메뉴 건너뛰기




Volumn 20, Issue 1, 2015, Pages 36-49

Peroxin Pex14p is the key component for coordinated autophagic degradation of mammalian peroxisomes by direct binding to LC3-II

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA;

EID: 84930150889     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/gtc.12198     Document Type: Article
Times cited : (39)

References (54)
  • 3
    • 0037044768 scopus 로고    scopus 로고
    • Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha
    • Bellu, A.R., Salomons, F.A., Kiel, J.A.K.W., Veenhuis, M. & van der Klei, I.J. (2002) Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha. J. Biol. Chem. 277, 42875-42880.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42875-42880
    • Bellu, A.R.1    Salomons, F.A.2    Kiel, J.A.K.W.3    Veenhuis, M.4    van der Klei, I.J.5
  • 5
    • 84877579321 scopus 로고    scopus 로고
    • Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11
    • Farré, J.-C., Burkenroad, A., Burnett, S.F. & Subramani, S. (2013) Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11. EMBO Rep. 14, 441-449.
    • (2013) EMBO Rep. , vol.14 , pp. 441-449
    • Farré, J.-C.1    Burkenroad, A.2    Burnett, S.F.3    Subramani, S.4
  • 6
    • 42049094041 scopus 로고    scopus 로고
    • PpAtg30 tags peroxisomes for turnover by selective autophagy
    • Farré, J.-C., Manjithaya, R., Mathewson, R.D. & Subramani, S. (2008) PpAtg30 tags peroxisomes for turnover by selective autophagy. Dev. Cell 14, 365-376.
    • (2008) Dev. Cell , vol.14 , pp. 365-376
    • Farré, J.-C.1    Manjithaya, R.2    Mathewson, R.D.3    Subramani, S.4
  • 9
    • 55149097659 scopus 로고    scopus 로고
    • The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes
    • Hara-Kuge, S. & 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
  • 12
    • 33744519453 scopus 로고    scopus 로고
    • Functional domains and dynamic assembly of the peroxin Pex14p, the entry site of matrix proteins
    • Itoh, R. & Fujiki, Y. (2006) Functional domains and dynamic assembly of the peroxin Pex14p, the entry site of matrix proteins. J. Biol. Chem. 281, 10196-10205.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10196-10205
    • Itoh, R.1    Fujiki, Y.2
  • 16
    • 15444353327 scopus 로고    scopus 로고
    • Newly identified Chinese hamster ovary cell mutants are defective in biogenesis of peroxisomal membrane vesicles (peroxisomal ghosts), representing a novel complementation group in mammals
    • Kinoshita, N., Ghaedi, K., Shimozawa, N., Wanders, R.J.A., Matsuzono, Y., Imanaka, T., Okumoto, K., Suzuki, Y., Kondo, N. & Fujiki, Y. (1998) Newly identified Chinese hamster ovary cell mutants are defective in biogenesis of peroxisomal membrane vesicles (peroxisomal ghosts), representing a novel complementation group in mammals. J. Biol. Chem. 273, 24122-24130.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24122-24130
    • Kinoshita, N.1    Ghaedi, K.2    Shimozawa, N.3    Wanders, R.J.A.4    Matsuzono, Y.5    Imanaka, T.6    Okumoto, K.7    Suzuki, Y.8    Kondo, N.9    Fujiki, Y.10
  • 17
    • 0034676037 scopus 로고    scopus 로고
    • The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway
    • Kirisako, T., Ichimura, Y., Okada, H., Kabeya, Y., Mizushima, N., Yoshimori, T., Ohsumi, M., Takao, T., Noda, T. & Ohsumi, Y. (2000) The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway. J. Cell Biol. 151, 263-276.
    • (2000) J. Cell Biol. , vol.151 , pp. 263-276
    • Kirisako, T.1    Ichimura, Y.2    Okada, H.3    Kabeya, Y.4    Mizushima, N.5    Yoshimori, T.6    Ohsumi, M.7    Takao, T.8    Noda, T.9    Ohsumi, Y.10
  • 18
    • 0033280667 scopus 로고    scopus 로고
    • Vacuolar import of proteins and organelles from the cytoplasm
    • Klionsky, D.J. & Ohsumi, Y. (1999) Vacuolar import of proteins and organelles from the cytoplasm. Annu. Rev. Cell Dev. Biol. 15, 1-32.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 1-32
    • Klionsky, D.J.1    Ohsumi, Y.2
  • 19
    • 0031023643 scopus 로고    scopus 로고
    • The Hansenula polymorpha PEX14 gene encodes a novel peroxisomal membrane protein essential for peroxisome biogenesis
    • Komori, M., Rasmussen, S.W., Kiel, J.A., Baerends, R.J., Cregg, J.M., van der Klei, I.J. & Veenhuis, M. (1997) The Hansenula polymorpha PEX14 gene encodes a novel peroxisomal membrane protein essential for peroxisome biogenesis. EMBO J. 16, 44-53.
