메뉴 건너뛰기




Volumn 1863, Issue 5, 2016, Pages 999-1005

Pexophagy and peroxisomal protein turnover in plants

Author keywords

Autophagy; LON protease; Organelle quality control; Peroxisome; Pexophagy; Protein degradation

Indexed keywords

ENDOPEPTIDASE LA; LON2 PROTEIN; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; ARABIDOPSIS PROTEIN; CELL RECEPTOR; ISOPROTEIN; LON2 PROTEIN, ARABIDOPSIS; PEROXISOMAL TARGETING SIGNAL 2 RECEPTOR; PEX5 PROTEIN, ARABIDOPSIS;

EID: 84975842459     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.09.005     Document Type: Review
Times cited : (52)

References (83)
  • 2
    • 44949151664 scopus 로고    scopus 로고
    • Seed storage oil mobilization
    • Graham I.A. Seed storage oil mobilization. Annu. Rev. Plant Biol. 2008, 59:115-142.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 115-142
    • Graham, I.A.1
  • 3
    • 79957506657 scopus 로고    scopus 로고
    • Transport and metabolism of the endogenous auxin precursor indole-3-butyric acid
    • Strader L.C., Bartel B. Transport and metabolism of the endogenous auxin precursor indole-3-butyric acid. Mol. Plant 2011, 4:477-486.
    • (2011) Mol. Plant , vol.4 , pp. 477-486
    • Strader, L.C.1    Bartel, B.2
  • 5
    • 84961129466 scopus 로고    scopus 로고
    • Peroxisome biogenesis, protein targeting mechanisms and PEX gene functions in plants
    • (in this issue)
    • Cross L.L., Ebeed H.T., Baker A. Peroxisome biogenesis, protein targeting mechanisms and PEX gene functions in plants. Biochim. Biophys. Acta, Mol. Cell Res. 2016, 1863(5):850-862. (in this issue).
    • (2016) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1863 , Issue.5 , pp. 850-862
    • Cross, L.L.1    Ebeed, H.T.2    Baker, A.3
  • 7
    • 57749091634 scopus 로고    scopus 로고
    • The DEG15 serine protease cleaves peroxisomal targeting signal 2-containing proteins in Arabidopsis
    • Schuhmann H., Huesgen P.F., Gietl C., Adamska I. The DEG15 serine protease cleaves peroxisomal targeting signal 2-containing proteins in Arabidopsis. Plant Physiol. 2008, 148:1847-1856.
    • (2008) Plant Physiol. , vol.148 , pp. 1847-1856
    • Schuhmann, H.1    Huesgen, P.F.2    Gietl, C.3    Adamska, I.4
  • 8
    • 0025941962 scopus 로고
    • A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase
    • Swinkels B.W., Gould S., Bodnar A., Rachubinski R., Subramani S. A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase. EMBO J. 1991, 10:3255-3262.
    • (1991) EMBO J. , vol.10 , pp. 3255-3262
    • Swinkels, B.W.1    Gould, S.2    Bodnar, A.3    Rachubinski, R.4    Subramani, S.5
  • 9
    • 84895142640 scopus 로고    scopus 로고
    • The peroxisomal receptor dislocation pathway: to the exportomer and beyond
    • Platta H.W., Hagen S., Reidick C., Erdmann R. The peroxisomal receptor dislocation pathway: to the exportomer and beyond. Biochimie 2014, 98:16-28.
    • (2014) Biochimie , vol.98 , pp. 16-28
    • Platta, H.W.1    Hagen, S.2    Reidick, C.3    Erdmann, R.4
  • 10
    • 79954779971 scopus 로고    scopus 로고
    • Making new out of old: recycling and modification of an ancient protein translocation system during eukaryotic evolution
    • Bolte K., Gruenheit N., Felsner G., Sommer M.S., Maier U.-G., Hempel F. Making new out of old: recycling and modification of an ancient protein translocation system during eukaryotic evolution. BioEssays 2011, 33:368-376.
