메뉴 건너뛰기




Volumn 123, Issue 19, 2010, Pages 3389-3400

PEX11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance

Author keywords

DRP1 DLP1; hFis1; Microtubules; Organelle fission; Peroxisome proliferation; PEX11

Indexed keywords

ELONGATION FACTOR; GUANOSINE TRIPHOSPHATASE; PROTEIN DRP1; PROTEIN FIS1; PROTEIN PEX11; TUBULIN; UNCLASSIFIED DRUG;

EID: 77955986557     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.064907     Document Type: Article
Times cited : (129)

References (66)
  • 1
    • 0032545023 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p
    • Abe, I. and Fujiki, Y. (1998). cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p. Biochem. Biophys. Res. Commun. 252, 529-533.
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 529-533
    • Abe, I.1    Fujiki, Y.2
  • 2
    • 0032563281 scopus 로고    scopus 로고
    • Clofibrate-inducible, 28-kDa peroxisomal integral membrane protein is encoded by PEX11
    • DOI 10.1016/S0014-5793(98)00815-1, PII S0014579398008151
    • Abe, I., Okumoto, K., Tamura, S. and Fujiki, Y. (1998). Clofibrate-inducible, 28-kDa peroxisomal integral membrane protein is encoded by PEX11. FEBS Lett. 431, 468-472. (Pubitemid 28352413)
    • (1998) FEBS Letters , vol.431 , Issue.3 , pp. 468-472
    • Abe, I.1    Okumoto, K.2    Tamura, S.3    Fujiki, Y.4
  • 3
    • 0033591357 scopus 로고    scopus 로고
    • Protein targeting to endoplasmic reticulum by dilysine signals involves direct retention in addition to retrieval
    • Andersson, H., Kappeler, F. and Hauri, H. P. (1999). Protein targeting to endoplasmic reticulum by dilysine signals involves direct retention in addition to retrieval. J. Biol. Chem. 274, 15080-15084.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15080-15084
    • Andersson, H.1    Kappeler, F.2    Hauri, H.P.3
  • 4
    • 33845300838 scopus 로고    scopus 로고
    • Peroxisome targeting signal 1, Is it really a simple tripeptide? Biochim
    • Brocard, C. and Hartig, A. (2006). Peroxisome targeting signal 1, Is it really a simple tripeptide? Biochim. Biophys. Acta 1763, 1565-1573.
    • (2006) Biophys. Acta , vol.1763 , pp. 1565-1573
    • Brocard, C.1    Hartig, A.2
  • 5
    • 17444394885 scopus 로고    scopus 로고
    • Requirement for microtubules and dynein motors in the earliest stages of peroxisome biogenesis
    • Brocard, C. B., Boucher, K. K., Jedeszko, C., Kim, P. K. and Walton, P. A. (2005). Requirement for microtubules and dynein motors in the earliest stages of peroxisome biogenesis. Traffic 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
  • 6
    • 0032404053 scopus 로고    scopus 로고
    • New COP1-binding motifs involved in ER retrieval
    • Cosson, P., Lefkir, Y., Demolliere, C. and Letourneur, F. (1998). New COP1-binding motifs involved in ER retrieval. EMBO J. 17, 6863-6870. (Pubitemid 28550280)
    • (1998) EMBO Journal , vol.17 , Issue.23 , pp. 6863-6870
    • Cosson, P.1    Lefkir, Y.2    Demolliere, C.3    Letourneur, F.4
  • 7
    • 0142245636 scopus 로고    scopus 로고
    • A gateway cloning vector set for highthroughput functional analysis of genes in planta
    • Curtis, M. D. and Grossniklaus, U. (2003). A gateway cloning vector set for highthroughput functional analysis of genes in planta. Plant Physiol. 133, 462-469.
