Correction: Corrigendum: Mutations in NGLY1 cause an inherited disorder of the endoplasmic reticulum–associated degradation pathway (Genetics in Medicine (2014) 16(10) (751–758), (S1098360021031695), (10.1038/gim.2014.22));Mutations in NGLY1 cause an inherited disorder of the endoplasmic reticulum–associated degradation pathway

Genetics in Medicine

Volumn 16, Issue 10, 2014, Pages 751-758

  Enns, Gregory M ^a   Shashi, Vandana ^b   Bainbridge, Matthew ^c   Gambello, Michael J ^d   Zahir, Farah R ^e   Bast, Thomas ^f   Crimian, Rebecca ^b   Schoch, Kelly ^b   Platt, Julia ^a   Cox, Rachel ^a   Bernstein, Jonathan A ^a   Scavina, Mena ^g   Walter, Rhonda S ^g   Bibb, Audrey ^d   Jones, Melanie ^d   Hegde, Madhuri ^d   Graham, Brett H ^c   Need, Anna C ^h   Oviedo, Angelica ⁱ   Schaaf, Christian P ^c,j   Boyle, Sean ^k   Butte, Atul J ^k   Chen, Rong ^k   Clark, Michael J ^k   Haraksingh, Rajini ^k   Cowan, Tina M ^l   He, Ping ^m   Langlois, Sylvie ^e   Zoghbi, Huda Y ^c,j   Snyder, Michael ^k   Gibbs, Richard A ^c   Freeze, Hudson H ^m   Goldstein, David B ^b   more..

^a LUCILE PACKARD CHILDREN S HOSPITAL   (United States)

^b DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c BAYLOR COLLEGE OF MEDICINE   (United States)

^d EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^e UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^f Epilepsy Centre Kork   (Germany)

^g NEMOURS ALFRED I DUPONT HOSPITAL FOR CHILDREN   (United States)

^h IMPERIAL COLLEGE LONDON   (United Kingdom)

ⁱ DALHOUSIE UNIVERSITY   (Canada)

^j TEXAS CHILDREN S HOSPITAL   (United States)

^k STANFORD UNIVERSITY   (United States)

^l STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^m BURNHAM INSTITUTE   (United States)

more..

Author keywords

alacrima; choreoathetosis; liver disease; NGLY1; seizures

Indexed keywords

GLYCOPEPTIDASE;

ADOLESCENT; CASE REPORT; DEFICIENCY; DEVELOPMENTAL DISORDER; DNA SEQUENCE; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; ENZYMOLOGY; EXOME; FAMILY HEALTH; FATALITY; FEMALE; GENETICS; GENOME-WIDE ASSOCIATION STUDY; HUMAN; INFANT; MALE; MICROCEPHALY; MOTOR DYSFUNCTION; MULTIPLE MALFORMATION SYNDROME; MUSCLE HYPOTONIA; MUTATION; PATHOLOGY; PEDIGREE; PRESCHOOL CHILD; PROCEDURES; RETROSPECTIVE STUDY; SEIZURE; SIGNAL TRANSDUCTION; YOUNG ADULT;

ABNORMALITIES, MULTIPLE; ADOLESCENT; CHILD, PRESCHOOL; DEVELOPMENTAL DISABILITIES; ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION; EXOME; FAMILY HEALTH; FATAL OUTCOME; FEMALE; GENOME-WIDE ASSOCIATION STUDY; HUMANS; INFANT; MALE; MICROCEPHALY; MOVEMENT DISORDERS; MUSCLE HYPOTONIA; MUTATION; PEDIGREE; PEPTIDE-N4-(N-ACETYL-BETA-GLUCOSAMINYL) ASPARAGINE AMIDASE; RETROSPECTIVE STUDIES; SEIZURES; SEQUENCE ANALYSIS, DNA; SIGNAL TRANSDUCTION; YOUNG ADULT;

EID: 84991500706     PISSN: 10983600     EISSN: 15300366     Source Type: Journal    
DOI: 10.1038/gim.2014.61     Document Type: Erratum