    • (2011) BioEssays , vol.33 , pp. 368-376
    • Bolte, K.1    Gruenheit, N.2    Felsner, G.3    Sommer, M.S.4    Maier, U.-G.5    Hempel, F.6
  • 11
    • 78649403829 scopus 로고    scopus 로고
    • Peroxisomal protein import and ERAD: variations on a common theme
    • Schliebs W., Girzalsky W., Erdmann R. Peroxisomal protein import and ERAD: variations on a common theme. Nat. Rev. Mol. Cell Biol. 2010, 11:885-890.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 885-890
    • Schliebs, W.1    Girzalsky, W.2    Erdmann, R.3
  • 12
    • 33644825185 scopus 로고    scopus 로고
    • Identification and functional characterization of Arabidopsis PEROXIN4 and the interacting protein PEROXIN22
    • Zolman B.K., Monroe-Augustus M., Silva I.D., Bartel B. Identification and functional characterization of Arabidopsis PEROXIN4 and the interacting protein PEROXIN22. Plant Cell 2005, 17:3422-3435.
    • (2005) Plant Cell , vol.17 , pp. 3422-3435
    • Zolman, B.K.1    Monroe-Augustus, M.2    Silva, I.D.3    Bartel, B.4
  • 14
    • 84871743525 scopus 로고    scopus 로고
    • Genetic dissection of peroxisome-associated matrix protein degradation in Arabidopsis thaliana
    • Burkhart S.E., Lingard M.J., Bartel B. Genetic dissection of peroxisome-associated matrix protein degradation in Arabidopsis thaliana. Genetics 2013, 193:125-141.
    • (2013) Genetics , vol.193 , pp. 125-141
    • Burkhart, S.E.1    Lingard, M.J.2    Bartel, B.3
  • 15
    • 84908592628 scopus 로고    scopus 로고
    • Peroxisomal ubiquitin-protein ligases Peroxin2 and Peroxin10 have distinct but synergistic roles in matrix protein import and Peroxin5 retrotranslocation in Arabidopsis
    • Burkhart S.E., Kao Y.-T., Bartel B. Peroxisomal ubiquitin-protein ligases Peroxin2 and Peroxin10 have distinct but synergistic roles in matrix protein import and Peroxin5 retrotranslocation in Arabidopsis. Plant Physiol. 2014, 166:1329-1344.
    • (2014) Plant Physiol. , vol.166 , pp. 1329-1344
    • Burkhart, S.E.1    Kao, Y.-T.2    Bartel, B.3
  • 16
    • 84865596150 scopus 로고    scopus 로고
    • Autophagy: a multifaceted intracellular system for bulk and selective recycling
    • Li F., Vierstra R.D. Autophagy: a multifaceted intracellular system for bulk and selective recycling. Trends Plant Sci. 2012, 17:526-537.
    • (2012) Trends Plant Sci. , vol.17 , pp. 526-537
    • Li, F.1    Vierstra, R.D.2
  • 17
    • 0037031843 scopus 로고    scopus 로고
    • The APG8/12-activating enzyme APG7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana
    • Doelling J.H., Walker J.M., Friedman E.M., Thompson A.R., Vierstra R.D. The APG8/12-activating enzyme APG7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana. J. Biolumin. Chemilumin. 2002, 277:33105-33114.
    • (2002) J. Biolumin. Chemilumin. , vol.277 , pp. 33105-33114
    • Doelling, J.H.1    Walker, J.M.2    Friedman, E.M.3    Thompson, A.R.4    Vierstra, R.D.5
  • 18
    • 79958199637 scopus 로고    scopus 로고
    • A critical role of autophagy in plant resistance to necrotrophic fungal pathogens
    • Lai Z., Wang F., Zheng Z., Fan B., Chen Z. A critical role of autophagy in plant resistance to necrotrophic fungal pathogens. Plant J. 2011, 66:953-968.