    • (2003) Plant Physiol. , vol.133 , pp. 462-469
    • Curtis, M.D.1    Grossniklaus, U.2
  • 10
    • 33644872218 scopus 로고    scopus 로고
    • Gateway-compatible vectors for plant functional genomics and proteomics
    • DOI 10.1111/j.1365-313X.2005.02617.x
    • Earley, K. W., Haag, J. R., Pontes, O., Opper, K., Juehne, T., Song, K. and Pikaard, C. S. (2006). Gateway-compatible vectors for plant functional genomics and proteomics. Plant J. 45, 616-629. (Pubitemid 43373712)
    • (2006) Plant Journal , vol.45 , Issue.4 , pp. 616-629
    • Earley, K.W.1    Haag, J.R.2    Pontes, O.3    Opper, K.4    Juehne, T.5    Song, K.6    Pikaard, C.S.7
  • 11
    • 0028859252 scopus 로고
    • Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p
    • Erdmann, R. and Blobel, G. (1995). Giant peroxisomes in oleic acid-induced Saccharomyces cerevisiae lacking the peroxisomal membrane protein Pmp27p. J. Cell Biol. 128, 509-523.
    • (1995) J. Cell Biol. , vol.128 , pp. 509-523
    • Erdmann, R.1    Blobel, G.2
  • 12
    • 0029795490 scopus 로고    scopus 로고
    • Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor
    • Erdmann, R. and Blobel, G. (1996). Identification of Pex13p a peroxisomal membrane receptor for the PTS1 recognition factor. J. Cell Biol. 135, 111-121.
    • (1996) J. Cell Biol. , vol.135 , pp. 111-121
    • Erdmann, R.1    Blobel, G.2
  • 13
    • 33646093006 scopus 로고    scopus 로고
    • The peroxisomal membrane protein Inp2p is the peroxisome-specific receptor for the myosin V motor Myo2p of Saccharomyces cerevisiae
    • Fagarasanu, A., Fagarasanu, M., Eitzen, G. A., Aitchison, J. D. and Rachubinski, R. A. (2006). The peroxisomal membrane protein Inp2p is the peroxisome-specific receptor for the myosin V motor Myo2p of Saccharomyces cerevisiae. Dev. Cell 10, 587-600.
    • (2006) Dev. Cell , vol.10 , pp. 587-600
    • Fagarasanu, A.1    Fagarasanu, M.2    Eitzen, G.A.3    Aitchison, J.D.4    Rachubinski, R.A.5
  • 15
    • 0035159364 scopus 로고    scopus 로고
    • The GTPase effector domain sequence of the Dnm1p GTPase regulates self-assembly and controls a rate-limiting step in mitochondrial fission
    • Fukushima, N. H., Brisch, E., Keegan, B. R., Bleazard, W. and Shaw, J. M. (2001). The GTPase effector domain sequence of the Dnm1p GTPase regulates self-assembly and controls a rate-limiting step in mitochondrial fission. Mol. Biol. Cell 12, 2756-2766.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2756-2766
    • Fukushima, N.H.1    Brisch, E.2    Keegan, B.R.3    Bleazard, W.4    Shaw, J.M.5
  • 17
    • 70349446542 scopus 로고    scopus 로고
    • Protein transport across the peroxisomal membrane
    • Girzalsky, W., Platta, H. W. and Erdmann, R. (2009). Protein transport across the peroxisomal membrane. Biol. Chem. 390, 745-751.
    • (2009) Biol. Chem. , vol.390 , pp. 745-751
    • Girzalsky, W.1    Platta, H.W.2    Erdmann, R.3
  • 18
    • 55149097659 scopus 로고    scopus 로고
    • The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes
    • Hara-Kuge, S. and Fujiki, Y. (2008). The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes. Exp. Cell Res. 314, 3531-3541.
    • (2008) Exp. Cell Res. , vol.314 , pp. 3531-3541
    • Hara-Kuge, S.1    Fujiki, Y.2
  • 19
    • 0035842904 scopus 로고    scopus 로고
    • A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae
    • Hoepfner, D., van den Berg, M., Philippsen, P., Tabak, H. F. and Hettema, E. H. (2001). A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J. Cell Biol. 155, 979-990.
    • (2001) J. Cell Biol. , vol.155 , pp. 979-990
    • Hoepfner, D.1    Van Den Berg, M.2    Philippsen, P.3    Tabak, H.F.4    Hettema, E.H.5
  • 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., Mullen, R. T., Schumann, U. and Lippincott-Schwartz, J. (2006). The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER. J. Cell Biol. 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
  • 22
    • 0030917085 scopus 로고    scopus 로고
    • Protein transport from the cytoplasm into the vacuole
    • Klionsky, D. J. (1997). Protein transport from the cytoplasm into the vacuole. J. Membr. Biol. 157, 105-115.
