Molecular perspectives on protein adenylylation
Standard
Molecular perspectives on protein adenylylation. / Hedberg, Christian; Itzen, Aymelt.
in: ACS CHEM BIOL, Jahrgang 10, Nr. 1, 16.01.2015, S. 12-21.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Review › Forschung
Harvard
APA
Vancouver
Bibtex
}
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 -