    • (2011) Plant J. , vol.66 , pp. 953-968
    • Lai, Z.1    Wang, F.2    Zheng, Z.3    Fan, B.4    Chen, Z.5
  • 19
    • 84873519723 scopus 로고    scopus 로고
    • NBR1-mediated selective autophagy targets insoluble ubiquitinated protein aggregates in plant stress responses
    • Zhou J., Wang J., Cheng Y., Chi Y.J., Fan B., Yu J.Q., Chen Z. NBR1-mediated selective autophagy targets insoluble ubiquitinated protein aggregates in plant stress responses. PLoS Genet. 2013, 9.
    • (2013) PLoS Genet. , vol.9
    • Zhou, J.1    Wang, J.2    Cheng, Y.3    Chi, Y.J.4    Fan, B.5    Yu, J.Q.6    Chen, Z.7
  • 20
    • 70349645984 scopus 로고    scopus 로고
    • Autophagy is required for tolerance of drought and salt stress in plants
    • Liu Y., Xiong Y., Bassham D.C. Autophagy is required for tolerance of drought and salt stress in plants. Autophagy 2009, 5:954-963.
    • (2009) Autophagy , vol.5 , pp. 954-963
    • Liu, Y.1    Xiong, Y.2    Bassham, D.C.3
  • 21
    • 33846378524 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by autophagy during oxidative stress in Arabidopsis
    • Xiong Y., Contento A.L., Nguyen P.Q., Bassham D.C. Degradation of oxidized proteins by autophagy during oxidative stress in Arabidopsis. Plant Physiol. 2007, 143:291-299.
    • (2007) Plant Physiol. , vol.143 , pp. 291-299
    • Xiong, Y.1    Contento, A.L.2    Nguyen, P.Q.3    Bassham, D.C.4
  • 22
    • 70849127320 scopus 로고    scopus 로고
    • Autophagy negatively regulates cell death by controlling NPR1-dependent salicylic acid signaling during senescence and the innate immune response in Arabidopsis
    • Yoshimoto K., Jikumaru Y., Kamiya Y., Kusano M., Consonni C., Panstruga R., Ohsumi Y., Shirasu K. Autophagy negatively regulates cell death by controlling NPR1-dependent salicylic acid signaling during senescence and the innate immune response in Arabidopsis. Plant Cell 2009, 21:2914-2927.
    • (2009) Plant Cell , vol.21 , pp. 2914-2927
    • Yoshimoto, K.1    Jikumaru, Y.2    Kamiya, Y.3    Kusano, M.4    Consonni, C.5    Panstruga, R.6    Ohsumi, Y.7    Shirasu, K.8
  • 23
    • 82755166963 scopus 로고    scopus 로고
    • The ATG1/ATG13 protein kinase complex is both a regulator and a target of autophagic recycling in Arabidopsis
    • Suttangkakul A., Li F., Chung T., Vierstra R.D. The ATG1/ATG13 protein kinase complex is both a regulator and a target of autophagic recycling in Arabidopsis. Plant Cell 2011, 23:3761-3779.
    • (2011) Plant Cell , vol.23 , pp. 3761-3779
    • Suttangkakul, A.1    Li, F.2    Chung, T.3    Vierstra, R.D.4
  • 24
    • 84937574462 scopus 로고    scopus 로고
    • Autophagic degradation of the 26S proteasome is mediated by the dual ATG8/ubiquitin receptor RPN10 in Arabidopsis
    • Marshall R.S., Li F., Gemperline D.C., Book A.J., Vierstra R.D. Autophagic degradation of the 26S proteasome is mediated by the dual ATG8/ubiquitin receptor RPN10 in Arabidopsis. Mol. Cell 2015, 58:1053-1066.
