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Volumn 12, Issue 6, 2009, Pages 705-713

Cellular processes relying on sterol function in plants

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; CARRIER PROTEIN; INDOLEACETIC ACID DERIVATIVE; PHYTOSTEROL;

EID: 70450176714     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbi.2009.09.013     Document Type: Review
Times cited : (94)

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    • Definition of Arabidopsis sterol-rich membrane microdomains by differential treatment with methyl-beta-cyclodextrin and quantitative proteomics
    • This study uses an elegant proteomic approach to define which DRM-enriched proteins in Arabidopsis are sensitive to treatment with methyl-β-cyclodextrin. Future in vivo studies may reveal whether these proteins, sterols and sphingolipids cluster in nanodomains or microdomains of plant membranes.
    • Kierszniowska S., Seiwert B., and Schulze W.X. Definition of Arabidopsis sterol-rich membrane microdomains by differential treatment with methyl-beta-cyclodextrin and quantitative proteomics. Mol Cell Proteomics 8 (2009) 612-623. This study uses an elegant proteomic approach to define which DRM-enriched proteins in Arabidopsis are sensitive to treatment with methyl-β-cyclodextrin. Future in vivo studies may reveal whether these proteins, sterols and sphingolipids cluster in nanodomains or microdomains of plant membranes.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 612-623
    • Kierszniowska, S.1    Seiwert, B.2    Schulze, W.X.3
  • 41
    • 60149111601 scopus 로고    scopus 로고
    • Alterations in detergent-resistant plasma membrane microdomains in Arabidopsis thaliana during cold acclimation
    • •], the authors of this work characterize DRM composition before and after a cold acclimation of Arabidopsis plants. This reveals that P-type-ATPase, aquaporins and endocytosis-related proteins are enriched in DRMs during cold acclimation, whilst microtubule elements and V-type-ATPase are depleted.
    • •], the authors of this work characterize DRM composition before and after a cold acclimation of Arabidopsis plants. This reveals that P-type-ATPase, aquaporins and endocytosis-related proteins are enriched in DRMs during cold acclimation, whilst microtubule elements and V-type-ATPase are depleted.
    • (2009) Plant Cell Physiol , vol.50 , pp. 341-359
    • Minami, A.1    Fujiwara, M.2    Furuto, A.3    Fukao, Y.4    Yamashita, T.5    Kamo, M.6    Kawamura, Y.7    Uemura, M.8
  • 42
    • 67651092036 scopus 로고    scopus 로고
    • Remorin, a Solanaceae protein resident in membrane rafts and plasmodesmata, impairs Potato virus X movement
    • This paper reports that the DRM-enriched protein remorin clusters in ∼70 nm domains at the plasma-membrane in situ and that a fluorescent protein fusion to remorin displays a domain localization at the plasma-membrane in vivo. The study opens the door for in vivo characterization of nanodomains in plants. Future studies may address whether the observed nanodomains are enriched in sterols and sphingolipids in vivo.
    • Raffaele S., Bayer E., Lafarge D., Cluzet S., Retana S.G., Boubekeur T., Leborgne-Castel N., Carde J.P., Lherminier J., Noirot E., et al. Remorin, a Solanaceae protein resident in membrane rafts and plasmodesmata, impairs Potato virus X movement. Plant Cell 21 (2009) 1541-1555. This paper reports that the DRM-enriched protein remorin clusters in ∼70 nm domains at the plasma-membrane in situ and that a fluorescent protein fusion to remorin displays a domain localization at the plasma-membrane in vivo. The study opens the door for in vivo characterization of nanodomains in plants. Future studies may address whether the observed nanodomains are enriched in sterols and sphingolipids in vivo.
