메뉴 건너뛰기




Volumn 20, Issue 3, 2009, Pages 348-355

Human XTP3-B binds to α1-antitrypsin variant nullHong Kong via the C-terminal MRH domain in a glycan-dependent manner

Author keywords

ERAD; Lectin; N glycan; Sugar binding specificity; XTP3 B

Indexed keywords

ALANINE; ALPHA 1 ANTITRYPSIN; FC RECEPTOR; GLYCAN; KREMEN2 ASSOCIATED PROTEIN; MEMBRANE PROTEIN; N ACETYL BETA GLUCOSAMINIDASE; SOMATOMEDIN B RECEPTOR; UNCLASSIFIED DRUG;

EID: 77949893248     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwp182     Document Type: Article
Times cited : (43)

References (35)
  • 1
    • 47749109897 scopus 로고    scopus 로고
    • A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: Inhibiting secretion of misfolded protein conformers and enhancing their disposal
    • Bernasconi R, Pertel T, Luban J, Molinari M. 2008. A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: Inhibiting secretion of misfolded protein conformers and enhancing their disposal. J Biol Chem. 283:16446-16454.
    • (2008) J Biol Chem , vol.283 , pp. 16446-16454
    • Bernasconi, R.1    Pertel, T.2    Luban, J.3    Molinari, M.4
  • 2
    • 24944583185 scopus 로고    scopus 로고
    • Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen
    • Bhamidipati A, Denic V, Quan EM, Weissman JS. 2005. Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. Mol Cell. 19:741-751.
    • (2005) Mol Cell , vol.19 , pp. 741-751
    • Bhamidipati, A.1    Denic, V.2    Quan, E.M.3    Weissman, J.S.4
  • 3
    • 0022976402 scopus 로고
    • The use of 1-deoxymannojirimycin to evaluate the role of various alpha-mannosidases in oligosaccharide processing in intact cells
    • Bischoff J, Liscum L, Kornfeld R. 1986. The use of 1-deoxymannojirimycin to evaluate the role of various alpha-mannosidases in oligosaccharide processing in intact cells. J Biol Chem. 261:4766-4774.
    • (1986) J Biol Chem , vol.261 , pp. 4766-4774
    • Bischoff, J.1    Liscum, L.2    Kornfeld, R.3
  • 4
    • 0018901585 scopus 로고
    • The primary glycosylation defect in class E Thy-1-negative mutant mouse lymphoma cells is an inability to synthesize dolichol-P-mannose
    • Chapman A, Fujimoto K, Kornfeld S. 1980. The primary glycosylation defect in class E Thy-1-negative mutant mouse lymphoma cells is an inability to synthesize dolichol-P-mannose. J Biol Chem. 255:4441-4446.
    • (1980) J Biol Chem , vol.255 , pp. 4441-4446
    • Chapman, A.1    Fujimoto, K.2    Kornfeld, S.3
  • 5
    • 0018581477 scopus 로고
    • Structure of the lipidlinked oligosaccharides that accumulate in class E Thy-1-negative mutant lymphomas
    • Chapman A, Trowbridge, IS, Hyman R, Kornfeld S. 1979. Structure of the lipidlinked oligosaccharides that accumulate in class E Thy-1-negative mutant lymphomas. Cell. 17:503-508.
    • (1979) Cell , vol.17 , pp. 503-508
    • Chapman, A.1    Trowbridge, I.S.2    Hyman, R.3    Kornfeld, S.4
  • 6
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 delivermutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson JC, Shaler TA, Tyler RE, Kopito RR. 2008. OS-9 and GRP94 delivermutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol. 10:272-282.
    • (2008) Nat Cell Biol , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 7
    • 59849119398 scopus 로고    scopus 로고
    • Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
    • Clerc S, Hirsch C, Oggier DM, Deprez P, Jakob C, Sommer T, Aebi M. 2009. Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol. 184:159-172.
    • (2009) J Cell Biol , vol.184 , pp. 159-172
    • Clerc, S.1    Hirsch, C.2    Oggier, D.M.3    Deprez, P.4    Jakob, C.5    Sommer, T.6    Aebi, M.7
  • 8
    • 33744965386 scopus 로고    scopus 로고
    • TheMRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions inN-glycan recognition
    • Cruciat CM, Hassler C, Niehrs C. 2006. TheMRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions inN-glycan recognition. J Biol Chem. 281:12986-12993.
    • (2006) J Biol Chem , vol.281 , pp. 12986-12993
    • Cruciat, C.M.1    Hassler, C.2    Niehrs, C.3
  • 9
    • 0036019901 scopus 로고    scopus 로고
    • The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported
    • Herscovics A, Romero PA, Tremblay LO. 2002. The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported. Glycobiology. 12:14G-15G.
    • (2002) Glycobiology , vol.12
    • Herscovics, A.1    Romero, P.A.2    Tremblay, L.O.3
  • 11
    • 67650535999 scopus 로고    scopus 로고
    • Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
    • Hosokawa N, Kamiya Y, Kamiya D, Kato K, Nagata K. 2009. Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J Biol Chem. 284:17061-17068.
    • (2009) J Biol Chem , vol.284 , pp. 17061-17068
    • Hosokawa, N.1    Kamiya, Y.2    Kamiya, D.3    Kato, K.4    Nagata, K.5
  • 13
    • 51049121849 scopus 로고    scopus 로고
    • Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
    • Hosokawa N, Wada I, Nagasawa K, Moriyama T, Okawa K, Nagata K. 2008. Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP. J Biol Chem. 283:20914-20924.
    • (2008) J Biol Chem , vol.283 , pp. 20914-20924
    • Hosokawa, N.1    Wada, I.2    Nagasawa, K.3    Moriyama, T.4    Okawa, K.5    Nagata, K.6
  • 14
    • 24944552879 scopus 로고    scopus 로고
    • Yos9p detects and targets misfolded glycoproteins for ER-associated degradation
    • Kim W, Spear ED, Ng DT. 2005. Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell. 19:753-764.
    • (2005) Mol Cell , vol.19 , pp. 753-764
    • Kim, W.1    Spear, E.D.2    Ng, D.T.3
  • 15
    • 0018601092 scopus 로고
    • Class E Thy-1 negative mouse lymphoma cells utilize an alternate pathway of oligosaccharide processing to synthesize complex-type oligosacchrides
    • Kornfeld S, Gregory W, Chapman A. 1979. Class E Thy-1 negative mouse lymphoma cells utilize an alternate pathway of oligosaccharide processing to synthesize complex-type oligosacchrides. J Biol Chem. 254:11649-11654.
    • (1979) J Biol Chem , vol.254 , pp. 11649-11654
    • Kornfeld, S.1    Gregory, W.2    Chapman, A.3
  • 16
    • 0030898233 scopus 로고    scopus 로고
    • Intracellular disposal of incompletely folded human alpha1-antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharides
    • Liu Y, Choudhury P, Cabral CM, Sifers RN. 1997. Intracellular disposal of incompletely folded human alpha1-antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharides. J Biol Chem. 272:7946-7951.
    • (1997) J Biol Chem , vol.272 , pp. 7946-7951
    • Liu, Y.1    Choudhury, P.2    Cabral, C.M.3    Sifers, R.N.4
  • 17
    • 0033605219 scopus 로고    scopus 로고
    • Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
    • Liu Y, Choudhury P, Cabral CM, Sifers RN. 1999. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. J Biol Chem. 274:5861-5867.
    • (1999) J Biol Chem , vol.274 , pp. 5861-5867
    • Liu, Y.1    Choudhury, P.2    Cabral, C.M.3    Sifers, R.N.4
  • 18
    • 20444393746 scopus 로고    scopus 로고
    • Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins
    • Mast SW, Diekman K, Karaveg K, Davis A, Sifers RN, Moremen KW. 2005. Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins. Glycobiology. 15:421-436.
    • (2005) Glycobiology , vol.15 , pp. 421-436
    • Mast, S.W.1    Diekman, K.2    Karaveg, K.3    Davis, A.4    Sifers, R.N.5    Moremen, K.W.6
  • 20
    • 0035838410 scopus 로고    scopus 로고
    • The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins
    • Munro S. 2001. The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins. Curr Biol. 11:R499-501.
    • (2001) Curr Biol , vol.11
    • Munro, S.1
  • 21
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y, Hosokawa N, Wada I, Nagata K. 2003. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science. 299:1394- 1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 22
    • 0033569876 scopus 로고    scopus 로고
    • Structural basis for recognition of phosphorylated high mannose oligosaccharides by the cationdependent mannose 6-phosphate receptor
    • Olson LJ, Zhang J, Lee YC, Dahms NM, Kim JJ. 1999. Structural basis for recognition of phosphorylated high mannose oligosaccharides by the cationdependent mannose 6-phosphate receptor. J. Biol. Chem. 274:29889-29896.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29889-29896
    • Olson, L.J.1    Zhang, J.2    Lee, Y.C.3    Dahms, N.M.4    Kim, J.J.5
  • 23
    • 33751002037 scopus 로고    scopus 로고
    • Lectin-resistantCHOglycosylationmutants
