메뉴 건너뛰기




Volumn 322, Issue 3, 2004, Pages 957-965

ADRP is dissociated from lipid droplets by ARF1-dependent mechanism

Author keywords

ADRP; ARF1; Brefeldin A; Lipid droplet; Yeast two hybrid

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ADIPOCYTE DIFFENTIATION RELATED PROTEIN; BREFELDIN A; FAT DROPLET; GLUTATHIONE TRANSFERASE; GUANOSINE DIPHOSPHATE; PROTEIN; UNCLASSIFIED DRUG;

EID: 4444266442     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.010     Document Type: Article
Times cited : (36)

References (44)
  • 1
    • 0032911957 scopus 로고    scopus 로고
    • Mechanisms of lipid-body formation
    • D.J. Murphy, and J. Vance Mechanisms of lipid-body formation Trends Biochem. Sci. 24 1999 109 115
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 109-115
    • Murphy, D.J.1    Vance, J.2
  • 2
    • 0037113954 scopus 로고    scopus 로고
    • The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition
    • K. Tauchi-Sato, S. Ozeki, T. Houjou, R. Taguchi, and T. Fujimoto The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition J. Biol. Chem. 277 2002 44507 44512
    • (2002) J. Biol. Chem. , vol.277 , pp. 44507-44512
    • Tauchi-Sato, K.1    Ozeki, S.2    Houjou, T.3    Taguchi, R.4    Fujimoto, T.5
  • 3
    • 0035809923 scopus 로고    scopus 로고
    • Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets
    • A.G. Ostermeyer, J.M. Paci, Y. Zeng, D.M. Lublin, S. Munro, and D.A. Brown Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets J. Cell Biol. 152 2001 1071 1078
    • (2001) J. Cell Biol. , vol.152 , pp. 1071-1078
    • Ostermeyer, A.G.1    Paci, J.M.2    Zeng, Y.3    Lublin, D.M.4    Munro, S.5    Brown, D.A.6
  • 4
    • 0035809931 scopus 로고    scopus 로고
    • Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell
    • T. Fujimoto, H. Kogo, K. Ishiguro, K. Tauchi, and R. Nomura Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell J. Cell Biol. 152 2001 1079 1085
    • (2001) J. Cell Biol. , vol.152 , pp. 1079-1085
    • Fujimoto, T.1    Kogo, H.2    Ishiguro, K.3    Tauchi, K.4    Nomura, R.5
  • 5
    • 0035809933 scopus 로고    scopus 로고
    • A caveolin dominant negative mutant associates with lipid bodies and induces intracellular cholesterol imbalance
    • A. Pol, R. Luetterforst, M. Lindsay, S. Heino, E. Ikonen, and R.G. Parton A caveolin dominant negative mutant associates with lipid bodies and induces intracellular cholesterol imbalance J. Cell Biol. 152 2001 1057 1070
    • (2001) J. Cell Biol. , vol.152 , pp. 1057-1070
    • Pol, A.1    Luetterforst, R.2    Lindsay, M.3    Heino, S.4    Ikonen, E.5    Parton, R.G.6
  • 6
    • 0346099345 scopus 로고    scopus 로고
    • Dynamic and regulated association of caveolin with lipid bodies: Modulation of lipid body motility and function by a dominant negative mutant
    • A. Pol, S. Martin, M.A. Fernandez, C. Ferguson, A. Carozzi, R. Luetterforst, C. Enrich, and R.G. Parton Dynamic and regulated association of caveolin with lipid bodies: modulation of lipid body motility and function by a dominant negative mutant Mol. Biol. Cell 15 2004 99 110
    • (2004) Mol. Biol. Cell , vol.15 , pp. 99-110
    • Pol, A.1    Martin, S.2    Fernandez, M.A.3    Ferguson, C.4    Carozzi, A.5    Luetterforst, R.6    Enrich, C.7    Parton, R.G.8
  • 7
    • 0031889388 scopus 로고    scopus 로고
    • Co-compartmentalization of MAP kinases and cytosolic phospholipase A2 at cytoplasmic arachidonate-rich lipid bodies
    • W. Yu, P.T. Bozza, D.M. Tzizik, J.P. Gray, J. Cassara, A.M. Dvorak, and P.F. Weller Co-compartmentalization of MAP kinases and cytosolic phospholipase A2 at cytoplasmic arachidonate-rich lipid bodies Am. J. Pathol. 152 1998 759 769
    • (1998) Am. J. Pathol. , vol.152 , pp. 759-769
    • Yu, W.1    Bozza, P.T.2    Tzizik, D.M.3    Gray, J.P.4    Cassara, J.5    Dvorak, A.M.6    Weller, P.F.7
  • 8
    • 0030930401 scopus 로고    scopus 로고
    • Eosinophil lipid bodies: Specific, inducible intracellular sites for enhanced eicosanoid formation
