Multiple distinct O-Mannosylation pathways in eukaryotes

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Multiple distinct O-Mannosylation pathways in eukaryotes. / Larsen, Ida Signe Bohse; Narimatsu, Yoshiki; Clausen, Henrik; Joshi, Hiren J; Halim, Adnan.

In: Current Opinion in Structural Biology, Vol. 56, 2019, p. 171-178.

Research output: Contribution to journalReviewResearchpeer-review

Harvard

Larsen, ISB, Narimatsu, Y, Clausen, H, Joshi, HJ & Halim, A 2019, 'Multiple distinct O-Mannosylation pathways in eukaryotes', Current Opinion in Structural Biology, vol. 56, pp. 171-178. https://doi.org/10.1016/j.sbi.2019.03.003

APA

Larsen, I. S. B., Narimatsu, Y., Clausen, H., Joshi, H. J., & Halim, A. (2019). Multiple distinct O-Mannosylation pathways in eukaryotes. Current Opinion in Structural Biology, 56, 171-178. https://doi.org/10.1016/j.sbi.2019.03.003

Vancouver

Larsen ISB, Narimatsu Y, Clausen H, Joshi HJ, Halim A. Multiple distinct O-Mannosylation pathways in eukaryotes. Current Opinion in Structural Biology. 2019;56:171-178. https://doi.org/10.1016/j.sbi.2019.03.003

Author

Larsen, Ida Signe Bohse ; Narimatsu, Yoshiki ; Clausen, Henrik ; Joshi, Hiren J ; Halim, Adnan. / Multiple distinct O-Mannosylation pathways in eukaryotes. In: Current Opinion in Structural Biology. 2019 ; Vol. 56. pp. 171-178.

Bibtex

@article{7731f7b1242b42aebef64c4746eadc9b,
title = "Multiple distinct O-Mannosylation pathways in eukaryotes",
abstract = "Protein O-mannosylation (O-Man), originally discovered in yeast five decades ago, is an important post-translational modification (PTM) conserved from bacteria to humans, but not found in plants or nematodes. Until recently, the homologous family of ER-located protein O-mannosyl transferases (PMT1-7 in yeast; POMT1/POMT2 in humans), were the only known enzymes involved in directing O-Man biosynthesis in eukaryotes. However, recent studies demonstrate the existence of multiple distinct O-Man glycosylation pathways indicating that the genetic and biosynthetic regulation of O-Man in eukaryotes is more complex than previously envisioned. Introduction of sensitive glycoproteomics strategies provided an expansion of O-Man glycoproteomes in eukaryotes (yeast and mammalian cell lines) leading to the discovery of O-Man glycosylation on important mammalian cell adhesion (cadherin superfamily) and signaling (plexin family) macromolecules, and to the discovery of unique nucleocytoplasmic O-Man glycosylation in yeast. It is now evident that eukaryotes have multiple distinct O-Man glycosylation pathways including: i) the classical PMT1-7 and POMT1/POMT2 pathway conserved in all eukaryotes apart from plants; ii) a yet uncharacterized nucleocytoplasmic pathway only found in yeast; iii) an ER-located pathway directed by the TMTC1-4 genes found in metazoans and protists and primarily dedicated to the cadherin superfamily; and iv) a yet uncharacterized pathway found in metazoans primarily dedicated to plexins. O-Man glycosylation is thus emerging as a much more widespread and evolutionary diverse PTM with complex genetic and biosynthetic regulation. While deficiencies in the POMT1/POMT2 O-Man pathway underlie muscular dystrophies, the TMTC1-4 pathway appear to be involved in distinct congenital disorders with neurodevelopmental phenotypes. Here, we review and discuss the recent discoveries of the new non-classical O-Man glycosylation pathways, their substrates, functions and roles in disease.",
author = "Larsen, {Ida Signe Bohse} and Yoshiki Narimatsu and Henrik Clausen and Joshi, {Hiren J} and Adnan Halim",
note = "Copyright {\textcopyright} 2019 Elsevier Ltd. All rights reserved.",
year = "2019",
doi = "10.1016/j.sbi.2019.03.003",
language = "English",
volume = "56",
pages = "171--178",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier Ltd. * Current Opinion Journals",

}

RIS

TY - JOUR

T1 - Multiple distinct O-Mannosylation pathways in eukaryotes

AU - Larsen, Ida Signe Bohse

AU - Narimatsu, Yoshiki

AU - Clausen, Henrik

AU - Joshi, Hiren J

AU - Halim, Adnan

N1 - Copyright © 2019 Elsevier Ltd. All rights reserved.