References (38)

1. Takahashi, N., Demonstration of a new amidase acting on glycopeptides. 1:CAS:528:DyaE2sXks1Cmsrk%3D 10.1016/0006-291X(77)90982-2 Biochem Biophys Res Commun 76 (1977), 1194–1201.
2. Plummer, T.H. Jr, Elder, J.H., Alexander, S., Phelan, A.W., Tarentino, A.L., Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations. 1:CAS:528:DyaL2cXmt1Gmtbo%3D 6206060 J Biol Chem 259 (1984), 10700–10704.
3. Suzuki, T., Park, H., Hollingsworth, N.M., Sternglanz, R., Lennarz, W.J., PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase. 1:CAS:528:DC%2BD3cXjvFejs7g%3D 10.1083/jcb.149.5.1039 J Cell Biol 149 (2000), 1039–1052.
4. Xin, F., Wang, S., Song, L., Liang, Q., Qi, Q., Molecular identification and characterization of peptide: N-glycanase from Schizosaccharomyces pombe. 1:CAS:528:DC%2BD1cXjtVKlt7Y%3D 10.1016/j.bbrc.2008.02.017 Biochem Biophys Res Commun 368 (2008), 907–912.
5. Masahara-Negishi, Y., Hosomi, A., Della Mea, M., Serafini-Fracassini, D., Suzuki, T., A plant peptide: N-glycanase orthologue facilitates glycoprotein ER-associated degradation in yeast. 1:CAS:528:DC%2BC38XhtVymsbzO 10.1016/j.bbagen.2012.05.009 Biochim Biophys Acta 1820 (2012), 1457–1462.
6. Gosain, A., Lohia, R., Shrivastava, A., Saran, S., Identification and characterization of peptide: N-glycanase from Dictyostelium discoideum. 1:CAS:528:DC%2BC3sXht1yku70%3D 10.1186/1471-2091-13-9 BMC Biochem, 13, 2012, 9.
7. Seko, A., Kitajima, K., Inoue, Y., Inoue, S., Peptide:N-glycosidase activity found in the early embryos of Oryzias latipes (Medaka fish). The first demonstration of the occurrence of peptide:N-glycosidase in animal cells and its implication for the presence of a de-N-glycosylation system in living organisms. 1:CAS:528:DyaK3MXmt1ylu7o%3D 1718990 J Biol Chem 266 (1991), 22110–22114.
8. Suzuki, T., Seko, A., Kitajima, K., Inoue, Y., Inoue, S., Identification of peptide:N-glycanase activity in mammalian-derived cultured cells. 1:CAS:528:DyaK3sXlslenu70%3D 10.1006/bbrc.1993.1938 Biochem Biophys Res Commun 194 (1993), 1124–1130.
9. Suzuki, T., Seko, A., Kitajima, K., Inoue, Y., Inoue, S., Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells. Possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation. 1:CAS:528:DyaK2cXkslKqs74%3D 8021270 J Biol Chem 269 (1994), 17611–17618.
10. Park, H., Suzuki, T., Lennarz, W.J., Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation. 1:CAS:528:DC%2BD3MXnt1yqtr8%3D 10.1073/pnas.201393498 Proc Natl Acad Sci USA 98 (2001), 11163–11168.
11. Jarosch, E., Taxis, C., Volkwein, C., Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. 1:CAS:528:DC%2BD38XhsVKntbg%3D 10.1038/ncb746 Nat Cell Biol 4 (2002), 134–139.
12. Kato, K., Kamiya, Y., Structural views of glycoprotein-fate determination in cells. 1:CAS:528:DC%2BD2sXhtFCjsb3L 10.1093/glycob/cwm046 Glycobiology 17 (2007), 1031–1044.
