins. J Cell Biol 2004;164:57-67.
    • (2004) J Cell Biol , vol.164 , pp. 57-67
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 23
    • 33749392686 scopus 로고    scopus 로고
    • Functional domain mapping of peroxin Pex19p: interaction with Pex3p is essential for function and translocation
    • Matsuzono Y, Matsuzaki T, Fujiki Y. Functional domain mapping of peroxin Pex19p: interaction with Pex3p is essential for function and translocation. J Cell Sci 2006;119:3539-3550.
    • (2006) J Cell Sci , vol.119 , pp. 3539-3550
    • Matsuzono, Y.1    Matsuzaki, T.2    Fujiki, Y.3
  • 24
    • 32144448220 scopus 로고    scopus 로고
    • In vitro transport of membrane proteins to peroxisomes by shuttling receptor Pex19p
    • Matsuzono Y, Fujiki Y. In vitro transport of membrane proteins to peroxisomes by shuttling receptor Pex19p. J Biol Chem 2006;281:36-42.
    • (2006) J Biol Chem , vol.281 , pp. 36-42
    • Matsuzono, Y.1    Fujiki, Y.2
  • 25
    • 59449104113 scopus 로고    scopus 로고
    • The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway
    • Matsuzaki T, Fujiki Y. The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway. J Cell Biol 2008;183:1275-1286.
    • (2008) J Cell Biol , vol.183 , pp. 1275-1286
    • Matsuzaki, T.1    Fujiki, Y.2
  • 26
    • 84884552638 scopus 로고    scopus 로고
    • PEX16: a multifaceted regulator of peroxisome biogenesis
    • Kim PK, Mullen RT. PEX16: a multifaceted regulator of peroxisome biogenesis. Front Physiol 2013;4:241.
    • (2013) Front Physiol , vol.4 , pp. 241
    • Kim, P.K.1    Mullen, R.T.2
  • 27
    • 0037113975 scopus 로고    scopus 로고
    • The membrane biogenesis peroxin Pex16p. Topogenesis and functional roles in peroxisomal membrane assembly
    • Honsho M, Hiroshige T, Fujiki Y. The membrane biogenesis peroxin Pex16p. Topogenesis and functional roles in peroxisomal membrane assembly. J Biol Chem 2002;277:44513-44524.
    • (2002) J Biol Chem , vol.277 , pp. 44513-44524
    • Honsho, M.1    Hiroshige, T.2    Fujiki, Y.3
  • 28
    • 33646791462 scopus 로고    scopus 로고
    • The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER
    • Kim PK, Mullen RT, Schumann U, Lippincott-Schwartz J. The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER. J Cell Biol 2006;173:521-532.
    • (2006) J Cell Biol , vol.173 , pp. 521-532
    • Kim, P.K.1    Mullen, R.T.2    Schumann, U.3    Lippincott-Schwartz, J.4
  • 29
    • 79961245517 scopus 로고    scopus 로고
    • Sec16B is involved in the endoplasmic reticulum export of the peroxisomal membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells
    • Yonekawa S, Furuno A, Baba T, Fujiki Y, Ogasawara Y, Yamamoto A, Tagaya M, Tani K. Sec16B is involved in the endoplasmic reticulum export of the peroxisomal membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells. Proc Natl Acad Sci USA 2011;108:12746-12751.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 12746-12751
    • Yonekawa, S.1    Furuno, A.2    Baba, T.3    Fujiki, Y.4    Ogasawara, Y.5    Yamamoto, A.6    Tagaya, M.7    Tani, K.8
  • 30
    • 84906876094 scopus 로고    scopus 로고
    • PEX16 contributes to peroxisome maintenance by constantly trafficking PEX3 via the ER
    • Aranovich A, Hua R, Rutenberg AD, Kim PK. PEX16 contributes to peroxisome maintenance by constantly trafficking PEX3 via the ER. J Cell Sci 2014;127:3675-3686.
    • (2014) J Cell Sci , vol.127 , pp. 3675-3686
    • Aranovich, A.1    Hua, R.2    Rutenberg, A.D.3    Kim, P.K.4
  • 31
    • 34547466205 scopus 로고    scopus 로고
    • Arabidopsis peroxin 16 trafficks through the ER and an intermediate compartment to pre-existing peroxisomes via overlapping molecular targeting signals
    • Karnik SK, Trelease RN. Arabidopsis peroxin 16 trafficks through the ER and an intermediate compartment to pre-existing peroxisomes via overlapping molecular targeting signals. J Exp Bot 2007;58:1677-1693.
    • (2007) J Exp Bot , vol.58 , pp. 1677-1693
    • Karnik, S.K.1    Trelease, R.N.2
  • 32
    • 48249151759 scopus 로고    scopus 로고
    • The concept of translocational regulation
    • Hegde RS, Kang SW. The concept of translocational regulation. J Cell Biol 2008;182:225-232.
    • (2008) J Cell Biol , vol.182 , pp. 225-232
    • Hegde, R.S.1    Kang, S.W.2
  • 33
    • 0023782388 scopus 로고
    • Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence
    • Wessels HP, Spiess M. Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell 1988;55:61-70.
    • (1988) Cell , vol.55 , pp. 61-70
    • Wessels, H.P.1    Spiess, M.2
  • 34
    • 0034717704 scopus 로고    scopus 로고
    • Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis
    • South ST, Sacksteder KA, Li X, Liu Y, Gould SJ. Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis. J Cell Biol 2000;149:1345-1360.
    • (2000) J Cell Biol , vol.149 , pp. 1345-1360
    • South, S.T.1    Sacksteder, K.A.2    Li, X.3    Liu, Y.4    Gould, S.J.5
  • 35
    • 17444394885 scopus 로고    scopus 로고
    • Requirement for microtubules and dynein motors in the earliest stages of peroxisome biogenesis
    • Brocard CB, Boucher KK, Jedeszko C, Kim PK, Walton PA. Requirement for microtubules and dynein motors in the earliest stages of peroxisome biogenesis. Traffic 2005;6:386-395.
    • (2005) Traffic , vol.6 , pp. 386-395
    • Brocard, C.B.1    Boucher, K.K.2    Jedeszko, C.3    Kim, P.K.4    Walton, P.A.5
  • 36
    • 33845310297 scopus 로고    scopus 로고
    • Targeting signals in peroxisomal membrane proteins
    • Van Ael E, Fransen M. Targeting signals in peroxisomal membrane proteins. Biochim Biophys Acta 2006;1763:1629-1638.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 1629-1638
    • Van Ael, E.1    Fransen, M.2
  • 37
    • 84876230401 scopus 로고    scopus 로고
    • Peroxisome membrane proteins: multiple trafficking routes and multiple functions?
    • Theodoulou FL, Bernhardt K, Linka N, Baker A. Peroxisome membrane proteins: multiple trafficking routes and multiple functions? Biochem J 2013;451:345-352.
    • (2013) Biochem J , vol.451 , pp. 345-352
    • Theodoulou, F.L.1    Bernhardt, K.2    Linka, N.3    Baker, A.4
  • 38
    • 0006602702 scopus 로고
    • VAMP-1: a synaptic vesicle-associated integral membrane protein
    • Trimble WS, Cowan DM, Scheller RH. VAMP-1: a synaptic vesicle-associated integral membrane protein. Proc Natl Acad Sci USA 1988;85:4538-4542.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4538-4542
    • Trimble, W.S.1    Cowan, D.M.2    Scheller, R.H.3
  • 39
    • 0033601172 scopus 로고    scopus 로고
    • Identification of the endoplasmic reticulum targeting signal in vesicle-associated membrane proteins
    • Kim PK, Hollerbach C, Trimble WS, Leber B, Andrews DW. Identification of the endoplasmic reticulum targeting signal in vesicle-associated membrane proteins. J Biol Chem 1999;274:36876-36882.
    • (1999) J Biol Chem , vol.274 , pp. 36876-36882
    • Kim, P.K.1    Hollerbach, C.2    Trimble, W.S.3    Leber, B.4    Andrews, D.W.5
  • 40
    • 33847035916 scopus 로고    scopus 로고
    • Protein kinase D 3 is localized in vesicular structures and interacts with vesicle-associated membrane protein 2
    • Lu G, Chen J, Espinoza LA, Garfield S, Toshiyuki S, Akiko H, Huppler A, Wang QJ. Protein kinase D 3 is localized in vesicular structures and interacts with vesicle-associated membrane protein 2. Cell Signal 2007;19:867-879.
    • (2007) Cell Signal , vol.19 , pp. 867-879
    • Lu, G.1    Chen, J.2    Espinoza, L.A.3    Garfield, S.4    Toshiyuki, S.5    Akiko, H.6    Huppler, A.7    Wang, Q.J.8
  • 41
    • 33746072623 scopus 로고    scopus 로고
    • Targeting of the tail-anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-terminal PEX19-binding sites
    • Halbach A, Landgraf C, Lorenzen S, Rosenkranz K, Volkmer-Engert R, Erdmann R, Rottensteiner H. Targeting of the tail-anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-terminal PEX19-binding sites. J Cell Sci 2006;119:2508-2517.
    • (2006) J Cell Sci , vol.119 , pp. 2508-2517
    • Halbach, A.1    Landgraf, C.2    Lorenzen, S.3    Rosenkranz, K.4    Volkmer-Engert, R.5    Erdmann, R.6    Rottensteiner, H.7
  • 42
    • 84874959565 scopus 로고    scopus 로고
    • Tail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway
    • Yagita Y, Hiromasa T, Fujiki Y. Tail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway. J Cell Biol 2013;200:651-666.
    • (2013) J Cell Biol , vol.200 , pp. 651-666
    • Yagita, Y.1    Hiromasa, T.2    Fujiki, Y.3
  • 43
    • 0032231872 scopus 로고    scopus 로고
    • Identification of PEX10, the gene defective in complementation group 7 of the peroxisome-biogenesis disorders
    • Warren DS, Morrell JC, Moser HW, Valle D, Gould SJ. Identification of PEX10, the gene defective in complementation group 7 of the peroxisome-biogenesis disorders. Am J Hum Genet 1998;63:347-359.
    • (1998) Am J Hum Genet , vol.63 , pp. 347-359
    • Warren, D.S.1    Morrell, J.C.2    Moser, H.W.3    Valle, D.4    Gould, S.J.5
  • 44
    • 0032545023 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p
    • Abe I, Fujiki Y. cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p. Biochem Biophys Res Commun 1998;252:529-533.
    • (1998) Biochem Biophys Res Commun , vol.252 , pp. 529-533
    • Abe, I.1    Fujiki, Y.2
  • 45
    • 27144557499 scopus 로고    scopus 로고
    • A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells
    • Koch A, Yoon Y, Bonekamp NA, McNiven MA, Schrader M. A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells. Mol Biol Cell 2005;16:5077-5086.
    • (2005) Mol Biol Cell , vol.16 , pp. 5077-5086
    • Koch, A.1    Yoon, Y.2    Bonekamp, N.A.3    McNiven, M.A.4    Schrader, M.5
  • 46
    • 0033152496 scopus 로고    scopus 로고
    • Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein
    • Nemoto Y, De Camilli P. Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein. EMBO J 1999;18:2991-3006.
    • (1999) EMBO J , vol.18 , pp. 2991-3006
    • Nemoto, Y.1    De Camilli, P.2
  • 47
    • 0036000002 scopus 로고    scopus 로고
    • Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane
    • Horie C, Suzuki H, Sakaguchi M, Mihara K. Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane. Mol Biol Cell 2002;13:1615-1625.
    • (2002) Mol Biol Cell , vol.13 , pp. 1615-1625
    • Horie, C.1    Suzuki, H.2    Sakaguchi, M.3    Mihara, K.4
  • 48
    • 0034611003 scopus 로고    scopus 로고
    • PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis
    • Sacksteder KA, Jones JM, South ST, Li X, Liu Y, Gould SJ. PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis. J Cell Biol 2000;148:931-944.
    • (2000) J Cell Biol , vol.148 , pp. 931-944
    • Sacksteder, K.A.1    Jones, J.M.2    South, S.T.3    Li, X.4    Liu, Y.5    Gould, S.J.6
  • 49
    • 3042530250 scopus 로고    scopus 로고
    • The peroxisome deficient Arabidopsis mutant sse1 exhibits impaired fatty acid synthesis
    • Lin Y, Cluette-Brown JE, Goodman HM. The peroxisome deficient Arabidopsis mutant sse1 exhibits impaired fatty acid synthesis. Plant Physiol 2004;135:814-827.
    • (2004) Plant Physiol , vol.135 , pp. 814-827
    • Lin, Y.1    Cluette-Brown, J.E.2    Goodman, H.M.3
  • 50
    • 0034838201 scopus 로고    scopus 로고
    • Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin cotyledons
    • Fukao Y, Hayashi Y, Mano S, Hayashi M, Nishimura M. Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin cotyledons. Plant Cell Physiol 2001;42:835-841.
    • (2001) Plant Cell Physiol , vol.42 , pp. 835-841
    • Fukao, Y.1    Hayashi, Y.2    Mano, S.3    Hayashi, M.4    Nishimura, M.5
  • 51
    • 0346374719 scopus 로고    scopus 로고
    • Sorting pathway and molecular targeting signals for the Arabidopsis peroxin 3
    • Hunt JE, Trelease RN. Sorting pathway and molecular targeting signals for the Arabidopsis peroxin 3. Biochem Biophys Res Commun 2004;314:586-596.
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 586-596
    • Hunt, J.E.1    Trelease, R.N.2
  • 52
    • 34547595860 scopus 로고    scopus 로고
    • Yeast peroxisomes multiply by growth and division
    • Motley AM, Hettema EH. Yeast peroxisomes multiply by growth and division. J Cell Biol 2007;178:399-410.
    • (2007) J Cell Biol , vol.178 , pp. 399-410
    • Motley, A.M.1    Hettema, E.H.2
  • 53
    • 84859745968 scopus 로고    scopus 로고
    • Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes
    • van der Zand A, Gent J, Braakman I, Tabak HF. Biochemically distinct vesicles from the endoplasmic reticulum fuse to form peroxisomes. Cell 2012;149:397-409.
    • (2012) Cell , vol.149 , pp. 397-409
    • van der Zand, A.1    Gent, J.2    Braakman, I.3    Tabak, H.F.4
  • 54
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • Higy M, Junne T, Spiess M. Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 2004;43:12716-12722.
    • (2004) Biochemistry , vol.43 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 55
    • 0021722336 scopus 로고
    • Synthesis of a major integral membrane polypeptide of rat liver peroxisomes on free polysomes
    • Fujiki Y, Rachubinski RA, Lazarow PB. Synthesis of a major integral membrane polypeptide of rat liver peroxisomes on free polysomes. Proc Natl Acad Sci USA 1984;81:7127-7131.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7127-7131
    • Fujiki, Y.1    Rachubinski, R.A.2    Lazarow, P.B.3
  • 56
    • 0034627808 scopus 로고    scopus 로고
    • Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multistep peroxisome assembly pathway of Yarrowia lipolytica
    • Titorenko VI, Chan H, Rachubinski RA. Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multistep peroxisome assembly pathway of Yarrowia lipolytica. J Cell Biol 2000;148:29-44.
    • (2000) J Cell Biol , vol.148 , pp. 29-44
    • Titorenko, V.I.1    Chan, H.2    Rachubinski, R.A.3
  • 60
    • 70349136350 scopus 로고    scopus 로고
    • Subcellular localization and expression of multiple tomato gamma-aminobutyrate transaminases that utilize both pyruvate and glyoxylate
    • Clark SM, Di Leo R, Van Cauwenberghe OR, Mullen RT, Shelp BJ. Subcellular localization and expression of multiple tomato gamma-aminobutyrate transaminases that utilize both pyruvate and glyoxylate. J Exp Bot 2009;60:3255-3267.
    • (2009) J Exp Bot , vol.60 , pp. 3255-3267
    • Clark, S.M.1    Di Leo, R.2    Van Cauwenberghe, O.R.3    Mullen, R.T.4    Shelp, B.J.5
  • 61
    • 33749263895 scopus 로고    scopus 로고
    • Tung tree DGAT1 and DGAT2 have nonredundant functions in triacylglycerol biosynthesis and are localized to different subdomains of the endoplasmic reticulum
    • Shockey JM, Gidda SK, Chapital DC, Kuan JC, Dhanoa PK, Bland JM, Rothstein SJ, Mullen RT, Dyer JM. Tung tree DGAT1 and DGAT2 have nonredundant functions in triacylglycerol biosynthesis and are localized to different subdomains of the endoplasmic reticulum. Plant Cell 2006;18:2294-2313.
    • (2006) Plant Cell , vol.18 , pp. 2294-2313
    • Shockey, J.M.1    Gidda, S.K.2    Chapital, D.C.3    Kuan, J.C.4    Dhanoa, P.K.5    Bland, J.M.6    Rothstein, S.J.7    Mullen, R.T.8    Dyer, J.M.9
  • 62
    • 0023989774 scopus 로고
    • Purification and biosynthesis of cottonseed (Gossypium hirsutum L.) catalase
    • Kunce CM, Trelease RN, Turley RB. Purification and biosynthesis of cottonseed (Gossypium hirsutum L.) catalase. Biochem J 1988;251:147-155.
    • (1988) Biochem J , vol.251 , pp. 147-155
    • Kunce, C.M.1    Trelease, R.N.2    Turley, R.B.3
  • 63
    • 57749113632 scopus 로고    scopus 로고
    • Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A cooperate in cell cycle-associated replication of peroxisomes
    • Lingard MJ, Gidda SK, Bingham S, Rothstein SJ, Mullen RT, Trelease RN. Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A cooperate in cell cycle-associated replication of peroxisomes. Plant cell 2008;20:1567-1585.
    • (2008) Plant cell , vol.20 , pp. 1567-1585
    • Lingard, M.J.1    Gidda, S.K.2    Bingham, S.3    Rothstein, S.J.4    Mullen, R.T.5    Trelease, R.N.6


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