    • (1997) J. Membr. Biol. , vol.157 , pp. 105-115
    • Klionsky, D.J.1
  • 23
    • 34247107180 scopus 로고    scopus 로고
    • Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis
    • Kobayashi, S., Tanaka, A. and Fujiki, Y. (2007). Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis. Exp. Cell Res. 313, 1675-1686.
    • (2007) Exp. Cell Res. , vol.313 , pp. 1675-1686
    • Kobayashi, S.1    Tanaka, A.2    Fujiki, Y.3
  • 24
    • 4444236087 scopus 로고    scopus 로고
    • Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1
    • DOI 10.1242/jcs.01268
    • Koch, A., Schneider, G., Luers, G. H. and Schrader, M. (2004). Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1. J. Cell Sci. 117, 3995-4006. (Pubitemid 39207335)
    • (2004) Journal of Cell Science , vol.117 , Issue.17 , pp. 3995-4006
    • Koch, A.1    Schneider, G.2    Luers, G.H.3    Schrader, M.4
  • 25
    • 27144557499 scopus 로고    scopus 로고
    • A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells
    • Koch, A., Yoon, Y., Bonekamp, N. A., McNiven, M. A. and Schrader, M. (2005). A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell 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
  • 26
    • 60349105123 scopus 로고    scopus 로고
    • Hansenula polymorpha pex11 cells are affected in peroxisome retention
    • Krikken, A. M., Veenhuis, M. and van der Klei, I. J. (2009). Hansenula polymorpha pex11 cells are affected in peroxisome retention. FEBS J. 276, 1429-1439.
    • (2009) FEBS J. , vol.276 , pp. 1429-1439
    • Krikken, A.M.1    Veenhuis, M.2    Van Der Klei, I.J.3
  • 28
    • 0026344773 scopus 로고
    • A DNA transformation-competent Arabidopsis genomic library in Agrobacterium
    • Lazo, G. R., Stein, P. A. and Ludwig, R. A. (1991). A DNA transformation-competent Arabidopsis genomic library in Agrobacterium. Biotechnology 9, 963-967.
    • (1991) Biotechnology , vol.9 , pp. 963-967
    • Lazo, G.R.1    Stein, P.A.2    Ludwig, R.A.3
  • 29
    • 0037128209 scopus 로고    scopus 로고
    • PEX11 promotes peroxisome division independently of peroxisome metabolism
    • Li, X. and Gould, S. J. (2002). PEX11 promotes peroxisome division independently of peroxisome metabolism. J. Cell Biol. 156, 643-651.
    • (2002) J. Cell Biol. , vol.156 , pp. 643-651
    • Li, X.1    Gould, S.J.2
  • 30
    • 0037930873 scopus 로고    scopus 로고
    • The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11
    • Li, X. and Gould, S. J. (2003). The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11. J. Biol. Chem. 278, 17012-17020.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17012-17020
    • Li, X.1    Gould, S.J.2
  • 31
    • 0036261777 scopus 로고    scopus 로고
    • PEX11 beta deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function
    • Li, X., Baumgart, E., Morrell, J. C., Jimenez-Sanchez, G., Valle, D. and Gould, S. J. (2002). PEX11 beta deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function. Mol. Cell. Biol. 22, 4358-4365.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4358-4365
    • Li, X.1    Baumgart, E.2    Morrell, J.C.3    Jimenez-Sanchez, G.4    Valle, D.5    Gould, S.J.6
  • 32
    • 33744519174 scopus 로고    scopus 로고
    • Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, duplication or aggregation
    • Lingard, M. J. and Trelease, R. N. (2006). Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, duplication or aggregation. J. Cell Sci. 119, 1961-1972.