    • P.T. Bozza, W. Yu, J.F. Penrose, E.S. Morgan, A.M. Dvorak, and P.F. Weller Eosinophil lipid bodies: specific, inducible intracellular sites for enhanced eicosanoid formation J. Exp. Med. 186 1997 909 920
    • (1997) J. Exp. Med. , vol.186 , pp. 909-920
    • Bozza, P.T.1    Yu, W.2    Penrose, J.F.3    Morgan, E.S.4    Dvorak, A.M.5    Weller, P.F.6
  • 9
    • 0141814912 scopus 로고    scopus 로고
    • Localization of mammalian NAD(P)H steroid dehydrogenase-like protein on lipid droplets
    • M. Ohashi, N. Mizushima, Y. Kabeya, and T. Yoshimori Localization of mammalian NAD(P)H steroid dehydrogenase-like protein on lipid droplets J. Biol. Chem. 278 2003 36819 36829
    • (2003) J. Biol. Chem. , vol.278 , pp. 36819-36829
    • Ohashi, M.1    Mizushima, N.2    Kabeya, Y.3    Yoshimori, T.4
  • 10
    • 0037015277 scopus 로고    scopus 로고
    • Targeting of Nir2 to lipid droplets is regulated by a specific threonine residue within its PI-transfer domain
    • V. Litvak, Y.D. Shaul, M. Shulewitz, R. Amarilio, S. Carmon, and S. Lev Targeting of Nir2 to lipid droplets is regulated by a specific threonine residue within its PI-transfer domain Curr. Biol. 12 2002 1513 1518
    • (2002) Curr. Biol. , vol.12 , pp. 1513-1518
    • Litvak, V.1    Shaul, Y.D.2    Shulewitz, M.3    Amarilio, R.4    Carmon, S.5    Lev, S.6
  • 11
    • 0037924355 scopus 로고    scopus 로고
    • Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: Roles in endoplasmic reticulum lipid compartmentalization and export
    • T. Hayashi, and T.P. Su Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: roles in endoplasmic reticulum lipid compartmentalization and export J. Pharmacol. Exp. Ther. 306 2003 718 725
    • (2003) J. Pharmacol. Exp. Ther. , vol.306 , pp. 718-725
    • Hayashi, T.1    Su, T.P.2
  • 12
    • 0037155197 scopus 로고    scopus 로고
    • Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein
    • N.B. Cole, D.D. Murphy, T. Grider, S. Rueter, D. Brasaemle, and R.L. Nussbaum Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein J. Biol. Chem. 277 2002 6344 6352
    • (2002) J. Biol. Chem. , vol.277 , pp. 6344-6352
    • Cole, N.B.1    Murphy, D.D.2    Grider, T.3    Rueter, S.4    Brasaemle, D.5    Nussbaum, R.L.6
  • 13
    • 0037200026 scopus 로고    scopus 로고
    • Functional conservation for lipid storage droplet association among perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium
    • S. Miura, J.W. Gan, J. Brzostowski, M.J. Parisi, C.J. Schultz, C. Londos, B. Oliver, and A.R. Kimmel Functional conservation for lipid storage droplet association among perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium J. Biol. Chem. 277 2002 32253 32257
    • (2002) J. Biol. Chem. , vol.277 , pp. 32253-32257
    • Miura, S.1    Gan, J.W.2    Brzostowski, J.3    Parisi, M.J.4    Schultz, C.J.5    Londos, C.6    Oliver, B.7    Kimmel, A.R.8
  • 14
    • 0037477829 scopus 로고    scopus 로고
    • Perilipin a is essential for the translocation of hormone-sensitive lipase during lipolytic activation
    • C. Sztalryd, G. Xu, H. Dorward, J.T. Tansey, J.A. Contreras, A.R. Kimmel, and C. Londos Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation J. Cell Biol. 161 2003 1093 1103
    • (2003) J. Cell Biol. , vol.161 , pp. 1093-1103
    • Sztalryd, C.1    Xu, G.2    Dorward, H.3    Tansey, J.T.4    Contreras, J.A.5    Kimmel, A.R.6    Londos, C.7
  • 15
    • 0347065339 scopus 로고    scopus 로고
    • Lipase-selective functional domains of perilipin a differentially regulate constitutive and protein kinase A-stimulated lipolysis
    • H.H. Zhang, S.C. Souza, K.V. Muliro, F.B. Kraemer, M.S. Obin, and A.S. Greenberg Lipase-selective functional domains of perilipin A differentially regulate constitutive and protein kinase A-stimulated lipolysis J. Biol. Chem. 278 2003 51535 51542
    • (2003) J. Biol. Chem. , vol.278 , pp. 51535-51542
    • Zhang, H.H.1    Souza, S.C.2    Muliro, K.V.3    Kraemer, F.B.4    Obin, M.S.5    Greenberg, A.S.6
  • 18
    • 0033546310 scopus 로고    scopus 로고
