메뉴 건너뛰기




Volumn 288, Issue 28, 2013, Pages 20499-20509

Structural characterization of carbohydrate binding by LMAN1 protein provides new insight into the endoplasmic reticulum export of factors V (FV) and VIII (FVIII)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AND RELEASE; CARBOHYDRATE BINDING; CARBOHYDRATE-RECOGNITION DOMAINS; COAGULATION FACTOR; ENDOPLASMIC RETICULUM; SECRETORY PATHWAYS; SOLVED CRYSTAL STRUCTURES; STRUCTURAL CHARACTERIZATION;

EID: 84880070996     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.461434     Document Type: Article
Times cited : (41)

References (49)
  • 1
    • 0037683407 scopus 로고    scopus 로고
    • Signals for COPII-dependent export from the ER: What's the ticket out?
    • Barlowe, C. (2003) Signals for COPII-dependent export from the ER: what's the ticket out? Trends Cell Biol. 13, 295-300
    • (2003) Trends Cell Biol. , vol.13 , pp. 295-300
    • Barlowe, C.1
  • 2
    • 78650035575 scopus 로고    scopus 로고
    • Receptor-mediated ER export of human MHC class I molecules is regulated by the C-terminal single amino acid
    • Cho, S., Ryoo, J., Jun, Y., and Ahn, K. (2011) Receptor-mediated ER export of human MHC class I molecules is regulated by the C-terminal single amino acid. Traffic. 12, 42-55
    • (2011) Traffic. , vol.12 , pp. 42-55
    • Cho, S.1    Ryoo, J.2    Jun, Y.3    Ahn, K.4
  • 3
    • 34247579058 scopus 로고    scopus 로고
    • The Transport Signal on Sec22 for Packaging into COPII-Coated Vesicles Is a Conformational Epitope
    • DOI 10.1016/j.molcel.2007.03.017, PII S1097276507001876
    • Mancias, J. D., and Goldberg, J. (2007) The transport signal on Sec22 for packaging into COPII-coated vesicles is a conformational epitope. Mol. Cell 26, 403-414 (Pubitemid 46687095)
    • (2007) Molecular Cell , vol.26 , Issue.3 , pp. 403-414
    • Mancias, J.D.1    Goldberg, J.2
  • 5
    • 21844438479 scopus 로고    scopus 로고
    • LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway
    • DOI 10.1074/jbc.M502160200
    • Zhang, B., Kaufman, R. J., and Ginsburg, D. (2005) LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway. J. Biol. Chem. 280, 25881-25886 (Pubitemid 40962299)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.27 , pp. 25881-25886
    • Zhang, B.1    Kaufman, R.J.2    Ginsburg, D.3
  • 6
    • 0033202958 scopus 로고    scopus 로고
    • The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
    • Appenzeller, C., Andersson, H., Kappeler, F., and Hauri, H. P. (1999) The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nat. Cell Biol. 1, 330-334 (Pubitemid 129493573)
    • (1999) Nature Cell Biology , vol.1 , Issue.6 , pp. 330-334
    • Appenzeller, C.1    Andersson, H.2    Kappeler, F.3    Hauri, H.-P.4
  • 7
    • 0032572579 scopus 로고    scopus 로고
    • Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of hela cells impairs the secretion of a lysosomal enzyme
    • DOI 10.1083/jcb.142.2.377
    • Vollenweider, F., Kappeler, F., Itin, C., and Hauri, H. P. (1998) Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme. J. Cell Biol. 142, 377-389 (Pubitemid 28361546)
    • (1998) Journal of Cell Biology , vol.142 , Issue.2 , pp. 377-389
    • Vollenweider, F.1    Kappeler, F.2    Itin, C.3    Hauri, H.-P.4
  • 10
    • 27744508476 scopus 로고    scopus 로고
    • Oligomerization and interacellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds
    • DOI 10.1016/j.jmb.2005.09.077, PII S0022283605011812
    • Neve, E. P., Lahtinen, U., and Pettersson, R. F. (2005) Oligomerization and interacellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds. J. Mol. Biol. 354, 556-568 (Pubitemid 41628275)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.3 , pp. 556-568
    • Neve, E.P.A.1    Lahtinen, U.2    Pettersson, R.F.3