13. Kamiya, Y., Satoh, T., Kato, K., Molecular and structural basis for N-glycan-dependent determination of glycoprotein fates in cells. 1:CAS:528:DC%2BC38XhvVGmsLo%3D 10.1016/j.bbagen.2011.12.017 Biochim Biophys Acta 1820 (2012), 1327–1337.
14. Kamiya, Y., Uekusa, Y., Sumiyoshi, A., NMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23. 1:CAS:528:DC%2BC38Xlt1KntLs%3D 10.1016/j.febslet.2012.03.027 FEBS Lett 586 (2012), 1141–1146.
15. Need, A.C., Shashi, V., Hitomi, Y., Clinical application of exome sequencing in undiagnosed genetic conditions. 1:CAS:528:DC%2BC38Xht1Sht7fI 10.1136/jmedgenet-2012-100819 J Med Genet 49 (2012), 353–361.
16. Tullio-Pelet, A., Salomon, R., Hadj-Rabia, S., Mutant WD-repeat protein in triple-A syndrome. 1:CAS:528:DC%2BD3cXotVWhsbo%3D 10.1038/81642 Nat Genet 26 (2000), 332–335.
17. Handschug, K., Sperling, S., Yoon, S.J., Hennig, S., Clark, A.J., Huebner, A., Triple A syndrome is caused by mutations in AAAS, a new WD-repeat protein gene. 1:CAS:528:DC%2BD3MXht1Skurw%3D 10.1093/hmg/10.3.283 Hum Mol Genet 10 (2001), 283–290.
18. Koehler, K., Malik, M., Mahmood, S., Mutations in GMPPA cause a glycosylation disorder characterized by intellectual disability and autonomic dysfunction. 1:CAS:528:DC%2BC3sXhsVCls7bM 10.1016/j.ajhg.2013.08.002 Am J Hum Genet 93 (2013), 727–734.
19. Anderson, S.L., Coli, R., Daly, I.W., Familial dysautonomia is caused by mutations of the IKAP gene. 1:CAS:528:DC%2BD3MXit1aks74%3D 10.1086/318808 Am J Hum Genet 68 (2001), 753–758.
20. Edvardson, S., Cinnamon, Y., Jalas, C., Hereditary sensory autonomic neuropathy caused by a mutation in dystonin. 1:CAS:528:DC%2BC38Xlslyiu7k%3D 10.1002/ana.23524 Ann Neurol 71 (2012), 569–572.
21. Freeze, H.H., Eklund, E.A., Ng, B.G., Patterson, M.C., Neurology of inherited glycosylation disorders. 1:CAS:528:DC%2BC38XlvFaktL8%3D 10.1016/S1474-4422(12)70040-6 Lancet Neurol 11 (2012), 453–466.
22. Freeze, H.H., Understanding human glycosylation disorders: biochemistry leads the charge. 1:CAS:528:DC%2BC3sXjslegs7k%3D 10.1074/jbc.R112.429274 J Biol Chem 288 (2013), 6936–6945.
23. Rafiq, M.A., Kuss, A.W., Puettmann, L., Mutations in the alpha 1,2-mannosidase gene, MAN1B1, cause autosomal-recessive intellectual disability. 1:CAS:528:DC%2BC3MXovF2mt7Y%3D 10.1016/j.ajhg.2011.06.006 Am J Hum Genet 89 (2011), 176–182.
24. Pan, S., Wang, S., Utama, B., Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system. 1:CAS:528:DC%2BC3MXhtVOlu7zP 10.1091/mbc.e11-02-0118 Mol Biol Cell 22 (2011), 2810–2822.
25. Pan, S., Cheng, X., Sifers, R.N., Golgi-situated endoplasmic reticulum α-1, 2-mannosidase contributes to the retrieval of ERAD substrates through a direct interaction with γ-COP. 1:CAS:528:DC%2BC3sXmtFartrg%3D 10.1091/mbc.e12-12-0886 Mol Biol Cell 24 (2013), 1111–1121.
26. Yildirim, Y., Orhan, E.K., Iseri, S.A., A frameshift mutation of ERLIN2 in recessive intellectual disability, motor dysfunction and multiple joint contractures. 1:CAS:528:DC%2BC3MXltFehs7o%3D 10.1093/hmg/ddr070 Hum Mol Genet 20 (2011), 1886–1892.