    • Adipose differentiation related protein (ADRP) expressed in transfected COS-7 cells selectively stimulates long chain fatty acid uptake
    • J. Gao, and G. Serrero Adipose differentiation related protein (ADRP) expressed in transfected COS-7 cells selectively stimulates long chain fatty acid uptake J. Biol. Chem. 274 1999 16825 16830
    • (1999) J. Biol. Chem. , vol.274 , pp. 16825-16830
    • Gao, J.1    Serrero, G.2
  • 20
    • 0026677375 scopus 로고
    • Brefeldin a inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • J.G. Donaldson, D. Finazzi, and R.D. Klausner Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein Nature 360 1992 350 352
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 21
    • 0030903768 scopus 로고    scopus 로고
    • Post-translational regulation of perilipin expression. Stabilization by stored intracellular neutral lipids
    • D.L. Brasaemle, T. Barber, A.R. Kimmel, and C. Londos Post-translational regulation of perilipin expression. Stabilization by stored intracellular neutral lipids J. Biol. Chem. 272 1997 9378 9387
    • (1997) J. Biol. Chem. , vol.272 , pp. 9378-9387
    • Brasaemle, D.L.1    Barber, T.2    Kimmel, A.R.3    Londos, C.4
  • 22
    • 0035933883 scopus 로고    scopus 로고
    • Involvement of ADP-ribosylation factor 1 in cholera toxin-induced morphological changes of Chinese hamster ovary cells
    • N. Morinaga, Y. Kaihou, N. Vitale, J. Moss, and M. Noda Involvement of ADP-ribosylation factor 1 in cholera toxin-induced morphological changes of Chinese hamster ovary cells J. Biol. Chem. 276 2001 22838 22843
    • (2001) J. Biol. Chem. , vol.276 , pp. 22838-22843
    • Morinaga, N.1    Kaihou, Y.2    Vitale, N.3    Moss, J.4    Noda, M.5
  • 23
    • 0026708135 scopus 로고
    • The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport
    • R.A. Kahn, P. Randazzo, T. Serafini, O. Weiss, C. Rulka, J. Clark, M. Amherdt, P. Roller, L. Orci, and J.E. Rothman The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport J. Biol. Chem. 267 1992 13039 13046
    • (1992) J. Biol. Chem. , vol.267 , pp. 13039-13046
    • Kahn, R.A.1    Randazzo, P.2    Serafini, T.3    Weiss, O.4    Rulka, C.5    Clark, J.6    Amherdt, M.7    Roller, P.8    Orci, L.9    Rothman, J.E.10
  • 26
    • 0027937942 scopus 로고
    • Factors underlying the variability of lipid droplet fluorescence in MA-10 Leydig tumor cells
    • P.M. Gocze, and D.A. Freeman Factors underlying the variability of lipid droplet fluorescence in MA-10 Leydig tumor cells Cytometry 17 1994 151 158
    • (1994) Cytometry , vol.17 , pp. 151-158
    • Gocze, P.M.1    Freeman, D.A.2
  • 27
    • 0033071156 scopus 로고    scopus 로고
    • Perilipins, ADRP, and other proteins that associate with intracellular neutral lipid droplets in animal cells
    • C. Londos, D.L. Brasaemle, C.J. Schultz, J.P. Segrest, and A.R. Kimmel Perilipins, ADRP, and other proteins that associate with intracellular neutral lipid droplets in animal cells Semin. Cell Dev. Biol. 10 1999 51 58
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 51-58
    • Londos, C.1    Brasaemle, D.L.2    Schultz, C.J.3    Segrest, J.P.4    Kimmel, A.R.5
  • 28
    • 0038546739 scopus 로고    scopus 로고
    • Adipose differentiation-related protein has two independent domains for targeting to lipid droplets
    • N. Nakamura, and T. Fujimoto Adipose differentiation-related protein has two independent domains for targeting to lipid droplets Biochem. Biophys. Res. Commun. 306 2003 333 338
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 333-338
    • Nakamura, N.1    Fujimoto, T.2
  • 31
    • 0026713293 scopus 로고
    • The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins
    • R. Regazzi, A. Kikuchi, Y. Takai, and C.B. Wollheim The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins J. Biol. Chem. 267 1992 17512 17519
    • (1992) J. Biol. Chem. , vol.267 , pp. 17512-17519
    • Regazzi, R.1    Kikuchi, A.2    Takai, Y.3    Wollheim, C.B.4
  • 32
    • 0346725004 scopus 로고    scopus 로고
