메뉴 건너뛰기




Volumn 109, Issue 30, 2012, Pages

Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a β-propeller protein family

Author keywords

Autophagy; Protein lipid interactions; X ray crystallography; Yeast

Indexed keywords

BETA PROPELLER PROTEIN THAT BIND POLYPHOSPHOINOSITIDE; LIPOSOME; MUTANT PROTEIN; PHOSPHATIDYLINOSITIDE; UNCLASSIFIED DRUG;

EID: 84864337089     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1205128109     Document Type: Article
Times cited : (138)

References (52)
  • 1
    • 77953762012 scopus 로고    scopus 로고
    • Translation of the phosphoinositide code by PI effectors
    • Kutateladze TG (2010) Translation of the phosphoinositide code by PI effectors. Nat Chem Biol 6:507-513.
    • (2010) Nat Chem Biol , vol.6 , pp. 507-513
    • Kutateladze, T.G.1
  • 3
    • 62749090535 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,5-bisphosphate and Fab1p/PIKfyve underPPIn endo-lysosome function
    • Dove SK, Dong K, Kobayashi T, Williams FK, Michell RH (2009) Phosphatidylinositol 3,5-bisphosphate and Fab1p/PIKfyve underPPIn endo-lysosome function. Biochem J 419:1-13.
    • (2009) Biochem J , vol.419 , pp. 1-13
    • Dove, S.K.1    Dong, K.2    Kobayashi, T.3    Williams, F.K.4    Michell, R.H.5
  • 4
    • 3342951135 scopus 로고    scopus 로고
    • Atg21 is a phosphoinositide binding protein required for efficient lipidation and localization of Atg8 during uptake of aminopeptidase I by selective autophagy
    • DOI 10.1091/mbc.E04-02-0147
    • Strømhaug PE, Reggiori F, Guan J, Wang CW, Klionsky DJ (2004) Atg21 is a phosphoinositide binding protein required for efficient lipidation and localization of Atg8 during uptake of aminopeptidase I by selective autophagy. Mol Biol Cell 15:3553-3566. (Pubitemid 38989696)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.8 , pp. 3553-3566
    • Stromhaug, P.E.1    Reggiori, F.2    Guan, J.3    Wang, C.-W.4    Klionsky, D.J.5
  • 5
    • 33746867157 scopus 로고    scopus 로고
    • The relevance of the phosphatidylinositolphosphat-binding motif FRRGT of Atg18 and Atg21 for the Cvt pathway and autophagy
    • DOI 10.1016/j.febslet.2006.07.041, PII S0014579306008829
    • Krick R, Tolstrup J, Appelles A, Henke S, Thumm M (2006) The relevance of the phosphatidylinositolphosphat-binding motif FRRGT of Atg18 and Atg21 for the Cvt pathway and autophagy. FEBS Lett 580:4632-4638. (Pubitemid 44189382)
    • (2006) FEBS Letters , vol.580 , Issue.19 , pp. 4632-4638
    • Krick, R.1    Tolstrup, J.2    Appelles, A.3    Henke, S.4    Thumm, M.5
  • 6
    • 2542450910 scopus 로고    scopus 로고
    • PtdIns-specific MPR pathway association of a novel WD40 repeat protein, WIPI49
    • DOI 10.1091/mbc.E03-10-0732
    • Jeffries TR, Dove SK, Michell RH, Parker PJ (2004) PtdIns-specific MPR pathway association of a novel WD40 repeat protein, WIPI49. Mol Biol Cell 15:2652-2663. (Pubitemid 38691855)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.6 , pp. 2652-2663
    • Jeffries, T.R.1    Dove, S.K.2    Michell, R.H.3    Parker, P.J.4
  • 7
    • 80051474094 scopus 로고    scopus 로고
    • The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of omegasomes to autophagosomes
    • Lu Q, et al. (2011) The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of omegasomes to autophagosomes. Dev Cell 21:343-357.
    • (2011) Dev Cell , vol.21 , pp. 343-357
    • Lu, Q.1
  • 8
    • 77951215334 scopus 로고    scopus 로고
    • Roles of the lipid-binding motifs of Atg18 and Atg21 in the cytoplasm to vacuole targeting pathway and autophagy
    • Nair U, Cao Y, Xie Z, Klionsky DJ (2010) Roles of the lipid-binding motifs of Atg18 and Atg21 in the cytoplasm to vacuole targeting pathway and autophagy. J Biol Chem 285:11476-11488.
    • (2010) J Biol Chem , vol.285 , pp. 11476-11488