    • (1997) EMBO J. , vol.16 , pp. 44-53
    • Komori, M.1    Rasmussen, S.W.2    Kiel, J.A.3    Baerends, R.J.4    Cregg, J.M.5    van der Klei, I.J.6    Veenhuis, M.7
  • 20
    • 67650517556 scopus 로고    scopus 로고
    • NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets
    • Lamark, T., Kirkin, V., Dikic, I. & Johansen, T. (2009) NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets. Cell Cycle 8, 1986-1990.
    • (2009) Cell Cycle , vol.8 , pp. 1986-1990
    • Lamark, T.1    Kirkin, V.2    Dikic, I.3    Johansen, T.4
  • 21
    • 0242570685 scopus 로고    scopus 로고
    • Peroxisome homeostasis in Hansenula polymorpha
    • Leão, A.N. & Kiel, J.A.K.W. (2003) Peroxisome homeostasis in Hansenula polymorpha. FEMS Yeast Res. 4, 131-139.
    • (2003) FEMS Yeast Res. , vol.4 , pp. 131-139
    • Leão, A.N.1    Kiel, J.A.K.W.2
  • 22
    • 84862789618 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
    • Liu, L., Feng, D., Chen, G. et al. (2012) Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells. Nat. Cell Biol. 14, 177-185.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 177-185
    • Liu, L.1    Feng, D.2    Chen, G.3
  • 23
    • 34548077177 scopus 로고    scopus 로고
    • Autophagy and vacuole homeostasis: a case for self degradation?
    • Mijaljica, D., Prescott, M., Klionsky, D.J. & Devenish, R.J. (2007) Autophagy and vacuole homeostasis: a case for self degradation? Autophagy 3, 417-421.
    • (2007) Autophagy , vol.3 , pp. 417-421
    • Mijaljica, D.1    Prescott, M.2    Klionsky, D.J.3    Devenish, R.J.4
  • 24
    • 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, 10822-10832.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10822-10832
    • Miyata, N.1    Fujiki, Y.2
  • 25
    • 34250864795 scopus 로고    scopus 로고
    • Protein turnover via autophagy: implications for metabolism
    • Mizushima, N. & Klionsky, D.J. (2007) Protein turnover via autophagy: implications for metabolism. Annu. Rev. Nutr. 27, 19-40.
    • (2007) Annu. Rev. Nutr. , vol.27 , pp. 19-40
    • Mizushima, N.1    Klionsky, D.J.2
  • 26
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N., Levine, B., Cuervo, A.M. & Klionsky, D.J. (2008) Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 29
    • 84863843241 scopus 로고    scopus 로고
    • Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
    • Motley, A.M., Nuttall, J.M. & Hettema, E.H. (2012) Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae. EMBO J. 31, 2852-2868.
    • (2012) EMBO J. , vol.31 , pp. 2852-2868
    • Motley, A.M.1    Nuttall, J.M.2    Hettema, E.H.3
  • 30
    • 84870936161 scopus 로고    scopus 로고
    • Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101
    • Natsuyama, R., Okumoto, K. & Fujiki, Y. (2013) Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101. Biochem. J. 449, 195-207.
    • (2013) Biochem. J. , vol.449 , pp. 195-207
    • Natsuyama, R.1    Okumoto, K.2    Fujiki, Y.3
  • 32
    • 84884536709 scopus 로고    scopus 로고
    • Peroxisome degradation in mammals: mechanisms of action, recent advances, and perspectives
    • Nordgren, M., Wang, B., Apanasets, O. & Fransen, M. (2013) Peroxisome degradation in mammals: mechanisms of action, recent advances, and perspectives. Front. Physiol. 4, Article 145; doi:10.3389/fphys.2013.00145.