    • Arf GAPs: Multifunctional proteins that regulate membrane traffic and actin remodelling
    • P.A. Randazzo, and D.S. Hirsch Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling Cell. Signal. 16 2004 401 413
    • (2004) Cell. Signal. , vol.16 , pp. 401-413
    • Randazzo, P.A.1    Hirsch, D.S.2
  • 34
    • 0037903214 scopus 로고    scopus 로고
    • Live cell analysis and targeting of the lipid droplet-binding adipocyte differentiation-related protein
    • P. Targett-Adams, D. Chambers, S. Gledhill, R.G. Hope, J.F. Coy, A. Girod, and J. McLauchlan Live cell analysis and targeting of the lipid droplet-binding adipocyte differentiation-related protein J. Biol. Chem. 278 2003 15998 16007
    • (2003) J. Biol. Chem. , vol.278 , pp. 15998-16007
    • Targett-Adams, P.1    Chambers, D.2    Gledhill, S.3    Hope, R.G.4    Coy, J.F.5    Girod, A.6    McLauchlan, J.7
  • 36
    • 0037414820 scopus 로고    scopus 로고
    • The central domain is required to target and anchor perilipin a to lipid droplets
    • A. Garcia, A. Sekowski, V. Subramanian, and D.L. Brasaemle The central domain is required to target and anchor perilipin A to lipid droplets J. Biol. Chem. 278 2003 625 635
    • (2003) J. Biol. Chem. , vol.278 , pp. 625-635
    • Garcia, A.1    Sekowski, A.2    Subramanian, V.3    Brasaemle, D.L.4
  • 37
    • 0030469694 scopus 로고    scopus 로고
    • Adipocyte differentiation-related protein is secreted into milk as a constituent of milk lipid globule membrane
    • H.W. Heid, M. Schnolzer, and T.W. Keenan Adipocyte differentiation- related protein is secreted into milk as a constituent of milk lipid globule membrane Biochem. J. 320 Pt. 3 1996 1025 1030
    • (1996) Biochem. J. , vol.320 , Issue.3 , pp. 1025-1030
    • Heid, H.W.1    Schnolzer, M.2    Keenan, T.W.3
  • 39
    • 0033832729 scopus 로고    scopus 로고
    • Intracellular distribution and mobilization of unesterified cholesterol in adipocytes: Triglyceride droplets are surrounded by cholesterol-rich ER-like surface layer structures
    • S. Prattes, G. Horl, A. Hammer, A. Blaschitz, W.F. Graier, W. Sattler, R. Zechner, and E. Steyrer Intracellular distribution and mobilization of unesterified cholesterol in adipocytes: triglyceride droplets are surrounded by cholesterol-rich ER-like surface layer structures J. Cell Sci. 113 Pt 17 2000 2977 2989
    • (2000) J. Cell Sci. , vol.113 , Issue.17 , pp. 2977-2989
    • Prattes, S.1    Horl, G.2    Hammer, A.3    Blaschitz, A.4    Graier, W.F.5    Sattler, W.6    Zechner, R.7    Steyrer, E.8
  • 40
    • 0034903123 scopus 로고    scopus 로고
    • The biogenesis and functions of lipid bodies in animals, plants and microorganisms
    • D.J. Murphy The biogenesis and functions of lipid bodies in animals, plants and microorganisms Prog. Lipid Res. 40 2001 325 438
    • (2001) Prog. Lipid Res. , vol.40 , pp. 325-438
    • Murphy, D.J.1
  • 41
    • 0038711498 scopus 로고    scopus 로고
    • A phospholipase D-dependent process forms lipid droplets containing caveolin, adipocyte differentiation-related protein, and vimentin in a cell-free system
    • D. Marchesan, M. Rutberg, L. Andersson, L. Asp, T. Larsson, J. Boren, B.R. Johansson, and S.O. Olofsson A phospholipase D-dependent process forms lipid droplets containing caveolin, adipocyte differentiation-related protein, and vimentin in a cell-free system J. Biol. Chem. 278 2003 27293 27300
    • (2003) J. Biol. Chem. , vol.278 , pp. 27293-27300
    • Marchesan, D.1    Rutberg, M.2    Andersson, L.3    Asp, L.4    Larsson, T.5    Boren, J.6    Johansson, B.R.7    Olofsson, S.O.8
  • 42
    • 0942287191 scopus 로고    scopus 로고
    • Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic
    • P. Liu, Y. Ying, Y. Zhao, D.I. Mundy, M. Zhu, and R.G. Anderson Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic J. Biol. Chem. 279 2004 3787 3792
    • (2004) J. Biol. Chem. , vol.279 , pp. 3787-3792
    • Liu, P.1    Ying, Y.2    Zhao, Y.3    Mundy, D.I.4    Zhu, M.5    Anderson, R.G.6
  • 43


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.