  • 12
    • 78650436274 scopus 로고    scopus 로고
    • Molecular basis of LMAN1 in coordinating LMAN1-MCFD2 cargo receptor formation and ER-to-Golgi transport of FV/FVIII
    • Zheng, C., Liu, H. H., Yuan, S., Zhou, J., and Zhang, B. (2010) Molecular basis of LMAN1 in coordinating LMAN1-MCFD2 cargo receptor formation and ER-to-Golgi transport of FV/FVIII. Blood 116, 5698-6706
    • (2010) Blood , vol.116 , pp. 5698-6706
    • Zheng, C.1    Liu, H.H.2    Yuan, S.3    Zhou, J.4    Zhang, B.5
  • 14
    • 0344873595 scopus 로고    scopus 로고
    • The Crystal Structure of the Carbohydrate-recognition Domain of the Glycoprotein Sorting Receptor p58/ERGIC-53 Reveals an Unpredicted Metal-binding Site and Conformational Changes Associated with Calcium Ion Binding
    • DOI 10.1016/j.jmb.2003.10.031
    • Velloso, L. M., Svensson, K., Pettersson, R. F., and Lindqvist, Y. (2003) The crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding. J. Mol. Biol. 334, 845-851 (Pubitemid 37485674)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.5 , pp. 845-851
    • Velloso, L.M.1    Svensson, K.2    Pettersson, R.F.3    Lindqvist, Y.4
  • 16
    • 33749510461 scopus 로고    scopus 로고
    • Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex
    • DOI 10.1111/j.1600-0854.2006.00483.x
    • Nyfeler, B., Zhang, B., Ginsburg, D., Kaufman, R. J., and Hauri, H. P. (2006) Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex. Traffic 7, 1473-1481 (Pubitemid 44524520)
    • (2006) Traffic , vol.7 , Issue.11 , pp. 1473-1481
    • Nyfeler, B.1    Zhang, B.2    Ginsburg, D.3    Kaufman, R.J.4    Hauri, H.-P.5
  • 17
    • 48449089504 scopus 로고    scopus 로고
    • New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2
    • Guy, J. E., Wigren, E., Svärd, M., Härd, T., and Lindqvist, Y. (2008) New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. J. Mol. Biol. 381, 941-955
    • (2008) J. Mol. Biol. , vol.381 , pp. 941-955
    • Guy, J.E.1    Wigren, E.2    Svärd, M.3    Härd, T.4    Lindqvist, Y.5
  • 18
    • 77649229333 scopus 로고    scopus 로고
    • EF hand domains of MCFD2 mediate interactions with both LMAN1 and coagulation factor V or VIII
    • Zheng, C., Liu, H. H., Zhou, J., and Zhang, B. (2010) EF hand domains of MCFD2 mediate interactions with both LMAN1 and coagulation factor V or VIII. Blood 115, 1081-1087
    • (2010) Blood , vol.115 , pp. 1081-1087
    • Zheng, C.1    Liu, H.H.2    Zhou, J.3    Zhang, B.4
  • 20
    • 76749118043 scopus 로고    scopus 로고
    • Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII
    • Wigren, E., Bourhis, J. M., Kursula, I., Guy, J. E., and Lindqvist, Y. (2010) Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII. FEBS Lett. 584, 878-882
    • (2010) FEBS Lett. , vol.584 , pp. 878-882
    • Wigren, E.1    Bourhis, J.M.2    Kursula, I.3    Guy, J.E.4    Lindqvist, Y.5
  • 21
    • 39649119621 scopus 로고    scopus 로고
    • The pH of the secretory pathway: Measurement, determinants, and regulation
    • Paroutis, P., Touret, N., and Grinstein, S. (2004) The pH of the secretory pathway: measurement, determinants, and regulation. Physiology 19, 207-215 (Pubitemid 39481936)
    • (2004) Physiology , Issue.4 , pp. 207-215
    • Paroutis, P.1    Touret, N.2    Grinstein, S.3
  • 23
    • 74649086808 scopus 로고    scopus 로고
    • The unique kinetics of iron release from transferrin: The role of receptor, lobe-lobe interactions, and salt at endosomal pH
    • Byrne, S. L., Chasteen, N. D., Steere, A. N., and Mason, A. B. (2010) The unique kinetics of iron release from transferrin: the role of receptor, lobe-lobe interactions, and salt at endosomal pH. J. Mol. Biol. 396, 130-140
    • (2010) J. Mol. Biol. , vol.396 , pp. 130-140
    • Byrne, S.L.1    Chasteen, N.D.2    Steere, A.N.3    Mason, A.B.4