    • (2006) J. Cell Sci. , vol.119 , pp. 1961-1972
    • Lingard, M.J.1    Trelease, R.N.2
  • 33
    • 57749113632 scopus 로고    scopus 로고
    • Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A cooperate in cell cycle-associated replication of peroxisomes
    • Lingard, M. J., Gidda, S. K., Bingham, S., Rothstein, S. J., Mullen, R. T. and Trelease, R. N. (2008). Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A cooperate in cell cycle-associated replication of peroxisomes. Plant Cell 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
  • 34
    • 0032125799 scopus 로고    scopus 로고
    • Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p
    • Lorenz, P., Maier, A. G., Baumgart, E., Erdmann, R. and Clayton, C. (1998). Elongation and clustering of glycosomes in Trypanosoma brucei overexpressing the glycosomal Pex11p. EMBO J. 17, 3542-3555.
    • (1998) EMBO J. , vol.17 , pp. 3542-3555
    • Lorenz, P.1    Maier, A.G.2    Baumgart, E.3    Erdmann, R.4    Clayton, C.5
  • 36
    • 0029792856 scopus 로고    scopus 로고
    • Redox-sensitive homodimerization of Pex11p: A proposed mechanism to regulate peroxisomal division
    • Marshall, P. A., Dyer, J. M., Quick, M. E. and Goodman, J. M. (1996). Redox-sensitive homodimerization of Pex11p: a proposed mechanism to regulate peroxisomal division. J. Cell Biol. 135, 123-137.
    • (1996) J. Cell Biol. , vol.135 , pp. 123-137
    • Marshall, P.A.1    Dyer, J.M.2    Quick, M.E.3    Goodman, J.M.4
  • 37
    • 0036006052 scopus 로고    scopus 로고
    • 1[w]
    • DOI 10.1104/pp.011018
    • Mathur, J., Mathur, N. and Hulskamp, M. (2002). Simultaneous visualization of peroxisomes and cytoskeletal elements reveals actin and not microtubule-based peroxisome motility in plants. Plant Physiol. 128, 1031-1045. (Pubitemid 34243839)
    • (2002) Plant Physiology , vol.128 , Issue.3 , pp. 1031-1045
    • Mathur, J.1    Mathur, N.2    Hulskamp, M.3
  • 38
    • 13044312086 scopus 로고    scopus 로고
    • Human PEX19: CDNA cloning by functional complementation, mutation analysis in a patient with Zellweger syndrome, and potential role in peroxisomal membrane assembly
    • Matsuzono, Y., Kinoshita, N., Tamura, S., Shimozawa, N., Hamasaki, M., Ghaedi, K., Wanders, R. J., Suzuki, Y., Kondo, N. and Fujiki, Y. (1999). Human PEX19: cDNA cloning by functional complementation, mutation analysis in a patient with Zellweger syndrome, and potential role in peroxisomal membrane assembly. Proc. Natl. Acad. Sci. USA 96, 2116-2121.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2116-2121
    • Matsuzono, Y.1    Kinoshita, N.2    Tamura, S.3    Shimozawa, N.4    Hamasaki, M.5    Ghaedi, K.6    Wanders, R.J.7    Suzuki, Y.8    Kondo, N.9    Fujiki, Y.10
  • 39
    • 34547595860 scopus 로고    scopus 로고
    • Yeast peroxisomes multiply by growth and division
    • Motley, A. M. and Hettema, E. H. (2007). Yeast peroxisomes multiply by growth and division. J. Cell Biol. 178, 399-410.
    • (2007) J. Cell Biol. , vol.178 , pp. 399-410
    • Motley, A.M.1    Hettema, E.H.2
  • 40
    • 46249130452 scopus 로고    scopus 로고
    • Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p
    • Motley, A. M., Ward, G. P. and Hettema, E. H. (2008). Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. J. Cell Sci. 121, 1633-1640.
    • (2008) J. Cell Sci. , vol.121 , pp. 1633-1640
    • Motley, A.M.1    Ward, G.P.2    Hettema, E.H.3
  • 41
    • 33645061266 scopus 로고    scopus 로고
    • Failure of microtubule-mediated peroxisome division and trafficking in disorders with reduced peroxisome abundance
    • Nguyen, T., Bjorkman, J., Paton, B. C. and Crane, D. I. (2006). Failure of microtubule-mediated peroxisome division and trafficking in disorders with reduced peroxisome abundance. J. Cell Sci. 119, 636-645.