    • (2015) Mol. Cell , vol.58 , pp. 1053-1066
    • Marshall, R.S.1    Li, F.2    Gemperline, D.C.3    Book, A.J.4    Vierstra, R.D.5
  • 25
    • 84871899675 scopus 로고    scopus 로고
    • Degradation of the endoplasmic reticulum by autophagy during endoplasmic reticulum stress in Arabidopsis
    • Liu Y., Burgos J.S., Deng Y., Srivastava R., Howell S.H., Bassham D.C. Degradation of the endoplasmic reticulum by autophagy during endoplasmic reticulum stress in Arabidopsis. Plant Cell 2012, 24:4635-4651.
    • (2012) Plant Cell , vol.24 , pp. 4635-4651
    • Liu, Y.1    Burgos, J.S.2    Deng, Y.3    Srivastava, R.4    Howell, S.H.5    Bassham, D.C.6
  • 27
    • 0014837856 scopus 로고
    • Cytochemical and developmental changes in microbodies (glyoxysomes) and related organelles of castor bean endosperm
    • Vigil E.L. Cytochemical and developmental changes in microbodies (glyoxysomes) and related organelles of castor bean endosperm. J. Cell Biol. 1970, 46:435-454.
    • (1970) J. Cell Biol. , vol.46 , pp. 435-454
    • Vigil, E.L.1
  • 28
    • 84888418176 scopus 로고    scopus 로고
    • Disrupting autophagy restores peroxisome function to an Arabidopsis lon2 mutant and reveals a role for the LON2 protease in peroxisomal matrix protein degradation
    • Farmer L.M., Rinaldi M.A., Young P.G., Danan C.H., Burkhart S.E., Bartel B. Disrupting autophagy restores peroxisome function to an Arabidopsis lon2 mutant and reveals a role for the LON2 protease in peroxisomal matrix protein degradation. Plant Cell 2013, 25:4085-4100.
    • (2013) Plant Cell , vol.25 , pp. 4085-4100
    • Farmer, L.M.1    Rinaldi, M.A.2    Young, P.G.3    Danan, C.H.4    Burkhart, S.E.5    Bartel, B.6
  • 29
    • 84893114070 scopus 로고    scopus 로고
    • Autophagy-related proteins are required for degradation of peroxisomes in Arabidopsis hypocotyls during seedling growth
    • Kim J., Lee H., Lee H.N., Kim S.-H., Shin K.D., Chung T. Autophagy-related proteins are required for degradation of peroxisomes in Arabidopsis hypocotyls during seedling growth. Plant Cell 2013, 25:4956-4966.
    • (2013) Plant Cell , vol.25 , pp. 4956-4966
    • Kim, J.1    Lee, H.2    Lee, H.N.3    Kim, S.-H.4    Shin, K.D.5    Chung, T.6
  • 33
    • 0001124810 scopus 로고
    • Microbodies in higher plants
    • Beevers H. Microbodies in higher plants. Annu. Rev. Plant Physiol. 1979, 30:159-193.
    • (1979) Annu. Rev. Plant Physiol. , vol.30 , pp. 159-193
    • Beevers, H.1
  • 34
    • 0022395410 scopus 로고
    • Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double-label immunoelectron microscopy
    • Titus D.E., Becker W.M. Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double-label immunoelectron microscopy. J. Cell Biol. 1985, 101:1288-1299.
    • (1985) J. Cell Biol. , vol.101 , pp. 1288-1299
    • Titus, D.E.1    Becker, W.M.2
  • 35
    • 0001661482 scopus 로고
    • Immunocytochemical analysis shows that glyoxysomes are directly transformed to leaf peroxisomes during greening of pumpkin cotyledons
    • Nishimura M., Yamaguchi J., Mori H., Akazawa T., Yokota S. Immunocytochemical analysis shows that glyoxysomes are directly transformed to leaf peroxisomes during greening of pumpkin cotyledons. Plant Physiol. 1986, 81:313-316.