  • 24
    • 0037147281 scopus 로고    scopus 로고
    • Structure of the LDL receptor extracellular domain at endosomal pH
    • DOI 10.1126/science.1078124
    • Rudenko, G., Henry, L., Henderson, K., Ichtchenko, K., Brown, M. S., Goldstein, J. L., and Deisenhofer, J. (2002) Structure of the LDL receptor extracellular domain at endosomal pH. Science 298, 2353-2358 (Pubitemid 36014201)
    • (2002) Science , vol.298 , Issue.5602 , pp. 2353-2358
    • Rudenko, G.1    Henry, L.2    Henderson, K.3    Ichtchenko, K.4    Brown, M.S.5    Goldstein, J.L.6    Deisenhofer, J.7
  • 25
    • 44349171796 scopus 로고    scopus 로고
    • Structural insights into the mechanism of pH-dependent ligand binding and release by the cation-dependent mannose 6-phosphate receptor
    • Olson, L. J., Hindsgaul, O., Dahms, N. M., and Kim, J. J. (2008) Structural insights into the mechanism of pH-dependent ligand binding and release by the cation-dependent mannose 6-phosphate receptor. J. Biol. Chem. 283, 10124-10134
    • (2008) J. Biol. Chem. , vol.283 , pp. 10124-10134
    • Olson, L.J.1    Hindsgaul, O.2    Dahms, N.M.3    Kim, J.J.4
  • 26
    • 1842529346 scopus 로고    scopus 로고
    • pH-induced Conversion of the Transport Lectin ERGIC-53 Triggers Glycoprotein Release
    • DOI 10.1074/jbc.M313245200
    • Appenzeller-Herzog, C., Roche, A. C., Nufer, O., and Hauri, H. P. (2004) pH-induced conversion of the transport lectin ERGIC-53 triggers glycoprotein release. J. Biol. Chem. 279, 12943-12950 (Pubitemid 38445869)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12943-12950
    • Appenzeller-Herzog, C.1    Roche, A.-C.2    Nufer, O.3    Hauri, H.-P.4
  • 27
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J. W. (1999) The finer things in X-ray diffraction data collection. Acta Crystallogr. D Biol. Crystallogr. 55, 1718-1725
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 30
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A. J. (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D. Biol. Crystallogr. 63, 32-41
    • (2007) Acta Crystallogr. D. Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 32
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution and density modification
    • Terwilliger, T. C. (2003) SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374, 22-37
    • (2003) Methods Enzymol. , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 35
    • 0037013292 scopus 로고    scopus 로고
    • Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum
    • DOI 10.1074/jbc.M112098200
    • Velloso, L. M., Svensson, K., Schneider, G., Pettersson, R. F., and Lindqvist, Y. (2002) Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum. J. Biol. Chem. 277, 15979-15984 (Pubitemid 34967880)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15979-15984
    • Velloso, L.M.1    Svensson, K.2    Schneider, G.3    Pettersson, R.F.4    Lindqvist, Y.5
  • 37
    • 38349136210 scopus 로고    scopus 로고
    • Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36
    • Kamiya, Y., Kamiya, D., Yamamoto, K., Nyfeler, B., Hauri, H. P., and Kato, K. (2008) Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36. J. Biol. Chem. 283, 1857-1861
    • (2008) J. Biol. Chem. , vol.283 , pp. 1857-1861
    • Kamiya, Y.1    Kamiya, D.2    Yamamoto, K.3    Nyfeler, B.4    Hauri, H.P.5    Kato, K.6
  • 38
    • 77958122966 scopus 로고    scopus 로고
    • Role of the lectin VIP36 in post-ER quality control of human α1-antitrypsin
    • Reiterer, V., Nyfeler, B., and Hauri, H. P. (2010) Role of the lectin VIP36 in post-ER quality control of human α1-antitrypsin. Traffic. 11, 1044-1055
    • (2010) Traffic. , vol.11 , pp. 1044-1055
    • Reiterer, V.1    Nyfeler, B.2    Hauri, H.P.3
  • 39
    • 77949450563 scopus 로고    scopus 로고