    • Nair, U.1    Cao, Y.2    Xie, Z.3    Klionsky, D.J.4
  • 9
    • 53049102656 scopus 로고    scopus 로고
    • The Atg18-Atg2 complex is recruited to autophagic membranes via phosphatidylinositol 3-phosphate and exerts an essential function
    • Obara K, Sekito T, Niimi K, Ohsumi Y (2008) The Atg18-Atg2 complex is recruited to autophagic membranes via phosphatidylinositol 3-phosphate and exerts an essential function. J Biol Chem 283:23972-23980.
    • (2008) J Biol Chem , vol.283 , pp. 23972-23980
    • Obara, K.1    Sekito, T.2    Niimi, K.3    Ohsumi, Y.4
  • 10
    • 11244289333 scopus 로고    scopus 로고
    • WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy
    • DOI 10.1038/sj.onc.1208331
    • Proikas-Cezanne T, et al. (2004) WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy. Oncogene 23:9314-9325. (Pubitemid 40069664)
    • (2004) Oncogene , vol.23 , Issue.58 , pp. 9314-9325
    • Proikas-Cezanne, T.1    Waddell, S.2    Gaugel, A.3    Frickey, T.4    Lupas, A.5    Nordheim, A.6
  • 11
    • 82855170845 scopus 로고    scopus 로고
    • Resveratrol-mediated autophagy requires WIPI-1-regulated LC3 lipidation in the absence of induced phagophore formation
    • Mauthe M, et al. (2011) Resveratrol-mediated autophagy requires WIPI-1-regulated LC3 lipidation in the absence of induced phagophore formation. Autophagy 7:1448-1461.
    • (2011) Autophagy , vol.7 , pp. 1448-1461
    • Mauthe, M.1
  • 12
    • 77953726483 scopus 로고    scopus 로고
    • Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation
    • Polson HE, et al. (2010) Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation. Autophagy 6:6.
    • (2010) Autophagy , vol.6 , pp. 6
    • Polson, H.E.1
  • 13
    • 77956414236 scopus 로고    scopus 로고
    • The origin of the autophagosomal membrane
    • Tooze SA, Yoshimori T (2010) The origin of the autophagosomal membrane. Nat Cell Biol 12:831-835.
    • (2010) Nat Cell Biol , vol.12 , pp. 831-835
    • Tooze, S.A.1    Yoshimori, T.2
  • 14
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: A history of macroautophagy
    • Yang Z, Klionsky DJ (2010) Eaten alive: A history of macroautophagy. Nat Cell Biol 12:814-822.
    • (2010) Nat Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 17
    • 0035834395 scopus 로고    scopus 로고
    • Autophagy and the cytoplasm to vacuole targeting pathway both require Aut10p
    • DOI 10.1016/S0014-5793(01)03016-2, PII S0014579301030162
    • Barth H, Meiling-Wesse K, Epple UD, Thumm M (2001) Autophagy and the cytoplasm to vacuole targeting pathway both require Aut10p. FEBS Lett 508:23-28. (Pubitemid 33055660)
    • (2001) FEBS Letters , vol.508 , Issue.1 , pp. 23-28
    • Barth, H.1    Meiling-Wesse, K.2    Epple, U.D.3    Thumm, M.4
  • 19
    • 35848929068 scopus 로고    scopus 로고
    • Atg18 regulates organelle morphology and Fab1 kinase activity independent of its membrane recruitment by phosphatidylinositol 3,5-bisphosphate
    • DOI 10.1091/mbc.E07-04-0301
    • Efe JA, Botelho RJ, Emr SD (2007) Atg18 regulates organelle morphology and Fab1 kinase activity independent of its membrane recruitment by phosphatidylinositol 3,5-bisphosphate. Mol Biol Cell 18:4232-4244. (Pubitemid 350060155)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.11 , pp. 4232-4244
    • Efe, J.A.1    Botelho, R.J.2    Emr, S.D.3
  • 20
    • 58049198294 scopus 로고    scopus 로고
    • VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and mouse
    • Jin N, et al. (2008) VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and mouse. EMBO J 27:3221-3234.
    • (2008) EMBO J , vol.27 , pp. 3221-3234
    • Jin, N.1
  • 21
    • 57349198328 scopus 로고    scopus 로고
    • Piecemeal microautophagy of the nucleus requires the core macroautophagy genes