    • (1986) Plant Physiol. , vol.81 , pp. 313-316
    • Nishimura, M.1    Yamaguchi, J.2    Mori, H.3    Akazawa, T.4    Yokota, S.5
  • 36
    • 0001454517 scopus 로고
    • Microbody transition in greening watermelon cotyledons. Double immunocytochemical labeling of isocitrate lyase and hydroxypyruvate reductase
    • Sautter C. Microbody transition in greening watermelon cotyledons. Double immunocytochemical labeling of isocitrate lyase and hydroxypyruvate reductase. Planta 1986, 167:491-503.
    • (1986) Planta , vol.167 , pp. 491-503
    • Sautter, C.1
  • 37
    • 0001713550 scopus 로고
    • Glyoxysomal malate synthetase is specifically degraded in microbodies during greening of pumpkin cotyledons
    • Mori H., Nishimura M. Glyoxysomal malate synthetase is specifically degraded in microbodies during greening of pumpkin cotyledons. FEBS Lett. 1989, 244:163-166.
    • (1989) FEBS Lett. , vol.244 , pp. 163-166
    • Mori, H.1    Nishimura, M.2
  • 38
    • 70350633819 scopus 로고    scopus 로고
    • Arabidopsis LON2 is necessary for peroxisomal function and sustained matrix protein import
    • Lingard M.J., Bartel B. Arabidopsis LON2 is necessary for peroxisomal function and sustained matrix protein import. Plant Physiol. 2009, 151:1354-1365.
    • (2009) Plant Physiol. , vol.151 , pp. 1354-1365
    • Lingard, M.J.1    Bartel, B.2
  • 39
    • 84928895757 scopus 로고    scopus 로고
    • Protein maturation and proteolysis in plant plastids, mitochondria, and peroxisomes
    • van Wijk K.J. Protein maturation and proteolysis in plant plastids, mitochondria, and peroxisomes. Annu. Rev. Plant Biol. 2015, 66:75-111.
    • (2015) Annu. Rev. Plant Biol. , vol.66 , pp. 75-111
    • van Wijk, K.J.1
  • 40
    • 12444275266 scopus 로고
    • Phytochrome-mediated transformation of glyoxysomes into peroxisomes in the cotyledons of mustard (Sinapis alba L.) seedlings
    • Schopfer P., Bajracharya D., Bergfeld R., Falk H. Phytochrome-mediated transformation of glyoxysomes into peroxisomes in the cotyledons of mustard (Sinapis alba L.) seedlings. Planta 1976, 133:73-80.
    • (1976) Planta , vol.133 , pp. 73-80
    • Schopfer, P.1    Bajracharya, D.2    Bergfeld, R.3    Falk, H.4
  • 42
    • 15544374294 scopus 로고    scopus 로고
    • Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in β-oxidation
    • Adham A.R., Zolman B.K., Millius A., Bartel B. Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in β-oxidation. Plant J. 2005, 41:859-874.
    • (2005) Plant J. , vol.41 , pp. 859-874
    • Adham, A.R.1    Zolman, B.K.2    Millius, A.3    Bartel, B.4
  • 45
    • 57749111568 scopus 로고    scopus 로고
    • Generation of hydrogen peroxide in chloroplasts of Arabidopsis overexpressing glycolate oxidase as an inducible system to study oxidative stress
    • Fahnenstich H., Scarpeci T.E., Valle E.M., Flugge U.I., Maurino V.G. Generation of hydrogen peroxide in chloroplasts of Arabidopsis overexpressing glycolate oxidase as an inducible system to study oxidative stress. Plant Physiol. 2008, 148:719-729.
    • (2008) Plant Physiol. , vol.148 , pp. 719-729
    • Fahnenstich, H.1    Scarpeci, T.E.2    Valle, E.M.3    Flugge, U.I.4    Maurino, V.G.5
  • 47
    • 70350329375 scopus 로고    scopus 로고
    • Hydrogen peroxide induced oxidation of peroxisomal malate synthase and catalase
    • Anand P., Kwak Y., Simha R., Donaldson R.P. Hydrogen peroxide induced oxidation of peroxisomal malate synthase and catalase. Arch. Biochem. Biophys. 2009, 491:25-31.