    • Vesicular calcium regulates coat retention, fusogenicity, and size of pre-Golgi intermediates
    • Bentley, M., Nycz, D. C., Joglekar, A., Fertschai, I., Malli, R., Graier, W. F., and Hay, J. C. (2010) Vesicular calcium regulates coat retention, fusogenicity, and size of pre-Golgi intermediates. Mol. Biol. Cell 21, 1033-1046
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1033-1046
    • Bentley, M.1    Nycz, D.C.2    Joglekar, A.3    Fertschai, I.4    Malli, R.5    Graier, W.F.6    Hay, J.C.7
  • 40
    • 0242550980 scopus 로고    scopus 로고
    • ER export of ERGIC-53 is controlled by cooperation of targeting determinants in all three of its domains
    • DOI 10.1242/jcs.00759
    • Nufer, O., Kappeler, F., Guldbrandsen, S., and Hauri, H. P. (2003) ER export of ERGIC-53 is controlled by cooperation of targeting determinants in all three of its domains. J. Cell Sci. 116, 4429-4440 (Pubitemid 37369598)
    • (2003) Journal of Cell Science , vol.116 , Issue.21 , pp. 4429-4440
    • Nufer, O.1    Kappeler, F.2    Guldbrandsen, S.3    Hauri, H.-P.4
  • 41
    • 2442505584 scopus 로고    scopus 로고
    • Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation
    • Spiro, R. G. (2004) Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation. Cell Mol. Life Sci. 61, 1025-1041
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 1025-1041
    • Spiro, R.G.1
  • 44
    • 0032530396 scopus 로고    scopus 로고
    • + store, with functional properties distinct from those of the endoplasmic reticulum
    • + store, with functional properties distinct from those of the endoplasmic reticulum. EMBO J. 17, 5298-5308
    • (1998) EMBO J. , vol.17 , pp. 5298-5308
    • Pinton, P.1    Pozzan, T.2    Rizzuto, R.3
  • 46
    • 11244273061 scopus 로고    scopus 로고
    • Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment
    • DOI 10.1083/jcb.200408135
    • Xu, D., and Hay, J. C. (2004) Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment. J. Cell Biol. 167, 997-1003 (Pubitemid 40066615)
    • (2004) Journal of Cell Biology , vol.167 , Issue.6 , pp. 997-1003
    • Xu, D.1    Hay, J.C.2
  • 47
    • 0030982434 scopus 로고    scopus 로고
    • High-resolution calcium mapping of the endoplasmic reticulum-Golgi- exocytic membrane system Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells
    • Pezzati, R., Bossi, M., Podini, P., Meldolesi, J., and Grohovaz, F. (1997) High-resolution calcium mapping of the endoplasmic reticulum-Golgi- exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells. Mol. Biol. Cell 8, 1501-1512 (Pubitemid 27385572)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.8 , pp. 1501-1512
    • Pezzati, R.1    Bossi, M.2    Podini, P.3    Meldolesi, J.4    Grohovaz, F.5
  • 48
    • 41349121801 scopus 로고    scopus 로고
    • The sugar-binding ability of ERGIC-53 is enhanced by its interaction with MCFD2
    • DOI 10.1182/blood-2007-06-097022
    • Kawasaki, N., Ichikawa, Y., Matsuo, I., Totani, K., Matsumoto, N., Ito, Y., and Yamamoto, K. (2008) The sugar-binding ability of ERGIC-53 is enhanced by its interaction with MCFD2. Blood 111, 1972-1979 (Pubitemid 351451507)
    • (2008) Blood , vol.111 , Issue.4 , pp. 1972-1979
    • Kawasaki, N.1    Ichikawa, Y.2    Matsuo, I.3    Totani, K.4    Matsumoto, N.5    Ito, Y.6    Yamamoto, K.7
  • 49
    • 0345293146 scopus 로고    scopus 로고
    • On the Value of c: Can Low Affinity Systems Be Studied by Isothermal Titration Calorimetry?
    • DOI 10.1021/ja036166s
    • Turnbull, W. B., and Daranas, A. H. (2003) On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J. Am. Chem. Soc. 125, 14859-14866 (Pubitemid 37475576)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.48 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.