Stimulation of ERAD of misfolded null Hong Kong α1-antitrypsin by Golgi α1,2-mannosidases

作者: Nobuko Hosokawa , Zhipeng You , Linda O. Tremblay , Kazuhiro Nagata , Annette Herscovics

DOI: 10.1016/J.BBRC.2007.08.057

关键词: Endoplasmic reticulumCell biologyMannoseCytoplasmMannosidaseMannosidasesBiologyProtein degradationGolgi apparatusBiochemistryEndoplasmic-reticulum-associated protein degradation

摘要: Terminally misfolded or unassembled proteins are degraded by the cytoplasmic ubiquitin-proteasome pathway in a process known as ERAD (endoplasmic reticulum-associated protein degradation). Overexpression of ER alpha1,2-mannosidase I and EDEMs target glycoproteins for ERAD, most likely due to trimming N-glycans. Here we demonstrate that overexpression Golgi IA, IB, IC also accelerates terminally human alpha1-antitrypsin variant null (Hong Kong) (NHK), mannose from N-glycans on NHK 293 cells. Although transfected is primarily localized ER, some co-localizes with markers, suggesting alpha1,2-mannosidases can contribute degradation.

参考文章(44)
A. Herscovics, J. Schneikert, A. Athanassiadis, K.W. Moremen, Isolation of a mouse Golgi mannosidase cDNA, a member of a gene family conserved from yeast to mammals. Journal of Biological Chemistry. ,vol. 269, pp. 9864- 9871 ,(1994) , 10.1016/S0021-9258(17)36963-6
Peter Arvan, Xiang Zhao, Jose Ramos-Castaneda, Amy Chang, Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems. Traffic. ,vol. 3, pp. 771- 780 ,(2002) , 10.1034/J.1600-0854.2002.31102.X
Christopher M Cabral, Yan Liu, Richard N Sifers, Dissecting glycoprotein quality control in the secretory pathway Trends in Biochemical Sciences. ,vol. 26, pp. 619- 624 ,(2001) , 10.1016/S0968-0004(01)01942-9
Zehavit Frenkel, Walter Gregory, Stuart Kornfeld, Gerardo Z. Lederkremer, Endoplasmic Reticulum-associated Degradation of Mammalian Glycoproteins Involves Sugar Chain Trimming to Man6–5GlcNAc2 Journal of Biological Chemistry. ,vol. 278, pp. 34119- 34124 ,(2003) , 10.1074/JBC.M305929200
Shilpa Vashist, Davis T.W. Ng, Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control Journal of Cell Biology. ,vol. 165, pp. 41- 52 ,(2004) , 10.1083/JCB.200309132
Yan Liu, Priya Choudhury, Christopher M. Cabral, Richard N. Sifers, Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. Journal of Biological Chemistry. ,vol. 274, pp. 5861- 5867 ,(1999) , 10.1074/JBC.274.9.5861
Roberta Mancini, Markus Aebi, Ari Helenius, Multiple Endoplasmic Reticulum-associated Pathways Degrade Mutant Yeast Carboxypeptidase Y in Mammalian Cells Journal of Biological Chemistry. ,vol. 278, pp. 46895- 46905 ,(2003) , 10.1074/JBC.M302979200
Francois Foulquier, Sandrine Duvet, Andre Klein, Anne-Marie Mir, Frederic Chirat, Rene Cacan, Endoplasmic reticulum-associated degradation of glycoproteins bearing Man5GlcNAc2 and Man9GlcNAc2 species in the MI8-5 CHO cell line. FEBS Journal. ,vol. 271, pp. 398- 404 ,(2004) , 10.1046/J.1432-1033.2003.03938.X
Nobuko Hosokawa, Linda O. Tremblay, Zhipeng You, Annette Herscovics, Ikuo Wada, Kazuhiro Nagata, Enhancement of Endoplasmic Reticulum (ER) Degradation of Misfolded Null Hong Kong α1-Antitrypsin by Human ER Mannosidase I Journal of Biological Chemistry. ,vol. 278, pp. 26287- 26294 ,(2003) , 10.1074/JBC.M303395200