    • (2009) Arch. Biochem. Biophys. , vol.491 , pp. 25-31
    • Anand, P.1    Kwak, Y.2    Simha, R.3    Donaldson, R.P.4
  • 49
    • 84979944488 scopus 로고    scopus 로고
    • Plant peroxisomes are degraded by starvation-induced and constitutive autophagy in tobacco BY-2 suspension-cultured cells
    • Voitsekhovskaja O.V., Schiermeyer A., Reumann S. Plant peroxisomes are degraded by starvation-induced and constitutive autophagy in tobacco BY-2 suspension-cultured cells. Front. Plant. Sci. 2014, 5:629.
    • (2014) Front. Plant. Sci. , vol.5 , pp. 629
    • Voitsekhovskaja, O.V.1    Schiermeyer, A.2    Reumann, S.3
  • 50
    • 84975787725 scopus 로고    scopus 로고
    • Using forward genetics to elucidate peroxisome biogenesis and peroxisome-associated protein degradation in Arabidopsis thaliana
    • Rice University
    • Burkhart S. Using forward genetics to elucidate peroxisome biogenesis and peroxisome-associated protein degradation in Arabidopsis thaliana. BioSciences 2013, Rice University, (https://scholarship.rice.edu/handle/1911/76470).
    • (2013) BioSciences
    • Burkhart, S.1
  • 51
    • 84899115843 scopus 로고    scopus 로고
    • Chaperone and protease functions of LON protease 2 modulate the peroxisomal transition and degradation with autophagy
    • Goto-Yamada S., Mano S., Nakamori C., Kondo M., Yamawaki R., Kato A., Nishimura M. Chaperone and protease functions of LON protease 2 modulate the peroxisomal transition and degradation with autophagy. Plant Cell Physiol. 2014, 55:482-496.
    • (2014) Plant Cell Physiol. , vol.55 , pp. 482-496
    • Goto-Yamada, S.1    Mano, S.2    Nakamori, C.3    Kondo, M.4    Yamawaki, R.5    Kato, A.6    Nishimura, M.7
  • 53
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer L.M., Leipe D.D., Koonin E.V., Aravind L. Evolutionary history and higher order classification of AAA+ ATPases. J. Struct. Biol. 2004, 146:11-31.
    • (2004) J. Struct. Biol. , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 54
    • 84901056356 scopus 로고    scopus 로고
    • Evolution and significance of the Lon gene family in Arabidopsis organelle biogenesis and energy metabolism
    • Rigas S., Daras G., Tsitsekian D., Alatzas A., Hatzopoulos P. Evolution and significance of the Lon gene family in Arabidopsis organelle biogenesis and energy metabolism. Front. Plant. Sci. 2014, 5:145.
    • (2014) Front. Plant. Sci. , vol.5 , pp. 145
    • Rigas, S.1    Daras, G.2    Tsitsekian, D.3    Alatzas, A.4    Hatzopoulos, P.5
  • 56
    • 84891165714 scopus 로고    scopus 로고
    • Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity
    • Wohlever M.L., Baker T.A., Sauer R.T. Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity. Mol. Microbiol. 2014, 91:66-78.
    • (2014) Mol. Microbiol. , vol.91 , pp. 66-78
    • Wohlever, M.L.1    Baker, T.A.2    Sauer, R.T.3
  • 57
    • 84901017612 scopus 로고    scopus 로고
    • Alternative transcription initiation and the AUG context configuration control dual-organellar targeting and functional competence of Arabidopsis Lon1 protease
    • Daras G., Rigas S., Tsitsekian D., Zur H., Tuller T., Hatzopoulos P. Alternative transcription initiation and the AUG context configuration control dual-organellar targeting and functional competence of Arabidopsis Lon1 protease. Mol. Plant 2014, 7:989-1005.
