Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns
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Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. / Lundby, Alicia; Hansen, Kasper Lage; Weinert, Brian Tate; Breinholt Bekker-Jensen, Dorte; Secher, Anna; Skovgaard, Tine; Kelstrup, Christian; Dmytriyev, Anatoliy; Choudhary, Chuna Ram; Lundby, Carsten; Olsen, Jesper Velgaard.
I: Cell Reports, Bind 2, Nr. 2, 30.08.2012, s. 419-431.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns
AU - Lundby, Alicia
AU - Hansen, Kasper Lage
AU - Weinert, Brian Tate
AU - Breinholt Bekker-Jensen, Dorte
AU - Secher, Anna
AU - Skovgaard, Tine
AU - Kelstrup, Christian
AU - Dmytriyev, Anatoliy
AU - Choudhary, Chuna Ram
AU - Lundby, Carsten
AU - Olsen, Jesper Velgaard
N1 - Copyright © 2012 The Authors. Published by Elsevier Inc. All rights reserved.
PY - 2012/8/30
Y1 - 2012/8/30
N2 - Lysine acetylation is a major posttranslational modification involved in a broad array of physiological functions. Here, we provide an organ-wide map of lysine acetylation sites from 16 rat tissues analyzed by high-resolution tandem mass spectrometry. We quantify 15,474 modification sites on 4,541 proteins and provide the data set as a web-based database. We demonstrate that lysine acetylation displays site-specific sequence motifs that diverge between cellular compartments, with a significant fraction of nuclear sites conforming to the consensus motifs G-AcK and AcK-P. Our data set reveals that the subcellular acetylation distribution is tissue-type dependent and that acetylation targets tissue-specific pathways involved in fundamental physiological processes. We compare lysine acetylation patterns for rat as well as human skeletal muscle biopsies and demonstrate its general involvement in muscle contraction. Furthermore, we illustrate that acetylation of fructose-bisphosphate aldolase and glycerol-3-phosphate dehydrogenase serves as a cellular mechanism to switch off enzymatic activity.
AB - Lysine acetylation is a major posttranslational modification involved in a broad array of physiological functions. Here, we provide an organ-wide map of lysine acetylation sites from 16 rat tissues analyzed by high-resolution tandem mass spectrometry. We quantify 15,474 modification sites on 4,541 proteins and provide the data set as a web-based database. We demonstrate that lysine acetylation displays site-specific sequence motifs that diverge between cellular compartments, with a significant fraction of nuclear sites conforming to the consensus motifs G-AcK and AcK-P. Our data set reveals that the subcellular acetylation distribution is tissue-type dependent and that acetylation targets tissue-specific pathways involved in fundamental physiological processes. We compare lysine acetylation patterns for rat as well as human skeletal muscle biopsies and demonstrate its general involvement in muscle contraction. Furthermore, we illustrate that acetylation of fructose-bisphosphate aldolase and glycerol-3-phosphate dehydrogenase serves as a cellular mechanism to switch off enzymatic activity.
KW - Faculty of Health and Medical Sciences
U2 - 10.1016/j.celrep.2012.07.006
DO - 10.1016/j.celrep.2012.07.006
M3 - Journal article
C2 - 22902405
VL - 2
SP - 419
EP - 431
JO - Cell Reports
JF - Cell Reports
SN - 2211-1247
IS - 2
ER -
ID: 45558227