Cited by 5Glycosylation and Glycoproteins ResearchCellular transport and secretionGenomics and Phylogenetic Studies

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Evolution and phylogenetic distribution of endo -α-mannosidase

Open access
Sobala, Łukasz F·2023·Glycobiology

Published version of a preprint

Abstract

While glycans underlie many biological processes, such as protein folding, cell adhesion, and cell–cell recognition, deep evolution of glycosylation machinery remains an understudied topic. N-linked glycosylation is a conserved process in which mannosidases are key trimming enzymes. One of them is the glycoprotein endo-α-1,2-mannosidase which participates in the initial trimming of mannose moieties from an N-linked glycan inside the cis-Golgi. It is unique as the only endo-acting mannosidase found in this organelle. Relatively little is known about its origins and evolutionary history; so far it was reported to occur only in vertebrates. In this work, a taxon-rich bioinformatic survey to unravel the evolutionary history of this enzyme, including all major eukaryotic clades and a wide representation of animals, is presented. The endomannosidase was found to be more widely distributed in animals and other eukaryotes. The protein motif changes in context of the canonical animal enzyme were tracked. Additionally, the data show the two canonical vertebrate endomannosidase genes, MANEA and MANEAL, arose at the second round of the two vertebrate genome duplications and one more vertebrate paralog, CMANEAL, is uncovered. Finally, a framework where N-glycosylation co-evolved with complex multicellularity is described. A better understanding of the evolution of core glycosylation pathways is pivotal to understanding biology of eukaryotes in general, and the Golgi apparatus in particular. This systematic analysis of the endomannosidase evolution is one step toward this goal.

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Metadata

Authors
Sobala, Ł. F.
Affiliations
Laboratory of Glycobiology, Hirszfeld Institute of Immunology and Experimental Therapy , Weigla 12, 53-114 Wroclaw , Poland
Venue
Glycobiology
Published
2023-05-18
Volume
33
Issue
9
Pages
687-699
ISSN
  • 0959-6658 (ISSN-L)
  • 1460-2423
OpenAlex
W4377012484
Cited by
5
References
10
Citations by year
2026: 2 · 2025: 2 · 2024: 1
FWCI
0.44
Type
journal article
Language
en
Open access
Locations
  • Glycobiology (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
National Science Centre of Poland (2020/36/C/NZ8/00081)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
Keywords
N-glycosylation, cis-Golgi, whole-genome duplication, paralogs, multicellularity, eukaryotic phylogeny, Golgi apparatus
MeSH terms
Animals, Glycosylation, Golgi Apparatus, Mannosidases, Phylogeny, Polysaccharides, Vertebrates, alpha-Mannosidase, Eukaryota

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