27. Pearce, M.M., Wormer, D.B., Wilkens, S., Wojcikiewicz, R.J., An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors. 1:CAS:528:DC%2BD1MXktlGktrw%3D 10.1074/jbc.M809801200 J Biol Chem 284 (2009), 10433–10445.
28. Alazami, A.M., Adly, N., Al Dhalaan, H., Alkuraya, F.S., A nullimorphic ERLIN2 mutation defines a complicated hereditary spastic paraplegia locus (SPG18). 1:CAS:528:DC%2BC3MXhsVyrsbbJ 10.1007/s10048-011-0291-8 Neurogenetics 12 (2011), 333–336.
29. Lu, J.P., Wang, Y., Sliter, D.A., Pearce, M.M., Wojcikiewicz, R.J., RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation. 1:CAS:528:DC%2BC3MXot1Gltbk%3D 10.1074/jbc.M111.251983 J Biol Chem 286 (2011), 24426–24433.
30. Valdmanis, P.N., Simões Lopes, A.A., Gros-Louis, F., Stewart, J.D., Rouleau, G.A., Dupré, N., A novel neurodegenerative disease characterised by posterior column ataxia and pyramidal tract involvement maps to chromosome 8p12-8q12.1. 1:CAS:528:DC%2BD2cXnsFCrsrw%3D 10.1136/jmg.2004.019711 J Med Genet 41 (2004), 634–639.
31. Valdmanis, P.N., Brunet, D., St-Onge, J., Weston, L., Rouleau, G.A., Dupré, N., A founder haplotype for autosomal dominant sensory ataxia in Eastern Canada. 1:STN:280:DC%2BD28jltlKgtg%3D%3D 10.1212/01.wnl.0000249314.96183.48 Neurology 67 (2006), 2239–2242.
32. Valdmanis, P.N., Dupré, N., Lachance, M., A mutation in the RNF170 gene causes autosomal dominant sensory ataxia. 10.1093/brain/awq329 Brain 134:Pt 2 (2011), 602–607.
33. Saifi, G.M., Szigeti, K., Wiszniewski, W., SIMPLE mutations in Charcot-Marie-Tooth disease and the potential role of its protein product in protein degradation. 1:CAS:528:DC%2BD2MXps1Cks70%3D 10.1002/humu.20153 Hum Mutat 25 (2005), 372–383.
34. Tanabe, K., Lennarz, W.J., Suzuki, T., A cytoplasmic peptide: N-glycanase. 1:CAS:528:DC%2BD1cXhs1OmsLg%3D 10.1016/S0076-6879(06)15004-1 Meth Enzymol 415 (2006), 46–55.
35. Suzuki, T., Park, H., Lennarz, W.J., Cytoplasmic peptide:N-glycanase (PNGase) in eukaryotic cells: occurrence, primary structure, and potential functions. 1:CAS:528:DC%2BD38XjsVChtL4%3D 10.1096/fj.01-0889rev FASEB J 16 (2002), 635–641.
36. Freeze, H.H., Aebi, M., Altered glycan structures: the molecular basis of congenital disorders of glycosylation. 1:CAS:528:DC%2BD2MXhtVKjsL%2FK 10.1016/j.sbi.2005.08.010 Curr Opin Struct Biol 15 (2005), 490–498.
37. Habibi-Babadi, N., Su, A., de Carvalho, C.E., Colavita, A., The N-glycanase png-1 acts to limit axon branching during organ formation in Caenorhabditis elegans. 1:CAS:528:DC%2BC3cXitV2jurg%3D 10.1523/JNEUROSCI.4962-08.2010 J Neurosci 30 (2010), 1766–1776.
38. Petrovski, S., Wang, Q., Heinzen, E.L., Allen, A.S., Goldstein, D.B., Genic intolerance to functional variation and the interpretation of personal genomes. 1:CAS:528:DC%2BC3sXhsVCku7rJ 10.1371/journal.pgen.1003709 PLoS Genet, 9, 2013, e1003709.