    • (2006) J. Cell Sci. , vol.119 , pp. 636-645
    • Nguyen, T.1    Bjorkman, J.2    Paton, B.C.3    Crane, D.I.4
  • 42
    • 34249804174 scopus 로고    scopus 로고
    • The PEROXIN11 protein family controls peroxisome proliferation in Arabidopsis
    • Orth, T., Reumann, S., Zhang, X., Fan, J., Wenzel, D., Quan, S. and Hu, J. (2007). The PEROXIN11 protein family controls peroxisome proliferation in Arabidopsis. Plant Cell 19, 333-350.
    • (2007) Plant Cell , vol.19 , pp. 333-350
    • Orth, T.1    Reumann, S.2    Zhang, X.3    Fan, J.4    Wenzel, D.5    Quan, S.6    Hu, J.7
  • 45
    • 0141541655 scopus 로고    scopus 로고
    • Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis
    • Rottensteiner, H., Stein, K., Sonnenhol, E. and Erdmann, R. (2003). Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis. Mol. Biol. Cell 14, 4316-4328.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4316-4328
    • Rottensteiner, H.1    Stein, K.2    Sonnenhol, E.3    Erdmann, R.4
  • 46
    • 3042724871 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals
    • Rottensteiner, H., Kramer, A., Lorenzen, S., Stein, K., Landgraf, C., Volkmer-Engert, R. and Erdmann, R. (2004). Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals. Mol. Biol. Cell 15, 3406-3417.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3406-3417
    • Rottensteiner, H.1    Kramer, A.2    Lorenzen, S.3    Stein, K.4    Landgraf, C.5    Volkmer-Engert, R.6    Erdmann, R.7
  • 47
    • 0034611003 scopus 로고    scopus 로고
    • PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis
    • Sacksteder, K. A., Jones, J. M., South, S. T., Li, X., Liu, Y. and Gould, S. J. (2000). PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis. J. Cell Biol. 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
  • 52
    • 0027333416 scopus 로고
    • Protein import into peroxisomes and biogenesis of the organelle
    • Subramani, S. (1993). Protein import into peroxisomes and biogenesis of the organelle. Annu. Rev. Cell Biol. 9, 445-478.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 445-478
    • Subramani, S.1
  • 53
    • 34249689057 scopus 로고    scopus 로고
    • Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    • Taguchi, N., Ishihara, N., Jofuku, A., Oka, T. and Mihara, K. (2007). Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J. Biol. Chem. 282, 11521-11529.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4    Mihara, K.5
  • 54
    • 0141764783 scopus 로고    scopus 로고
    • Pex11-related proteins in peroxisome dynamics: A role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae
    • Tam, Y. Y., Torres-Guzman, J. C., Vizeacoumar, F. J., Smith, J. J., Marelli, M., Aitchison, J. D. and Rachubinski, R. A. (2003). Pex11-related proteins in peroxisome dynamics: a role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae. Mol. Biol. Cell 14, 4089-4102.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4089-4102
    • Tam, Y.Y.1    Torres-Guzman, J.C.2    Vizeacoumar, F.J.3    Smith, J.J.4    Marelli, M.5    Aitchison, J.D.6    Rachubinski, R.A.7
  • 55
    • 0037462961 scopus 로고    scopus 로고
    • cDNA cloning and characterization of the third isoform of human peroxin Pex11p
    • Tanaka, A., Okumoto, K. and Fujiki, Y. (2003). cDNA cloning and characterization of the third isoform of human peroxin Pex11p. Biochem. Biophys. Res. Commun. 300, 819-823.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 819-823
    • Tanaka, A.1    Okumoto, K.2    Fujiki, Y.3
  • 57
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady, G. E. and Simon, I. (2001). The HMMTOP transmembrane topology prediction server. Bioinformatics 17, 849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 58
    • 0041816190 scopus 로고    scopus 로고
    • Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes
    • Voncken, F., van Hellemond, J. J., Pfisterer, I., Maier, A., Hillmer, S. and Clayton, C. (2003). Depletion of GIM5 causes cellular fragility, a decreased glycosome number, and reduced levels of ether-linked phospholipids in trypanosomes. J. Biol. Chem. 278, 35299-35310.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35299-35310
    • Voncken, F.1    Van Hellemond, J.J.2    Pfisterer, I.3    Maier, A.4    Hillmer, S.5    Clayton, C.6
  • 59
    • 14244267510 scopus 로고    scopus 로고
    • Peroxisomal disorders I: Biochemistry and genetics of peroxisome biogenesis disorders
    • Wanders, R. J. and Waterham, H. R. (2005). Peroxisomal disorders I: biochemistry and genetics of peroxisome biogenesis disorders. Clin. Genet. 67, 107-133.