    • Krick R, et al. (2008) Piecemeal microautophagy of the nucleus requires the core macroautophagy genes. Mol Biol Cell 19:4492-4505.
    • (2008) Mol Biol Cell , vol.19 , pp. 4492-4505
    • Krick, R.1
  • 23
    • 53549091843 scopus 로고    scopus 로고
    • Dissecting the localization and function of Atg18, Atg21 and Ygr223c
    • Krick R, Henke S, Tolstrup J, Thumm M (2008) Dissecting the localization and function of Atg18, Atg21 and Ygr223c. Autophagy 4:896-910.
    • (2008) Autophagy , vol.4 , pp. 896-910
    • Krick, R.1    Henke, S.2    Tolstrup, J.3    Thumm, M.4
  • 25
    • 0035936157 scopus 로고    scopus 로고
    • Crystal structure of the tricorn protease reveals a protein disassembly line
    • DOI 10.1038/35106609
    • Brandstetter H, Kim JS, Groll M, Huber R (2001) Crystal structure of the tricorn protease reveals a protein disassembly line. Nature 414:466-470. (Pubitemid 34173730)
    • (2001) Nature , vol.414 , Issue.6862 , pp. 466-470
    • Brandstetter, H.1    Kim, J.-S.2    Groll, M.3    Huber, R.4
  • 26
    • 80053646544 scopus 로고    scopus 로고
    • Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex
    • Yoshida K, Seo HS, Debler EW, Blobel G, Hoelz A (2011) Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex. Proc Natl Acad Sci USA 108:16571-16576.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 16571-16576
    • Yoshida, K.1    Seo, H.S.2    Debler, E.W.3    Blobel, G.4    Hoelz, A.5
  • 27
    • 0030069667 scopus 로고    scopus 로고
    • G protein heterodimers: New structures propel new questions
    • DOI 10.1016/S0092-8674(00)80969-1
    • Neer EJ, Smith TF (1996) G protein heterodimers: New structures propel new questions. Cell 84:175-178. (Pubitemid 26040834)
    • (1996) Cell , vol.84 , Issue.2 , pp. 175-178
    • Neer, E.J.1    Smith, T.F.2
  • 28
    • 79960068470 scopus 로고    scopus 로고
    • Structure and function of WD40 domain proteins
    • Xu C,Min J (2011) Structure and function of WD40 domain proteins. Protein Cell 2:202-214.
    • (2011) Protein Cell , vol.2 , pp. 202-214
    • Xu, C.1    Min, J.2
  • 29
    • 0036791737 scopus 로고    scopus 로고
    • Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction
    • Karathanassis D, et al. (2002) Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction. EMBO J 21:5057-5068.
    • (2002) EMBO J , vol.21 , pp. 5057-5068
    • Karathanassis, D.1
  • 30
    • 36248988035 scopus 로고    scopus 로고
    • The PX-BAR membrane-remodeling unit of sorting nexin 9
    • DOI 10.1038/sj.emboj.7601889, PII 7601889
    • Pylypenko O, Lundmark R, Rasmuson E, Carlsson SR, Rak A (2007) The PX-BAR membrane-remodeling unit of sorting nexin 9. EMBO J 26:4788-4800. (Pubitemid 350126794)
    • (2007) EMBO Journal , vol.26 , Issue.22 , pp. 4788-4800
    • Pylypenko, O.1    Lundmark, R.2    Rasmuson, E.3    Carlsson, S.R.4    Rak, A.5
  • 31
    • 77955057137 scopus 로고    scopus 로고
    • High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA
    • Schoebel S, Blankenfeldt W, Goody RS, Itzen A (2010) High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. EMBO Rep 11:598-604.
    • (2010) EMBO Rep , vol.11 , pp. 598-604
    • Schoebel, S.1    Blankenfeldt, W.2    Goody, R.S.3    Itzen, A.4
  • 32
    • 33746288421 scopus 로고    scopus 로고
    • Determining selectivity of phosphoinositide-binding domains
    • DOI 10.1016/j.ymeth.2006.05.006, PII S1046202306000764
    • Narayan K, Lemmon MA (2006) Determining selectivity of phosphoinositide-binding domains. Methods 39:122-133. (Pubitemid 44107710)
    • (2006) Methods , vol.39 , Issue.2 , pp. 122-133
    • Narayan, K.1    Lemmon, M.A.2
  • 33
    • 0027556064 scopus 로고
    • Chemical and biochemical sensors based on interferometry at thin (multi-)layers