PY - 2019

Y1 - 2019

N2 - Protein O-mannosylation (O-Man), originally discovered in yeast five decades ago, is an important post-translational modification (PTM) conserved from bacteria to humans, but not found in plants or nematodes. Until recently, the homologous family of ER-located protein O-mannosyl transferases (PMT1-7 in yeast; POMT1/POMT2 in humans), were the only known enzymes involved in directing O-Man biosynthesis in eukaryotes. However, recent studies demonstrate the existence of multiple distinct O-Man glycosylation pathways indicating that the genetic and biosynthetic regulation of O-Man in eukaryotes is more complex than previously envisioned. Introduction of sensitive glycoproteomics strategies provided an expansion of O-Man glycoproteomes in eukaryotes (yeast and mammalian cell lines) leading to the discovery of O-Man glycosylation on important mammalian cell adhesion (cadherin superfamily) and signaling (plexin family) macromolecules, and to the discovery of unique nucleocytoplasmic O-Man glycosylation in yeast. It is now evident that eukaryotes have multiple distinct O-Man glycosylation pathways including: i) the classical PMT1-7 and POMT1/POMT2 pathway conserved in all eukaryotes apart from plants; ii) a yet uncharacterized nucleocytoplasmic pathway only found in yeast; iii) an ER-located pathway directed by the TMTC1-4 genes found in metazoans and protists and primarily dedicated to the cadherin superfamily; and iv) a yet uncharacterized pathway found in metazoans primarily dedicated to plexins. O-Man glycosylation is thus emerging as a much more widespread and evolutionary diverse PTM with complex genetic and biosynthetic regulation. While deficiencies in the POMT1/POMT2 O-Man pathway underlie muscular dystrophies, the TMTC1-4 pathway appear to be involved in distinct congenital disorders with neurodevelopmental phenotypes. Here, we review and discuss the recent discoveries of the new non-classical O-Man glycosylation pathways, their substrates, functions and roles in disease.

AB - Protein O-mannosylation (O-Man), originally discovered in yeast five decades ago, is an important post-translational modification (PTM) conserved from bacteria to humans, but not found in plants or nematodes. Until recently, the homologous family of ER-located protein O-mannosyl transferases (PMT1-7 in yeast; POMT1/POMT2 in humans), were the only known enzymes involved in directing O-Man biosynthesis in eukaryotes. However, recent studies demonstrate the existence of multiple distinct O-Man glycosylation pathways indicating that the genetic and biosynthetic regulation of O-Man in eukaryotes is more complex than previously envisioned. Introduction of sensitive glycoproteomics strategies provided an expansion of O-Man glycoproteomes in eukaryotes (yeast and mammalian cell lines) leading to the discovery of O-Man glycosylation on important mammalian cell adhesion (cadherin superfamily) and signaling (plexin family) macromolecules, and to the discovery of unique nucleocytoplasmic O-Man glycosylation in yeast. It is now evident that eukaryotes have multiple distinct O-Man glycosylation pathways including: i) the classical PMT1-7 and POMT1/POMT2 pathway conserved in all eukaryotes apart from plants; ii) a yet uncharacterized nucleocytoplasmic pathway only found in yeast; iii) an ER-located pathway directed by the TMTC1-4 genes found in metazoans and protists and primarily dedicated to the cadherin superfamily; and iv) a yet uncharacterized pathway found in metazoans primarily dedicated to plexins. O-Man glycosylation is thus emerging as a much more widespread and evolutionary diverse PTM with complex genetic and biosynthetic regulation. While deficiencies in the POMT1/POMT2 O-Man pathway underlie muscular dystrophies, the TMTC1-4 pathway appear to be involved in distinct congenital disorders with neurodevelopmental phenotypes. Here, we review and discuss the recent discoveries of the new non-classical O-Man glycosylation pathways, their substrates, functions and roles in disease.

U2 - 10.1016/j.sbi.2019.03.003

DO - 10.1016/j.sbi.2019.03.003

M3 - Review

C2 - 30999272

VL - 56

SP - 171

EP - 178

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

ER -

ID: 228732988