    • (2013) Front. Physiol. , vol.4
    • Nordgren, M.1    Wang, B.2    Apanasets, O.3    Fransen, M.4
  • 34
    • 52049091287 scopus 로고    scopus 로고
    • Physiological pH and acidic phospholipids contribute to substrate specificity in lipidation of Atg8
    • Oh-oka, K., Nakatogawa, H. & Ohsumi, Y. (2008) Physiological pH and acidic phospholipids contribute to substrate specificity in lipidation of Atg8. J. Biol. Chem. 283, 21847-21852.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21847-21852
    • Oh-oka, K.1    Nakatogawa, H.2    Ohsumi, Y.3
  • 35
    • 0031862579 scopus 로고    scopus 로고
    • PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of Pex12p
    • Okumoto, K., Shimozawa, N., Kawai, A., Tamura, S., Tsukamoto, T., Osumi, T., Moser, H., Wanders, R.J.A., Suzuki, Y., Kondo, N. & Fujiki, Y. (1998) PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of Pex12p. Mol. Cell. Biol. 18, 4324-4336.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4324-4336
    • Okumoto, K.1    Shimozawa, N.2    Kawai, A.3    Tamura, S.4    Tsukamoto, T.5    Osumi, T.6    Moser, H.7    Wanders, R.J.A.8    Suzuki, Y.9    Kondo, N.10    Fujiki, Y.11
  • 37
    • 0034647937 scopus 로고    scopus 로고
    • The mammalian peroxin Pex5pL, the longer isoform of the mobile peroxisome targeting signal (PTS) type 1 transporter, translocates Pex7p-PTS2 protein complex into peroxisomes via its initial docking site, Pex14p
    • Otera, H., Harano, T., Honsho, M., Ghaedi, K., Mukai, S., Tanaka, A., Kawai, A., Shimizu, N. & Fujiki, Y. (2000) The mammalian peroxin Pex5pL, the longer isoform of the mobile peroxisome targeting signal (PTS) type 1 transporter, translocates Pex7p-PTS2 protein complex into peroxisomes via its initial docking site, Pex14p. J. Biol. Chem. 275, 21703-21714.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21703-21714
    • Otera, H.1    Harano, T.2    Honsho, M.3    Ghaedi, K.4    Mukai, S.5    Tanaka, A.6    Kawai, A.7    Shimizu, N.8    Fujiki, Y.9
  • 39
    • 0036179374 scopus 로고    scopus 로고
    • Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import
    • Otera, H., Setoguchi, K., Hamasaki, M., Kumashiro, T., Shimizu, N. & Fujiki, Y. (2002) Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import. Mol. Cell. Biol. 22, 1639-1655.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1639-1655
    • Otera, H.1    Setoguchi, K.2    Hamasaki, M.3    Kumashiro, T.4    Shimizu, N.5    Fujiki, Y.6
  • 42
    • 0033617195 scopus 로고    scopus 로고
    • The peroxin Pex14p: cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis
    • Shimizu, N., Itoh, R., Hirono, Y., Otera, H., Ghaedi, K., Tateishi, K., Tamura, S., Okumoto, K., Harano, T., Mukai, S. & Fujiki, Y. (1999) The peroxin Pex14p: cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis. J. Biol. Chem. 274, 12593-12604.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12593-12604
    • Shimizu, N.1    Itoh, R.2    Hirono, Y.3    Otera, H.4    Ghaedi, K.5    Tateishi, K.6    Tamura, S.7    Okumoto, K.8    Harano, T.9    Mukai, S.10    Fujiki, Y.11
  • 43
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B. & Johnson, K.S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67, 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 44
    • 33645652024 scopus 로고    scopus 로고
    • Phosphatidylserine in addition to phosphatidylethanolamine is an in vitro target of the mammalian Atg8 modifiers, LC3, GABARAP, and GATE-16
    • Sou, Y.S., Tanida, I., Komatsu, M., Ueno, T. & Kominami, E. (2006) Phosphatidylserine in addition to phosphatidylethanolamine is an in vitro target of the mammalian Atg8 modifiers, LC3, GABARAP, and GATE-16. J. Biol. Chem. 281, 3017-3024.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3017-3024
    • Sou, Y.S.1    Tanida, I.2    Komatsu, M.3    Ueno, T.4    Kominami, E.5
  • 45
    • 58849148932 scopus 로고    scopus 로고
    • Crystal structure of the conserved N-terminal domain of the peroxisomal matrix-protein-import receptor, Pex14p
    • Su, J.R., Takeda, K., Tamura, S., Fujiki, Y. & Miki, K. (2009) Crystal structure of the conserved N-terminal domain of the peroxisomal matrix-protein-import receptor, Pex14p. Proc. Natl Acad. Sci. USA 106, 417-421.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 417-421
    • Su, J.R.1    Takeda, K.2    Tamura, S.3    Fujiki, Y.4    Miki, K.5
  • 46
    • 0029087571 scopus 로고
    • The Pichia pastoris peroxisomal protein PAS8p is the receptor for the C-terminal tripeptide peroxisome targeting signal
    • Terlecky, S.R., Nuttley, W.M., McCollum, D., Sock, E. & Subramani, S. (1995) The Pichia pastoris peroxisomal protein PAS8p is the receptor for the C-terminal tripeptide peroxisome targeting signal. EMBO J. 14, 3627-3634.