    • (2014) Mol. Plant , vol.7 , pp. 989-1005
    • Daras, G.1    Rigas, S.2    Tsitsekian, D.3    Zur, H.4    Tuller, T.5    Hatzopoulos, P.6
  • 58
    • 34548417715 scopus 로고    scopus 로고
    • Multiple intracellular locations of Lon protease in Arabidopsis: evidence for the localization of AtLon4 to chloroplasts
    • Ostersetzer O., Kato Y., Adam Z., Sakamoto W. Multiple intracellular locations of Lon protease in Arabidopsis: evidence for the localization of AtLon4 to chloroplasts. Plant Cell Physiol. 2007, 48:881-885.
    • (2007) Plant Cell Physiol. , vol.48 , pp. 881-885
    • Ostersetzer, O.1    Kato, Y.2    Adam, Z.3    Sakamoto, W.4
  • 60
    • 84901615924 scopus 로고    scopus 로고
    • PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix
    • Thomas R.E., Andrews L.A., Burman J.L., Lin W.-Y., Pallanck L.J. PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix. PLoS Genet. 2014, 10.
    • (2014) PLoS Genet. , vol.10
    • Thomas, R.E.1    Andrews, L.A.2    Burman, J.L.3    Lin, W.-Y.4    Pallanck, L.J.5
  • 66
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D., Tanaka A., Suen D.F., Youle R.J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 2008, 183:795-803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 67
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin S.M., Lazarou M., Wang C., Kane L.A., Narendra D.P., Youle R.J. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 2010, 191:933-942.
    • (2010) J. Cell Biol. , vol.191 , pp. 933-942
    • Jin, S.M.1    Lazarou, M.2    Wang, C.3    Kane, L.A.4    Narendra, D.P.5    Youle, R.J.6
  • 68
    • 58249113926 scopus 로고    scopus 로고
    • Role of Lon1 protease in post-germinative growth and maintenance of mitochondrial function in Arabidopsis thaliana
    • Rigas S., Daras G., Laxa M., Marathias N., Fasseas C., Sweetlove L.J., Hatzopoulos P. Role of Lon1 protease in post-germinative growth and maintenance of mitochondrial function in Arabidopsis thaliana. New Phytol. 2009, 181:588-600.
    • (2009) New Phytol. , vol.181 , pp. 588-600
    • Rigas, S.1    Daras, G.2    Laxa, M.3    Marathias, N.4    Fasseas, C.5    Sweetlove, L.J.6    Hatzopoulos, P.7
  • 70
    • 84863843241 scopus 로고    scopus 로고
    • Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
    • Motley A.M., Nuttall J.M., Hettema E.H. Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae. EMBO J. 2012, 31:2852-2868.
    • (2012) EMBO J. , vol.31 , pp. 2852-2868
    • Motley, A.M.1    Nuttall, J.M.2    Hettema, E.H.3
  • 74
    • 80052363973 scopus 로고    scopus 로고
    • Plant NBR1 is a selective autophagy substrate and a functional hybrid of the mammalian autophagic adapters NBR1 and p62/SQSTM1
    • Svenning S., Lamark T., Krause K., Johansen T. Plant NBR1 is a selective autophagy substrate and a functional hybrid of the mammalian autophagic adapters NBR1 and p62/SQSTM1. Autophagy 2011, 7:993-1010.
    • (2011) Autophagy , vol.7 , pp. 993-1010
    • Svenning, S.1    Lamark, T.2    Krause, K.3    Johansen, T.4
  • 76
    • 67849101909 scopus 로고    scopus 로고
    • Disruption of Arabidopsis CHY1 reveals an important role of metabolic status in plant cold stress signaling
    • Dong C.-H., Zolman B.K., Bartel B., Lee B.-h., Stevenson B., Agarwal M., Zhu J.-K. Disruption of Arabidopsis CHY1 reveals an important role of metabolic status in plant cold stress signaling. Mol. Plant 2009, 2:59-72.
