Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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.

In: Cell Reports, Vol. 2, No. 2, 30.08.2012, p. 419-431.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Lundby, A, Hansen, KL, Weinert, BT, Breinholt Bekker-Jensen, D, Secher, A, Skovgaard, T, Kelstrup, C, Dmytriyev, A, Choudhary, CR, Lundby, C & Olsen, JV 2012, 'Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns', Cell Reports, vol. 2, no. 2, pp. 419-431. https://doi.org/10.1016/j.celrep.2012.07.006

APA

Lundby, A., Hansen, K. L., