메뉴 건너뛰기




Volumn 215, Issue 4, 2016, Pages 515-529

A family of membrane-shaping proteins at ER subdomains regulates pre-peroxisomal vesicle biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN PEX30P; PROTEIN PEX31P; PROTEOLIPOSOME; UNCLASSIFIED DRUG; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 85004044980     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201602064     Document Type: Article
Times cited : (70)

References (49)
  • 1
    • 84975865504 scopus 로고    scopus 로고
    • De novo peroxisome biogenesis: Evolving concepts and conundrums
    • Agrawal, G., and S. Subramani. 2016. De novo peroxisome biogenesis: Evolving concepts and conundrums. Biochim. Biophys. Acta. 1863:892-901. http://dx.doi.org/10.1016/j.bbamcr.2015.09.014.
    • (2016) Biochim. Biophys. Acta , vol.1863 , pp. 892-901
    • Agrawal, G.1    Subramani, S.2
  • 2
    • 79959370908 scopus 로고    scopus 로고
    • Cell-free sorting of peroxisomal membrane proteins from the endoplasmic reticulum
    • Agrawal, G., S. Joshi, and S. Subramani. 2011. Cell-free sorting of peroxisomal membrane proteins from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 108:9113-9118. http://dx.doi.org/10.1073/pnas.1018749108.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 9113-9118
    • Agrawal, G.1    Joshi, S.2    Subramani, S.3
  • 3
    • 84959453936 scopus 로고    scopus 로고
    • Distinct requirements for intra-ER sorting and budding of peroxisomal membrane proteins from the ER
    • Agrawal, G., S.N. Fassas, Z.J. Xia, and S. Subramani. 2016. Distinct requirements for intra-ER sorting and budding of peroxisomal membrane proteins from the ER. J. Cell Biol. 212:335-348. http://dx.doi.org/10.1083/jcb.201506141.
    • (2016) J. Cell Biol , vol.212 , pp. 335-348
    • Agrawal, G.1    Fassas, S.N.2    Xia, Z.J.3    Subramani, S.4
  • 5
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G.R. 1959. Phosphorus assay in column chromatography. J. Biol. Chem. 234:466-468.
    • (1959) J. Biol. Chem , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 6
    • 0037044768 scopus 로고    scopus 로고
    • Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha
    • Bellu, A.R., F.A. Salomons, J.A. Kiel, M. Veenhuis, and I.J. Van Der Klei. 2002. Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha. J. Biol. Chem. 277:42875-42880. http://dx.doi.org/10.1074/jbc.M205437200.
    • (2002) J. Biol. Chem , vol.277 , pp. 42875-42880
    • Bellu, A.R.1    Salomons, F.A.2    Kiel, J.A.3    Veenhuis, M.4    Van Der Klei, I.J.5
  • 7
    • 33745386112 scopus 로고    scopus 로고
    • Yeast nuclear envelope subdomains with distinct abilities to resist membrane expansion
    • Campbell, J.L., A. Lorenz, K.L. Witkin, T. Hays, J. Loidl, and O. Cohen-Fix. 2006. Yeast nuclear envelope subdomains with distinct abilities to resist membrane expansion. Mol. Biol. Cell. 17:1768-1778. http://dx.doi.org/10.1091/mbc.E05-09-0839.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1768-1778
    • Campbell, J.L.1    Lorenz, A.2    Witkin, K.L.3    Hays, T.4    Loidl, J.5    Cohen-Fix, O.6
  • 8
    • 84863195175 scopus 로고    scopus 로고
    • ER network formation requires a balance of the dynamin-like GTPase Sey1p and the Lunapark family member Lnp1p
    • Chen, S., P. Novick, and S. Ferro-Novick. 2012. ER network formation requires a balance of the dynamin-like GTPase Sey1p and the Lunapark family member Lnp1p. Nat. Cell Biol. 14:707-716. http://dx.doi.org/10.1038/ncb2523.
    • (2012) Nat. Cell Biol , vol.14 , pp. 707-716
    • Chen, S.1    Novick, P.2    Ferro-Novick, S.3
  • 9
    • 84920996700 scopus 로고    scopus 로고
    • Lunapark stabilizes nascent three-way junctions in the endoplasmic reticulum
    • Chen, S., T. Desai, J.A. McNew, P. Gerard, P.J. Novick, and S. Ferro-Novick. 2015. Lunapark stabilizes nascent three-way junctions in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 112:418-423. http://dx.doi.org/10.1073/pnas.1423026112.
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 418-423
    • Chen, S.1    Desai, T.2    McNew, J.A.3    Gerard, P.4    Novick, P.J.5    Ferro-Novick, S.6
  • 10
    • 84971299729 scopus 로고    scopus 로고
    • A conserved family of proteins facilitates nascent lipid droplet budding from the ER
    • Choudhary, V., N. Ojha, A. Golden, and W.A. Prinz. 2015. A conserved family of proteins facilitates nascent lipid droplet budding from the ER. J. Cell Biol. 211:261-271. http://dx.doi.org/10.1083/jcb.201505067.
    • (2015) J. Cell Biol , vol.211 , pp. 261-271
    • Choudhary, V.1    Ojha, N.2    Golden, A.3    Prinz, W.A.4
  • 11
    • 84884369584 scopus 로고    scopus 로고
    • A combined approach of quantitative interaction proteomics and livecell imaging reveals a regulatory role for endoplasmic reticulum (ER) reticulon homology proteins in peroxisome biogenesis
    • David, C., J. Koch, S. Oeljeklaus, A. Laernsack, S. Melchior, S. Wiese, A. Schummer, R. Erdmann, B. Warscheid, and C. Brocard. 2013. A combined approach of quantitative interaction proteomics and livecell imaging reveals a regulatory role for endoplasmic reticulum (ER) reticulon homology proteins in peroxisome biogenesis. Mol. Cell. Proteomics. 12:2408-2425. http://dx.doi.org/10.1074/mcp.M112.017830.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 2408-2425
    • David, C.1    Koch, J.2    Oeljeklaus, S.3    Laernsack, A.4    Melchior, S.5    Wiese, S.6    Schummer, A.7    Erdmann, R.8    Warscheid, B.9    Brocard, C.10
  • 12
    • 64749091534 scopus 로고    scopus 로고
    • ER membranebending proteins are necessary for de novo nuclear pore formation
    • Dawson, T.R., M.D. Lazarus, M.W. Hetzer, and S.R. Wente. 2009. ER membranebending proteins are necessary for de novo nuclear pore formation. J. Cell Biol. 184:659-675. http://dx.doi.org/10.1083/jcb.200806174.
    • (2009) J. Cell Biol , vol.184 , pp. 659-675
    • Dawson, T.R.1    Lazarus, M.D.2    Hetzer, M.W.3    Wente, S.R.4
  • 13
    • 84877149297 scopus 로고    scopus 로고
    • The role of the endoplasmic reticulum in peroxisome biogenesis
    • Dimitrov, L., S.K. Lam, and R. Schekman. 2013. The role of the endoplasmic reticulum in peroxisome biogenesis. Cold Spring Harb. Perspect. Biol. 5:a013243. http://dx.doi.org/10.1101/cshperspect.a013243.
    • (2013) Cold Spring Harb. Perspect. Biol , vol.5
    • Dimitrov, L.1    Lam, S.K.2    Schekman, R.3
  • 14
    • 84873358822 scopus 로고    scopus 로고
    • Rab10 GTPase regulates ER dynamics and morphology
    • English, A.R., and G.K. Voeltz. 2013. Rab10 GTPase regulates ER dynamics and morphology. Nat. Cell Biol. 15:169-178. http://dx.doi.org/10.1038./ncb2647.
    • (2013) Nat. Cell Biol , vol.15 , pp. 169-178
    • English, A.R.1    Voeltz, G.K.2
  • 15
    • 84880617526 scopus 로고    scopus 로고
    • Untangling the web: mechanisms underlying ER network formation
    • Goyal, U., and C. Blackstone. 2013. Untangling the web: mechanisms underlying ER network formation. Biochim. Biophys. Acta. 1833:2492-2498. http://dx.doi.org/10.1016/j.bbamcr.2013.04.009.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2492-2498
    • Goyal, U.1    Blackstone, C.2
  • 16
    • 33645070532 scopus 로고    scopus 로고
    • Reassembly of peroxisomes in Hansenula polymorpha pex3 cells on reintroduction of Pex3p involves the nuclear envelope
    • Haan, G.J., R.J. Baerends, A.M. Krikken, M. Otzen, M. Veenhuis, and I.J. van der Klei. 2006. Reassembly of peroxisomes in Hansenula polymorpha pex3 cells on reintroduction of Pex3p involves the nuclear envelope. FEMS Yeast Res. 6:186-194. http://dx.doi.org/10.1111/j.1567-1364.2006.00037.x
    • (2006) FEMS Yeast Res , vol.6 , pp. 186-194
    • Haan, G.J.1    Baerends, R.J.2    Krikken, A.M.3    Otzen, M.4    Veenhuis, M.5    van der Klei, I.J.6
  • 17
    • 22144465170 scopus 로고    scopus 로고
    • Contribution of the endoplasmic reticulum to peroxisome formation
    • Hoepfner, D., D. Schildknegt, I. Braakman, P. Philippsen, and H.F. Tabak. 2005. Contribution of the endoplasmic reticulum to peroxisome formation. Cell. 122:85-95. http://dx.doi.org/10.1016/j.cell.2005.04.025.
    • (2005) Cell , vol.122 , pp. 85-95
    • Hoepfner, D.1    Schildknegt, D.2    Braakman, I.3    Philippsen, P.4    Tabak, H.F.5
  • 18
  • 19
    • 68049096310 scopus 로고    scopus 로고
    • A class of dynamin-like GTPases involved in the generation of the tubular ER network
    • Hu, J., Y. Shibata, P.P. Zhu, C. Voss, N. Rismanchi, W.A. Prinz, T.A. Rapoport, and C. Blackstone. 2009. A class of dynamin-like GTPases involved in the generation of the tubular ER network. Cell. 138:549-561. http://dx.doi.org/10.1016/j.cell.2009.05.025.
    • (2009) Cell , vol.138 , pp. 549-561
    • Hu, J.1    Shibata, Y.2    Zhu, P.P.3    Voss, C.4    Rismanchi, N.5    Prinz, W.A.6    Rapoport, T.A.7    Blackstone, C.8
  • 21
    • 33646791462 scopus 로고    scopus 로고
    • The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER
    • Kim, P.K., R.T. Mullen, U. Schumann, and J. Lippincott-Schwartz. 2006. The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER. J. Cell Biol. 173:521-532. http://dx.doi.org/10.1083/jcb.200601036.
    • (2006) J. Cell Biol , vol.173 , pp. 521-532
    • Kim, P.K.1    Mullen, R.T.2    Schumann, U.3    Lippincott-Schwartz, J.4
  • 23
    • 78650729949 scopus 로고    scopus 로고
    • A vesicle carrier that mediates peroxisome protein traffic from the endoplasmic reticulum
    • Lam, S.K., N. Yoda, and R. Schekman. 2010. A vesicle carrier that mediates peroxisome protein traffic from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 107:21523-21528. http://dx.doi.org/10.1073/pnas.1013397107.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 21523-21528
    • Lam, S.K.1    Yoda, N.2    Schekman, R.3
  • 24
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S., A. McKenzie III, D.J. Demarini, N.G. Shah, A. Wach, A. Brachat, P. Philippsen, and J.R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast. 14:953-961. http://dx.doi.org/10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 25
    • 84979609022 scopus 로고    scopus 로고
    • Peroxins Pex30 and Pex29. dynamically associate with reticulons to regulate peroxisome biogenesis from the endoplasmic reticulum
    • Mast, F.D., A. Jamakhandi, R.A. Saleem, D.J. Dilworth, R.S. Rogers, R.A. Rachubinski, and J.D. Aitchison. 2016. Peroxins Pex30 and Pex29. dynamically associate with reticulons to regulate peroxisome biogenesis from the endoplasmic reticulum. J. Biol. Chem. 291:15408-15427. http://dx.doi.org/10.1074/jbc.M116.728154.
    • (2016) J. Biol. Chem , vol.291 , pp. 15408-15427
    • Mast, F.D.1    Jamakhandi, A.2    Saleem, R.A.3    Dilworth, D.J.4    Rogers, R.S.5    Rachubinski, R.A.6    Aitchison, J.D.7
  • 26
    • 84934449988 scopus 로고    scopus 로고
    • Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus
    • Mochida, K., Y. Oikawa, Y. Kimura, H. Kirisako, H. Hirano, Y. Ohsumi, and H. Nakatogawa. 2015. Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus. Nature. 522:359-362. http://dx.doi.org/10.1038/nature14506.
    • (2015) Nature , vol.522 , pp. 359-362
    • Mochida, K.1    Oikawa, Y.2    Kimura, Y.3    Kirisako, H.4    Hirano, H.5    Ohsumi, Y.6    Nakatogawa, H.7
  • 27
    • 34547595860 scopus 로고    scopus 로고
    • Yeast peroxisomes multiply by growth and division
    • Motley, A.M., and E.H. Hettema. 2007. Yeast peroxisomes multiply by growth and division. J. Cell Biol. 178:399-410. http://dx.doi.org/10.1083/jcb.200702167.
    • (2007) J. Cell Biol , vol.178 , pp. 399-410
    • Motley, A.M.1    Hettema, E.H.2
  • 28
    • 79851510200 scopus 로고    scopus 로고
    • Protein import machineries of peroxisomes
    • Rucktäschel, R., W. Girzalsky, and R. Erdmann. 2011. Protein import machineries of peroxisomes. Biochim. Biophys. Acta. 1808:892-900. http://dx.doi.org/10.1016/j.bbamem.2010.07.020.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 892-900
    • Rucktäschel, R.1    Girzalsky, W.2    Erdmann, R.3
  • 29
    • 21244480972 scopus 로고    scopus 로고
    • The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
    • Santos-Rosa, H., J. Leung, N. Grimsey, S. Peak-Chew, and S. Siniossoglou. 2005. The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth. EMBO J. 24:1931-1941. http://dx.doi.org/10.1038/sj.emboj.7600672.
    • (2005) EMBO J , vol.24 , pp. 1931-1941
    • Santos-Rosa, H.1    Leung, J.2    Grimsey, N.3    Peak-Chew, S.4    Siniossoglou, S.5
  • 31
    • 49649084487 scopus 로고    scopus 로고
    • The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum
    • Shibata, Y., C. Voss, J.M. Rist, J. Hu, T.A. Rapoport, W.A. Prinz, and G.K. Voeltz. 2008. The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum. J. Biol. Chem. 283:18892-18904. http://dx.doi.org/10.1074/jbc.M800986200.
    • (2008) J. Biol. Chem , vol.283 , pp. 18892-18904
    • Shibata, Y.1    Voss, C.2    Rist, J.M.3    Hu, J.4    Rapoport, T.A.5    Prinz, W.A.6    Voeltz, G.K.7
  • 32
    • 79251471434 scopus 로고    scopus 로고
    • Mechanisms determining the morphology of the peripheral ER
    • Shibata, Y., T. Shemesh, W.A. Prinz, A.F. Palazzo, M.M. Kozlov, and T.A. Rapoport. 2010. Mechanisms determining the morphology of the peripheral ER. Cell. 143:774-788. http://dx.doi.org/10.1016/j.cell.2010.11.007.
    • (2010) Cell , vol.143 , pp. 774-788
    • Shibata, Y.1    Shemesh, T.2    Prinz, W.A.3    Palazzo, A.F.4    Kozlov, M.M.5    Rapoport, T.A.6
  • 33
    • 77951710195 scopus 로고    scopus 로고
    • Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae
    • Shindiapina, P., and C. Barlowe. 2010. Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae. Mol. Biol. Cell. 21:1530-1545. http://dx.doi.org/10.1091/mbc.E09-07-0605.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1530-1545
    • Shindiapina, P.1    Barlowe, C.2
  • 34
    • 37249073837 scopus 로고    scopus 로고
    • Overexpression of a plant reticulon remodels the lumen of the cortical endoplasmic reticulum but does not perturb protein transport
    • Tolley, N., I.A. Sparkes, P.R. Hunter, C.P. Craddock, J. Nuttall, L.M. Roberts, C. Hawes, E. Pedrazzini, and L. Frigerio. 2008. Overexpression of a plant reticulon remodels the lumen of the cortical endoplasmic reticulum but does not perturb protein transport. Traffic. 9:94-102. http://dx.doi.org/10.1111/j.1600-0854.2007.00670.x
    • (2008) Traffic , vol.9 , pp. 94-102
    • Tolley, N.1    Sparkes, I.A.2    Hunter, P.R.3    Craddock, C.P.4    Nuttall, J.5    Roberts, L.M.6    Hawes, C.7    Pedrazzini, E.8    Frigerio, L.9
  • 36
    • 77953507085 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins insert into the endoplasmic reticulum
    • van der Zand, A., I. Braakman, and H.F. Tabak. 2010. Peroxisomal membrane proteins insert into the endoplasmic reticulum. Mol. Biol. Cell. 21:2057-2065. http://dx.doi.org/10.1091/mbc.E10-02-0082.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2057-2065
    • van der Zand, A.1    Braakman, I.2    Tabak, H.F.3
  • 37
    • 77956867734 scopus 로고    scopus 로고
    • Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism
    • Van Veldhoven, P.P. 2010. Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism. J. Lipid Res. 51:2863-2895. http://dx.doi.org/10.1194/jlr.R005959.
    • (2010) J. Lipid Res , vol.51 , pp. 2863-2895
    • Van Veldhoven, P.P.1
  • 38
    • 16344366871 scopus 로고    scopus 로고
    • Phosphorylation controls CLI MP-63-mediated anchoring of the endoplasmic reticulum to microtubules
    • Vedrenne, C., D.R. Klopfenstein, and H.P. Hauri. 2005. Phosphorylation controls CLI MP-63-mediated anchoring of the endoplasmic reticulum to microtubules. Mol. Biol. Cell. 16:1928-1937. http://dx.doi.org/10.1091/mbc.E04-07-0554.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1928-1937
    • Vedrenne, C.1    Klopfenstein, D.R.2    Hauri, H.P.3
  • 39
    • 0742288046 scopus 로고    scopus 로고
    • Pex30p, Pex31p, and Pex32p form a family of peroxisomal integral membrane proteins regulating peroxisome size and number in Saccharomyces cerevisiae
    • Vizeacoumar, F.J., J.C. Torres-Guzman, D. Bouard, J.D. Aitchison, and R.A. Rachubinski. 2004. Pex30p, Pex31p, and Pex32p form a family of peroxisomal integral membrane proteins regulating peroxisome size and number in Saccharomyces cerevisiae. Mol. Biol. Cell. 15:665-677. http://dx.doi.org/10.1091/mbc.E03-09-0681.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 665-677
    • Vizeacoumar, F.J.1    Torres-Guzman, J.C.2    Bouard, D.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 40
    • 33744949079 scopus 로고    scopus 로고
    • Pex19p binds Pex30p and Pex32p at regions required for their peroxisomal localization but separate from their peroxisomal targeting signals
    • Vizeacoumar, F.J., W.N. Vreden, J.D. Aitchison, and R.A. Rachubinski. 2006. Pex19p binds Pex30p and Pex32p at regions required for their peroxisomal localization but separate from their peroxisomal targeting signals. J. Biol. Chem. 281:14805-14812. http://dx.doi.org/10.1074/jbc.M601808200.
    • (2006) J. Biol. Chem , vol.281 , pp. 14805-14812
    • Vizeacoumar, F.J.1    Vreden, W.N.2    Aitchison, J.D.3    Rachubinski, R.A.4
  • 41
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • Voeltz, G.K., W.A. Prinz, Y. Shibata, J.M. Rist, and T.A. Rapoport. 2006. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell. 124:573-586. http://dx.doi.org/10.1016/j.cell.2005.11.047.
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 42
    • 84872202122 scopus 로고    scopus 로고
    • ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae
    • Voss, C., S. Lahiri, B.P. Young, C.J. Loewen, and W.A. Prinz. 2012. ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae. J. Cell Sci. 125:4791-4799. http://dx.doi.org/10.1242/jcs.105635.
    • (2012) J. Cell Sci , vol.125 , pp. 4791-4799
    • Voss, C.1    Lahiri, S.2    Young, B.P.3    Loewen, C.J.4    Prinz, W.A.5
  • 43
    • 0032474825 scopus 로고    scopus 로고
    • Endoplasmic reticulum membrane tubules are distributed by microtubules in living cells using three distinct mechanisms
    • Waterman-Storer, C.M., and E.D. Salmon. 1998. Endoplasmic reticulum membrane tubules are distributed by microtubules in living cells using three distinct mechanisms. Curr. Biol. 8:798-806. http://dx.doi.org/10.1016/S0960-9822(98)70321-5.
    • (1998) Curr. Biol , vol.8 , pp. 798-806
    • Waterman-Storer, C.M.1    Salmon, E.D.2
  • 44
    • 79955488489 scopus 로고    scopus 로고
    • A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature
    • West, M., N. Zurek, A. Hoenger, and G.K. Voeltz. 2011. A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature. J. Cell Biol. 193:333-346. http://dx.doi.org/10.1083/jcb.201011039.
    • (2011) J. Cell Biol , vol.193 , pp. 333-346
    • West, M.1    Zurek, N.2    Hoenger, A.3    Voeltz, G.K.4
  • 45
    • 84930736511 scopus 로고    scopus 로고
    • Form follows function: The importance of endoplasmic reticulum shape
    • Westrate, L.M., J.E. Lee, W.A. Prinz, and G.K. Voeltz. 2015. Form follows function: The importance of endoplasmic reticulum shape. Annu. Rev. Biochem. 84:791-811. http://dx.doi.org/10.1146/annurev-biochem-072711-163501.
    • (2015) Annu. Rev. Biochem , vol.84 , pp. 791-811
    • Westrate, L.M.1    Lee, J.E.2    Prinz, W.A.3    Voeltz, G.K.4
  • 46
    • 84882641004 scopus 로고    scopus 로고
    • Pexophagy-linked degradation of the peroxisomal membrane protein Pex3p involves the ubiquitin-proteasome system
    • Williams, C., and I.J. van der Klei. 2013. Pexophagy-linked degradation of the peroxisomal membrane protein Pex3p involves the ubiquitin-proteasome system. Biochem. Biophys. Res. Commun. 438:395-401. http://dx.doi.org/10.1016/j.bbrc.2013.07.086.
    • (2013) Biochem. Biophys. Res. Commun , vol.438 , pp. 395-401
    • Williams, C.1    van der Klei, I.J.2
  • 48
    • 41649109400 scopus 로고    scopus 로고
    • Dysferlin domain-containing proteins, Pex30p and Pex31p, localized to two compartments, control the number and size of oleate-induced peroxisomes in Pichia pastoris
    • Yan, M., D.A. Rachubinski, S. Joshi, R.A. Rachubinski, and S. Subramani. 2008. Dysferlin domain-containing proteins, Pex30p and Pex31p, localized to two compartments, control the number and size of oleate-induced peroxisomes in Pichia pastoris. Mol. Biol. Cell. 19:885-898. http://dx.doi.org/10.1091/mbc.E07-10-1042.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 885-898
    • Yan, M.1    Rachubinski, D.A.2    Joshi, S.3    Rachubinski, R.A.4    Subramani, S.5
  • 49
    • 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., A. Furuno, T. Baba, Y. Fujiki, Y. Ogasawara, A. Yamamoto, M. Tagaya, and K. Tani. 2011. 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. 108:12746-12751. http://dx.doi.org/10.1073/pnas.1103283108
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.