    • (2005) Clin. Genet. , vol.67 , pp. 107-133
    • Wanders, R.J.1    Waterham, H.R.2
  • 60
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders, R. J. and Waterham, H. R. (2006). Biochemistry of mammalian peroxisomes revisited. Annu. Rev. Biochem. 75, 295-332.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 295-332
    • Wanders, R.J.1    Waterham, H.R.2
  • 61
    • 36348930592 scopus 로고    scopus 로고
    • Direct binding of the dynamin-like GTPase, Dnm1, to mitochondrial dynamics protein Fis1 is negatively regulated by the Fis1 N-terminal arm
    • Wells, R. C., Picton, L. K., Williams, S. C., Tan, F. J. and Hill, R. B. (2007). Direct binding of the dynamin-like GTPase, Dnm1, to mitochondrial dynamics protein Fis1 is negatively regulated by the Fis1 N-terminal arm. J. Biol. Chem. 282, 33769-33775.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33769-33775
    • Wells, R.C.1    Picton, L.K.2    Williams, S.C.3    Tan, F.J.4    Hill, R.B.5
  • 62
    • 0031030969 scopus 로고    scopus 로고
    • Visualization of the peroxisomal compartment in living mammalian cells: Dynamic behavior and association with microtubules
    • DOI 10.1083/jcb.136.1.71
    • Wiemer, E. A., Wenzel, T., Deerinck, T. J., Ellisman, M. H. and Subramani, S. (1997). Visualization of the peroxisomal compartment in living mammalian cells: dynamic behavior and association with microtubules. J. Cell Biol. 136, 71-80. (Pubitemid 27044805)
    • (1997) Journal of Cell Biology , vol.136 , Issue.1 , pp. 71-80
    • Wiemer, E.A.C.1    Wenzel, T.2    Deerinck, T.J.3    Ellisman, M.H.4    Subramani, S.5
  • 63
    • 37249046472 scopus 로고    scopus 로고
    • MPB2C, a microtubule-associated protein, regulates non-cell-autonomy of the homeodomain protein KNOTTED1
    • Winter, N., Kollwig, G., Zhang, S. and Kragler, F. (2007). MPB2C, a microtubule-associated protein, regulates non-cell-autonomy of the homeodomain protein KNOTTED1. Plant Cell 19, 3001-3018.
    • (2007) Plant Cell , vol.19 , pp. 3001-3018
    • Winter, N.1    Kollwig, G.2    Zhang, S.3    Kragler, F.4
  • 64
    • 0023788653 scopus 로고
    • Increased amounts of HMG-CoA reductase induce "karmellae": A proliferation of stacked membrane pairs surrounding the yeast nucleus
    • Wright, R., Basson, M., D'Ari, L. and Rine, J. (1988). Increased amounts of HMG-CoA reductase induce "karmellae": a proliferation of stacked membrane pairs surrounding the yeast nucleus. J. Cell Biol. 107, 101-114.
    • (1988) J. Cell Biol. , vol.107 , pp. 101-114
    • Wright, R.1    Basson, M.2    D'Ari, L.3    Rine, J.4
  • 65
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Yoon, Y., Krueger, E. W., Oswald, B. J. and McNiven, M. A. (2003). The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol. Cell. Biol. 23, 5409-5420.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5409-5420
    • Yoon, Y.1    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 66
    • 58149120882 scopus 로고    scopus 로고
    • Two small protein families, DYNAMIN-RELATED PROTEIN3 and FISSION1, are required for peroxisome fission in Arabidopsis
    • Zhang, X. and Hu, J. (2009). Two small protein families, DYNAMIN-RELATED PROTEIN3 and FISSION1, are required for peroxisome fission in Arabidopsis. Plant J. 57, 146-159.
    • (2009) Plant J. , vol.57 , pp. 146-159
    • Zhang, X.1    Hu, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.