The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Malectin: A Novel Carbohydrate-binding Protein of the Endoplasmic Reticulum and a Candidate Player in the Early Steps of Protein N -Glycosylation
Open accessAbstract
N-Glycosylation starts in the endoplasmic reticulum (ER) where a 14-sugar glycan composed of three glucoses, nine mannoses, and two N-acetylglucosamines (Glc 3 Man 9 GlcNAc 2 ) is transferred to nascent proteins. The glucoses are sequentially trimmed by ER-resident glucosidases. The Glc 3 Man 9 GlcNAc 2 moiety is the substrate for oligosaccharyltransferase; the Glc 1 Man 9 GlcNAc 2 and Man 9 GlcNAc 2 intermediates are signals for glycoprotein folding and quality control in the calnexin/calreticulin cycle. Here, we report a novel membrane-anchored ER protein that is highly conserved in animals and that recognizes the Glc 2 -N-glycan. Structure determination by nuclear magnetic resonance showed that its luminal part is a carbohydrate binding domain that recognizes glucose oligomers. Carbohydrate microarray analyses revealed a uniquely selective binding to a Glc 2 -N-glycan probe. The localization, structure, and binding specificity of this protein, which we have named malectin, open the way to studies of its role in the genesis, processing and secretion of N-glycosylated proteins.
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Cites
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
Roles of N-Linked Glycans in the Endoplasmic Reticulum
Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037
Cited by
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
Protein quality control in the ER: The recognition of misfolded proteins
Määttänen, P., Gehring, K., Bergeron, J. J. M., & Thomas, D. Y. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.006 · Cited by 284
Solís, D., Bovin, N. V., Davis, A. P., Jiménez-Barbero, J., Romero, A., Roy, R., Smetana, K., & Gabius, H.-J. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.03.016 · Cited by 222
Protein Quality Control in the Endoplasmic Reticulum
Adams, B. M., Oster, M. E., & Hebert, D. N. (2019) · The Protein Journal · doi:10.1007/s10930-019-09831-w · Cited by 142
Gutiérrez, T., & Simmen, T. (2018) · Cell Calcium · doi:10.1016/j.ceca.2017.05.015 · Cited by 104
Phylogenetic Analysis of the Kinesin Superfamily from Physcomitrella
Shen, Z., Collatos, A. R., Bibeau, J. P., Furt, F., & Vidali, L. (2012) · Frontiers in Plant Science · doi:10.3389/fpls.2012.00230 · Cited by 60
“…has been identified in malectins, which are conserved proteins of the endoplasmic reticulum in animals and involved in protein N -glycosylation (Schallus et al., 2008), as well as in plasma membrane-located leucin-rich repeat receptor kinases such as FERONIA in Arabidopsis, where it is thought…”
BackgroundOlson, L. J., Orsi, R., Alculumbre, S. G., Peterson, F. C., Stigliano, I. D., Parodi, A. J., D'Alessio, C., & Dahms, N. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.450239 · Cited by 24
Differential expansion and retention patterns of LRR‐RLK genes across plant evolution
Kileeg, Z., Haldar, A., Khan, H., Qamar, A., & Mott, G. A. (2023) · Plant Direct · doi:10.1002/pld3.556 · Cited by 13
Metadata
- Authors
- Schallus, T., Jaeckh, C., Fehér, K., Palma, A. S., Liu, Y., Simpson, J. C., Mackeen, M., Stier, G., Gibson, T. J., Feizi, T., Pieler, T., & Muhle-Goll, C.
- Venue
- Molecular Biology of the Cell
- Published
- 2008-08
- Volume
- 19
- Issue
- 8
- Pages
- 3404-3414
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2122255481
- Cited by
- 287
- References
- 2
- FWCI
- 4.71
- Type
- journal article
- Language
- en
- Open access
- green
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