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Molecular perspectives on protein adenylylation

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Molecular perspectives on protein adenylylation. / Hedberg, Christian; Itzen, Aymelt.

In: ACS CHEM BIOL, Vol. 10, No. 1, 16.01.2015, p. 12-21.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Hedberg, C & Itzen, A 2015, 'Molecular perspectives on protein adenylylation', ACS CHEM BIOL, vol. 10, no. 1, pp. 12-21. https://doi.org/10.1021/cb500854e

APA

Hedberg, C., & Itzen, A. (2015). Molecular perspectives on protein adenylylation. ACS CHEM BIOL, 10(1), 12-21. https://doi.org/10.1021/cb500854e

Vancouver

Hedberg C, Itzen A. Molecular perspectives on protein adenylylation. ACS CHEM BIOL. 2015 Jan 16;10(1):12-21. https://doi.org/10.1021/cb500854e

Bibtex

@article{0a02ba8b789f4cb8b290d908701da90c,
title = "Molecular perspectives on protein adenylylation",
abstract = "In the cell, proteins are frequently modified covalently at specific amino acids with post-translational modifications, leading to a diversification of protein functions and activities. Since the introduction of high-resolution mass spectrometry, new post-translational modifications are constantly being discovered. One particular modification is the adenylylation of mammalian proteins. In adenylylation, adenosine triphosphate (ATP) is utilized to attach an adenosine monophosphate at protein threonine or tyrosine residues via a phosphodiester linkage. Adenylylation is particularly interesting in the context of infections by bacterial pathogens during which mammalian proteins are manipulated through AMP attachment via secreted bacterial factors. In this review, we summarize the role and regulation of enzymatic adenylylation and the mechanisms of catalysis. We also refer to recent methods for the detection of adenylylated proteins by modification-specific antibodies, ATP analogues equipped with chemical handles, and mass spectrometry approaches. Additionally, we review screening approaches for inhibiting adenylylation and briefly discuss related modifications such as phosphocholination and phosphorylation. ",
keywords = "Adenosine Monophosphate, Adenosine Triphosphate, Animals, Bacteria, Bacterial Infections, Enzymes, Humans, Mass Spectrometry, Models, Molecular, Protein Conformation, Protein Processing, Post-Translational, Threonine, Tyrosine, Journal Article, Research Support, Non-U.S. Gov't, Review",
author = "Christian Hedberg and Aymelt Itzen",
year = "2015",
month = jan,
day = "16",
doi = "10.1021/cb500854e",
language = "English",
volume = "10",
pages = "12--21",
journal = "ACS CHEM BIOL",
issn = "1554-8929",
publisher = "American Chemical Society",
number = "1",

}

RIS

TY - JOUR

T1 - Molecular perspectives on protein adenylylation

AU - Hedberg, Christian

AU - Itzen, Aymelt

PY - 2015/1/16

Y1 - 2015/1/16

N2 - In the cell, proteins are frequently modified covalently at specific amino acids with post-translational modifications, leading to a diversification of protein functions and activities. Since the introduction of high-resolution mass spectrometry, new post-translational modifications are constantly being discovered. One particular modification is the adenylylation of mammalian proteins. In adenylylation, adenosine triphosphate (ATP) is utilized to attach an adenosine monophosphate at protein threonine or tyrosine residues via a phosphodiester linkage. Adenylylation is particularly interesting in the context of infections by bacterial pathogens during which mammalian proteins are manipulated through AMP attachment via secreted bacterial factors. In this review, we summarize the role and regulation of enzymatic adenylylation and the mechanisms of catalysis. We also refer to recent methods for the detection of adenylylated proteins by modification-specific antibodies, ATP analogues equipped with chemical handles, and mass spectrometry approaches. Additionally, we review screening approaches for inhibiting adenylylation and briefly discuss related modifications such as phosphocholination and phosphorylation.

AB - In the cell, proteins are frequently modified covalently at specific amino acids with post-translational modifications, leading to a diversification of protein functions and activities. Since the introduction of high-resolution mass spectrometry, new post-translational modifications are constantly being discovered. One particular modification is the adenylylation of mammalian proteins. In adenylylation, adenosine triphosphate (ATP) is utilized to attach an adenosine monophosphate at protein threonine or tyrosine residues via a phosphodiester linkage. Adenylylation is particularly interesting in the context of infections by bacterial pathogens during which mammalian proteins are manipulated through AMP attachment via secreted bacterial factors. In this review, we summarize the role and regulation of enzymatic adenylylation and the mechanisms of catalysis. We also refer to recent methods for the detection of adenylylated proteins by modification-specific antibodies, ATP analogues equipped with chemical handles, and mass spectrometry approaches. Additionally, we review screening approaches for inhibiting adenylylation and briefly discuss related modifications such as phosphocholination and phosphorylation.

KW - Adenosine Monophosphate

KW - Adenosine Triphosphate

KW - Animals

KW - Bacteria

KW - Bacterial Infections

KW - Enzymes

KW - Humans

KW - Mass Spectrometry

KW - Models, Molecular

KW - Protein Conformation

KW - Protein Processing, Post-Translational

KW - Threonine

KW - Tyrosine

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

KW - Review

U2 - 10.1021/cb500854e

DO - 10.1021/cb500854e

M3 - SCORING: Review article

C2 - 25486069

VL - 10

SP - 12

EP - 21

JO - ACS CHEM BIOL

JF - ACS CHEM BIOL

SN - 1554-8929

IS - 1

ER -