    • (2009) Mol. Plant , vol.2 , pp. 59-72
    • Dong, C.-H.1    Zolman, B.K.2    Bartel, B.3    Lee, B.-H.4    Stevenson, B.5    Agarwal, M.6    Zhu, J.-K.7
  • 77
    • 77954065435 scopus 로고    scopus 로고
    • Deficiencies in jasmonate-mediated plant defense reveal quantitative variation in Botrytis cinerea pathogenesis
    • Rowe H.C., Walley J.W., Corwin J., Chan E.K., Dehesh K., Kliebenstein D.J. Deficiencies in jasmonate-mediated plant defense reveal quantitative variation in Botrytis cinerea pathogenesis. PLoS Pathog. 2010, 6.
    • (2010) PLoS Pathog. , vol.6
    • Rowe, H.C.1    Walley, J.W.2    Corwin, J.3    Chan, E.K.4    Dehesh, K.5    Kliebenstein, D.J.6
  • 78
    • 84896731136 scopus 로고    scopus 로고
    • E3 ubiquitin ligase CHIP and NBR1-mediated selective autophagy protect additively against proteotoxicity in plant stress responses
    • Zhou J., Zhang Y., Qi J., Chi Y., Fan B., Yu J.Q., Chen Z. E3 ubiquitin ligase CHIP and NBR1-mediated selective autophagy protect additively against proteotoxicity in plant stress responses. PLoS Genet. 2014, 10.
    • (2014) PLoS Genet. , vol.10
    • Zhou, J.1    Zhang, Y.2    Qi, J.3    Chi, Y.4    Fan, B.5    Yu, J.Q.6    Chen, Z.7
  • 79
  • 80
    • 84925776380 scopus 로고    scopus 로고
    • Peroxisomal Pex3 activates selective autophagy of peroxisomes via interaction with the pexophagy receptor Atg30
    • Burnett S.F., Farré J.-C., Nazarko T.Y., Subramani S. Peroxisomal Pex3 activates selective autophagy of peroxisomes via interaction with the pexophagy receptor Atg30. J. Biolumin. Chemilumin. 2015, 290:8623-8631.
    • (2015) J. Biolumin. Chemilumin. , vol.290 , pp. 8623-8631
    • Burnett, S.F.1    Farré, J.-C.2    Nazarko, T.Y.3    Subramani, S.4
  • 81
    • 12844279810 scopus 로고    scopus 로고
    • The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5
    • Woodward A.W., Bartel B. The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5. Mol. Biol. Cell 2005, 16:573-583.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 573-583
    • Woodward, A.W.1    Bartel, B.2
  • 82
    • 34247330193 scopus 로고    scopus 로고
    • Arabidopsis peroxisomal malate dehydrogenase functions in β-oxidation but not in the glyoxylate cycle
    • Pracharoenwattana I., Cornah J.E., Smith S.M. Arabidopsis peroxisomal malate dehydrogenase functions in β-oxidation but not in the glyoxylate cycle. Plant J. 2007, 50:381-390.
    • (2007) Plant J. , vol.50 , pp. 381-390
    • Pracharoenwattana, I.1    Cornah, J.E.2    Smith, S.M.3
  • 83
    • 0027650968 scopus 로고
    • Targeting of glyoxysomal proteins to peroxisomes in leaves and roots of a higher plant
    • Olsen L.J., Ettinger W.F., Damsz B., Matsudaira K., Webb M.A., Harada J.J. Targeting of glyoxysomal proteins to peroxisomes in leaves and roots of a higher plant. Plant Cell 1993, 5:941-952.
    • (1993) Plant Cell , vol.5 , pp. 941-952
    • Olsen, L.J.1    Ettinger, W.F.2    Damsz, B.3    Matsudaira, K.4    Webb, M.A.5    Harada, J.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.