    • (2009) Plant Cell , vol.21 , pp. 1541-1555
    • Raffaele, S.1    Bayer, E.2    Lafarge, D.3    Cluzet, S.4    Retana, S.G.5    Boubekeur, T.6    Leborgne-Castel, N.7    Carde, J.P.8    Lherminier, J.9    Noirot, E.10
  • 43
    • 58149117560 scopus 로고    scopus 로고
    • ABCB19/PGP19 stabilises PIN1 inmembrane microdomains in Arabidopsis
    • This study raises the question as to whether ABCB19/PGP19 and PIN1 cluster together and interact in potential microdomains or nanodomains within the plasma membrane.
    • Titapiwatanakun B., Blakeslee J.J., Bandyopadhyay A., Yang H., Mravec J., Sauer M., Cheng Y., Adamec J., Nagashima A., Geisler M., et al. ABCB19/PGP19 stabilises PIN1 inmembrane microdomains in Arabidopsis. Plant J 57 (2009) 27-44. This study raises the question as to whether ABCB19/PGP19 and PIN1 cluster together and interact in potential microdomains or nanodomains within the plasma membrane.
    • (2009) Plant J , vol.57 , pp. 27-44
    • Titapiwatanakun, B.1    Blakeslee, J.J.2    Bandyopadhyay, A.3    Yang, H.4    Mravec, J.5    Sauer, M.6    Cheng, Y.7    Adamec, J.8    Nagashima, A.9    Geisler, M.10
  • 44
    • 54149103523 scopus 로고    scopus 로고
    • FM dyes label sterol-rich plasma membrane domains and are internalized independently of the cytoskeleton in characean internodal cells
    • These authors report that the endocytic tracer FM4-64 and the sterol-binding probe filipin co-label large sterol-enriched domains at the plasma membrane of internodal cells in the green alga Chara chorallina.
    • Klima A., and Foissner I. FM dyes label sterol-rich plasma membrane domains and are internalized independently of the cytoskeleton in characean internodal cells. Plant Cell Physiol 49 (2008) 1508-1521. These authors report that the endocytic tracer FM4-64 and the sterol-binding probe filipin co-label large sterol-enriched domains at the plasma membrane of internodal cells in the green alga Chara chorallina.
    • (2008) Plant Cell Physiol , vol.49 , pp. 1508-1521
    • Klima, A.1    Foissner, I.2
  • 45
    • 0035823586 scopus 로고    scopus 로고
    • Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide
    • Xu X., Bittman R., Duportail G., Heissler D., Vilcheze C., and London E. Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide. J Biol Chem 276 (2001) 33540-33546
    • (2001) J Biol Chem , vol.276 , pp. 33540-33546
    • Xu, X.1    Bittman, R.2    Duportail, G.3    Heissler, D.4    Vilcheze, C.5    London, E.6
  • 46
    • 34249811510 scopus 로고    scopus 로고
    • Plant sterols in "rafts": a better way to regulate membrane thermal shocks
    • 2H NMR to show that in vitro reconstituted membranes containing plant lipids can form liquid ordered phases. These are tightly packed and thought to resemble the physiological state of membrane rafts in animal and yeast cells. The study further compares membranes reconstituted from plant, mammal and yeast sterols/lipids showing that plant model membranes are less sensitive to temperature changes than others.
    • 2H NMR to show that in vitro reconstituted membranes containing plant lipids can form liquid ordered phases. These are tightly packed and thought to resemble the physiological state of membrane rafts in animal and yeast cells. The study further compares membranes reconstituted from plant, mammal and yeast sterols/lipids showing that plant model membranes are less sensitive to temperature changes than others.
