A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development

Daniel Mariappa; Nithya Selvan; Vladimir S. Borodkin; Jana Alonso; Andrew T. Ferenbach; Claire Shepherd; Iva Hopkins Navratilova; Daan M. F. Van Aalten

doi:10.1042/BJ20150610

A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development

Daniel Mariappa, Nithya Selvan, Vladimir S. Borodkin, Jana Alonso , Andrew T. Ferenbach, Claire Shepherd, Iva Hopkins Navratilova, Daan M. F. Van Aalten (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

38 Citations (Scopus)

Abstract

O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylation and the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-Nacetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development.

Original language	English
Pages (from-to)	255-262
Number of pages	8
Journal	Biochemical Journal
Volume	470
Issue number	2
DOIs	https://doi.org/10.1042/BJ20150610
Publication status	Published - Sept 2015

Keywords

Drosophila
Embryonic development
Fluorescence polarization
O-GlcNAc probe
O-GlcNAcase (OGA)

ASJC Scopus subject areas

Biochemistry
Cell Biology
Molecular Biology

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10.1042/BJ20150610

Cite this

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title = "A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development",

abstract = "O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylation and the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-Nacetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development.",

keywords = "Drosophila, Embryonic development, Fluorescence polarization, O-GlcNAc probe, O-GlcNAcase (OGA)",

author = "Daniel Mariappa and Nithya Selvan and Borodkin, {Vladimir S.} and Jana Alonso and Ferenbach, {Andrew T.} and Claire Shepherd and Navratilova, {Iva Hopkins} and {Van Aalten}, {Daan M. F.}",

year = "2015",

month = sep,

doi = "10.1042/BJ20150610",

language = "English",

volume = "470",

pages = "255--262",

journal = "Biochemical Journal",

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T1 - A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development

AU - Mariappa, Daniel

AU - Selvan, Nithya

AU - Borodkin, Vladimir S.

AU - Alonso , Jana

AU - Ferenbach, Andrew T.

AU - Shepherd, Claire

AU - Navratilova, Iva Hopkins

AU - Van Aalten, Daan M. F.

PY - 2015/9

Y1 - 2015/9

N2 - O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylation and the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-Nacetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development.

AB - O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylation and the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-Nacetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development.

KW - Drosophila

KW - Embryonic development

KW - Fluorescence polarization

KW - O-GlcNAc probe

KW - O-GlcNAcase (OGA)

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AN - SCOPUS:84940397727

SN - 0264-6021

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JO - Biochemical Journal

JF - Biochemical Journal

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ER -

A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

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Aref#d: 21318. Molecular Mechanisms of O-GlcNAc Signalling (Senior Fellowship Renewal)

Reductionist animal models to probe protein O-GlcNAcylation

Cite this

A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Projects

Aref#d: 21318. Molecular Mechanisms of O-GlcNAc Signalling (Senior Fellowship Renewal)

Student theses

Reductionist animal models to probe protein O-GlcNAcylation

Cite this