    • Gauglitz G, Brecht A, Kraus G, Nahm W (1993) Chemical and biochemical sensors based on interferometry at thin (multi-)layers. Sens Actuators B Chem 11:21-27.
    • (1993) Sens Actuators B Chem , vol.11 , pp. 21-27
    • Gauglitz, G.1    Brecht, A.2    Kraus, G.3    Nahm, W.4
  • 35
    • 77955915560 scopus 로고    scopus 로고
    • Quantification of nonselective bulk autophagy in S. cerevisiae using Pgk1-GFP
    • Welter E, Thumm M, Krick R (2010) Quantification of nonselective bulk autophagy in S. cerevisiae using Pgk1-GFP. Autophagy 6:794-797.
    • (2010) Autophagy , vol.6 , pp. 794-797
    • Welter, E.1    Thumm, M.2    Krick, R.3
  • 36
    • 0346503885 scopus 로고    scopus 로고
    • The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure
    • DOI 10.1016/S1534-5807(03)00402-7, PII S1534580703004027
    • Reggiori F, Tucker KA, Stromhaug PE, Klionsky DJ (2004) The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure. Dev Cell 6:79-90. (Pubitemid 38089207)
    • (2004) Developmental Cell , vol.6 , Issue.1 , pp. 79-90
    • Reggiori, F.1    Tucker, K.A.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 37
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris GM, et al. (2009) AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J Comput Chem 30:2785-2791.
    • (2009) J Comput Chem , vol.30 , pp. 2785-2791
    • Morris, G.M.1
  • 38
    • 78649853031 scopus 로고    scopus 로고
    • A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae
    • Gallego O, et al. (2010) A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol Syst Biol 6:430.
    • (2010) Mol Syst Biol , vol.6 , pp. 430
    • Gallego, O.1
  • 40
    • 0032581670 scopus 로고    scopus 로고
    • FYVE fingers bind PtdIns(3)P
    • Gaullier JM, et al. (1998) FYVE fingers bind PtdIns(3)P. Nature 394:432-433.
    • (1998) Nature , vol.394 , pp. 432-433
    • Gaullier, J.M.1
  • 41
    • 0034282751 scopus 로고    scopus 로고
    • Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
    • Gillooly DJ, et al. (2000) Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J 19:4577-4588.
    • (2000) EMBO J , vol.19 , pp. 4577-4588
    • Gillooly, D.J.1
  • 43
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • DOI 10.1038/nrm2328, PII NRM2328
    • Lemmon MA (2008) Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 9:99-111. (Pubitemid 351158910)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.2 , pp. 99-111
    • Lemmon, M.A.1
  • 46
    • 30944461203 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,5-bisphosphate: Metabolism and cellular functions
    • DOI 10.1016/j.tibs.2005.11.013, PII S0968000405003439
    • Michell RH, Heath VL, Lemmon MA, Dove SK (2006) Phosphatidylinositol 3,5-bisphosphate: Metabolism and cellular functions. Trends Biochem Sci 31:52-63. (Pubitemid 43117543)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.1 , pp. 52-63
    • Michell, R.H.1    Heath, V.L.2    Lemmon, M.A.3    Dove, S.K.4
  • 48
    • 51449111718 scopus 로고    scopus 로고
    • Molecular mechanism of membrane targeting by the GRP1 PH domain
    • He J, et al. (2008) Molecular mechanism of membrane targeting by the GRP1 PH domain. J Lipid Res 49:1807-1815.
    • (2008) J Lipid Res , vol.49 , pp. 1807-1815
    • He, J.1
  • 50
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment. J Mol Biol 302:205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 51
    • 0027764344 scopus 로고
    • Protein sequence alignments: A strategy for the hierarchical analysis of residue conservation
    • Livingstone CD, Barton GJ (1993) Protein sequence alignments: A strategy for the hierarchical analysis of residue conservation. Comput Appl Biosci 9:745-756. (Pubitemid 24016574)
    • (1993) Computer Applications in the Biosciences , vol.9 , Issue.6 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.