    • Patnaik SK, Stanley P. 2006. Lectin-resistant CHO glycosylation mutants. Methods Enzymol. 416:159-182.
    • (2006) Methods Enzymol , vol.416 , pp. 159-182
    • Patnaik, S.K.1    Stanley, P.2
  • 25
    • 24944446266 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation
    • Romisch K. 2005. Endoplasmic reticulum-associated degradation. Annu Rev Cell Dev Biol. 21:435-456.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 435-456
    • Romisch, K.1
  • 26
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • RonD,Walter P. 2007. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol. 8:519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 27
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M, Kaufman RJ. 2005. The mammalian unfolded protein response. Annu Rev Biochem. 74:739-789.
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 28
    • 0023907965 scopus 로고
    • A frameshift mutation results in a truncated alpha 1-antitrypsin that is retained within the rough endoplasmic reticulum
    • Sifers RN, Brashears-Macatee S, Kidd VJ, Muensch H, Woo SL. 1988. A frameshift mutation results in a truncated alpha 1-antitrypsin that is retained within the rough endoplasmic reticulum. J Biol Chem. 263:7330-7335.
    • (1988) J Biol Chem , vol.263 , pp. 7330-7335
    • Sifers, R.N.1    Brashears-Macatee, S.2    Kidd, V.J.3    Muensch, H.4    Woo, S.L.5
  • 29
    • 24944478240 scopus 로고    scopus 로고
    • Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD
    • Szathmary R, Bielmann R, Nita-Lazar M, Burda P, Jakob CA. 2005. Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell. 19:765-775.
    • (2005) Mol Cell , vol.19 , pp. 765-775
    • Szathmary, R.1    Bielmann, R.2    Nita-Lazar, M.3    Burda, P.4    Jakob, C.A.5
  • 30
    • 0018597869 scopus 로고
    • Abnormal lipid-linked oligosaccharides in class E Thy-1-negative mutant lymphoms
    • Trowbridge IS,Hyman R. 1979. Abnormal lipid-linked oligosaccharides in class E Thy-1-negative mutant lymphoms. Cell. 17:503-508.
    • (1979) Cell , vol.17 , pp. 503-508
    • Trowbridge, I.S.1    Hyman, R.2
  • 31
    • 0020469388 scopus 로고
    • Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of Golgi mannosidase II
    • Tulsiani DR, Harris TM, Touster O. 1982. Swainsonine inhibits the biosynthesis of complex glycoproteins by inhibition of Golgi mannosidase II. J Biol Chem. 257:7936-7939.
    • (1982) J Biol Chem , vol.257 , pp. 7936-7939
    • Tulsiani, D.R.1    Harris, T.M.2    Touster, O.3
  • 32
    • 0025334881 scopus 로고
    • Swainsonine induces the production of hybrid glycoproteins and accumulation of oligosaccharides in male reproductive tissues of the rat
    • Tulsiani DR, Skudlarek MD, Orgebin-Crist MC. 1990. Swainsonine induces the production of hybrid glycoproteins and accumulation of oligosaccharides in male reproductive tissues of the rat. Biol Reprod. 43:130-138.
    • (1990) Biol Reprod , vol.43 , pp. 130-138
    • Tulsiani, D.R.1    Skudlarek, M.D.2    Orgebin-Crist, M.C.3
  • 33
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulumassociated degradation
    • Vembar SS, Brodsky JL. 2008. One step at a time: Endoplasmic reticulumassociated degradation. Nat Rev Mol Cell Biol. 9:944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 34
    • 0027331577 scopus 로고
    • Demonstration that a kifunensine-resistant alphamannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells
    • Weng S, Spiro RG. 1993. Demonstration that a kifunensine-resistant alphamannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells. J Biol Chem. 268:25656-25663.
    • (1993) J Biol Chem , vol.268 , pp. 25656-25663
    • Weng, S.1    Spiro, R.G.2
  • 35
    • 9944224190 scopus 로고    scopus 로고
    • Measurement of the carbohydrate-binding specificity of lectins by a multiplexed beadbased flow cytometric assay
    • Yamamoto K, Ito S, Yasukawa F, Konami Y, Matsumoto N. 2005. Measurement of the carbohydrate-binding specificity of lectins by a multiplexed beadbased flow cytometric assay. Anal Biochem. 336:28-38.
    • (2005) Anal Biochem , vol.336 , pp. 28-38
    • Yamamoto, K.1    Ito, S.2    Yasukawa, F.3    Konami, Y.4    Matsumoto, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.