    • (2007) FASEB J , vol.21 , pp. 1714-1723
    • Beck, J.G.1    Mathieu, D.2    Loudet, C.3    Buchoux, S.4    Dufourc, E.J.5
  • 48
    • 33845784713 scopus 로고    scopus 로고
    • Subcellular trafficking of the Arabidopsis auxin influx carrier AUX1 uses a novel pathway distinct from PIN1
    • Kleine-Vehn J., Dhonukshe P., Swarup R., Bennett M., and Friml J. Subcellular trafficking of the Arabidopsis auxin influx carrier AUX1 uses a novel pathway distinct from PIN1. Plant Cell 18 (2006) 3171-3181
    • (2006) Plant Cell , vol.18 , pp. 3171-3181
    • Kleine-Vehn, J.1    Dhonukshe, P.2    Swarup, R.3    Bennett, M.4    Friml, J.5
  • 49
    • 64749115978 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase SCFTIR1/AFB and membrane sterols play key roles in auxin regulation of endocytosis, recycling, and plasma membrane accumulation of the auxin efflux transporter PIN2 in Arabidopsis thaliana
    • This study reports that sterol composition and TIR1-family auxin receptor signalling mediate the effects of exogenously applied auxin on PIN2 endocytosis.
    • Pan J., Fujioka S., Peng J., Chen J., Li G., and Chen R. The E3 ubiquitin ligase SCFTIR1/AFB and membrane sterols play key roles in auxin regulation of endocytosis, recycling, and plasma membrane accumulation of the auxin efflux transporter PIN2 in Arabidopsis thaliana. Plant Cell 21 (2009) 568-580. This study reports that sterol composition and TIR1-family auxin receptor signalling mediate the effects of exogenously applied auxin on PIN2 endocytosis.
    • (2009) Plant Cell , vol.21 , pp. 568-580
    • Pan, J.1    Fujioka, S.2    Peng, J.3    Chen, J.4    Li, G.5    Chen, R.6
  • 51
    • 7044260932 scopus 로고    scopus 로고
    • Where sterols are required for endocytosis
    • Pichler H., and Riezman H. Where sterols are required for endocytosis. Biochim Biophys Acta 1666 (2004) 51-61
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 51-61
    • Pichler, H.1    Riezman, H.2
  • 53
    • 53749097393 scopus 로고    scopus 로고
    • Comparison of the dynamics and functional redundancy of the Arabidopsis dynamin-related isoforms DRP1A and DRP1C during plant development
    • ••], this work employs confocal and variable angle microscopy-based advanced live imaging of DRP1A and DRP1C fused to fluorescent proteins, revealing co-localization and co-trafficking with CLC fused to a fluorescent protein in foci at the plasma membrane. The studies further report the dependence of DRP1A, DRP1C and CLC dynamics at the plasma membrane on correct sterol composition, as supported by pharmacological interference with sterol biosynthesis by employing the inhibitor fenpropimorph.
    • ••], this work employs confocal and variable angle microscopy-based advanced live imaging of DRP1A and DRP1C fused to fluorescent proteins, revealing co-localization and co-trafficking with CLC fused to a fluorescent protein in foci at the plasma membrane. The studies further report the dependence of DRP1A, DRP1C and CLC dynamics at the plasma membrane on correct sterol composition, as supported by pharmacological interference with sterol biosynthesis by employing the inhibitor fenpropimorph.
    • (2008) Plant Physiol , vol.147 , pp. 1590-1602
    • Konopka, C.A.1    Bednarek, S.Y.2
  • 54
    • 41649096142 scopus 로고    scopus 로고
    • Arabidopsis dynamin-like protein DRP1A: a null mutant with widespread defects in endocytosis, cellulose synthesis, cytokinesis, and cell expansion
    • Collings D.A., Gebbie L.K., Howles P.A., Hurley U.A., Birch R.J., Cork A.H., Hocart C.H., Arioli T., and Williamson R.E. Arabidopsis dynamin-like protein DRP1A: a null mutant with widespread defects in endocytosis, cellulose synthesis, cytokinesis, and cell expansion. J Exp Bot 59 (2008) 361-376
    • (2008) J Exp Bot , vol.59 , pp. 361-376
    • Collings, D.A.1    Gebbie, L.K.2    Howles, P.A.3    Hurley, U.A.4    Birch, R.J.5    Cork, A.H.6    Hocart, C.H.7    Arioli, T.8    Williamson, R.E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.