    • (1995) EMBO J. , vol.14 , pp. 3627-3634
    • Terlecky, S.R.1    Nuttley, W.M.2    McCollum, D.3    Sock, E.4    Subramani, S.5
  • 47
    • 0025342563 scopus 로고
    • Isolation and characterization of Chinese hamster ovary cell mutants defective in assembly of peroxisomes
    • Tsukamoto, T., Yokota, S. & Fujiki, Y. (1990) Isolation and characterization of Chinese hamster ovary cell mutants defective in assembly of peroxisomes. J. Cell Biol. 110, 651-660.
    • (1990) J. Cell Biol. , vol.110 , pp. 651-660
    • Tsukamoto, T.1    Yokota, S.2    Fujiki, Y.3
  • 48
    • 0034635364 scopus 로고    scopus 로고
    • Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p
    • Urquhart, A.J., Kennedy, D., Gould, S.J. & Crane, D.I. (2000) Interaction of Pex5p, the type 1 peroxisome targeting signal receptor, with the peroxisomal membrane proteins Pex14p and Pex13p. J. Biol. Chem. 275, 4127-4136.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4127-4136
    • Urquhart, A.J.1    Kennedy, D.2    Gould, S.J.3    Crane, D.I.4
  • 49
    • 0027138676 scopus 로고
    • PAS10 is a tetratricopeptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae
    • Van der Leij, I., Franse, M.M., Elgersma, Y., Distel, B. & Tabak, H.F. (1993) PAS10 is a tetratricopeptide-repeat protein that is essential for the import of most matrix proteins into peroxisomes of Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 90, 11782-11786.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11782-11786
    • Van der Leij, I.1    Franse, M.M.2    Elgersma, Y.3    Distel, B.4    Tabak, H.F.5
  • 50
    • 0029024783 scopus 로고
    • Human peroxisomal targeting signal-1 receptor restores peroxisomal protein import in cells from patients with fatal peroxisomal disorders
    • Wiemer, E.A., Nuttley, W.M., Bertolaet, B.L., Li, X., Francke, U., Wheelock, M.J., Anne, U.K., Johnson, K.R. & Subramani, S. (1995) Human peroxisomal targeting signal-1 receptor restores peroxisomal protein import in cells from patients with fatal peroxisomal disorders. J. Cell Biol. 130, 51-65.
    • (1995) J. Cell Biol. , vol.130 , pp. 51-65
    • Wiemer, E.A.1    Nuttley, W.M.2    Bertolaet, B.L.3    Li, X.4    Francke, U.5    Wheelock, M.J.6    Anne, U.K.7    Johnson, K.R.8    Subramani, S.9
  • 52
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: core machinery and adaptations
    • Xie, Z. & Klionsky, D.J. (2007) Autophagosome formation: core machinery and adaptations. Nat. Cell Biol. 9, 1102-1109.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 53
    • 84925775785 scopus 로고    scopus 로고
    • The membrane peroxin PEX3 induces peroxisome-ubiquitination-linked pexophagy
    • Yamashita, S., Abe, K., Tatemichi, Y. & Fujiki, Y. (2014) The membrane peroxin PEX3 induces peroxisome-ubiquitination-linked pexophagy. Autophagy 10, 1549-1564.
    • (2014) Autophagy , vol.10 , pp. 1549-1564
    • Yamashita, S.1    Abe, K.2    Tatemichi, Y.3    Fujiki, Y.4
  • 54
    • 38049062944 scopus 로고    scopus 로고
    • Pex14 is the sole component of the peroxisomal translocon that is required for pexophagy
    • van Zutphen, T., Veenhuis, M. & van der Klei, I.J. (2008) Pex14 is the sole component of the peroxisomal translocon that is required for pexophagy. Autophagy 4, 63-66.
    • (2008) Autophagy , vol.4 , pp. 63-66
    • van Zutphen, T.1    Veenhuis, M.2    van der Klei, I.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.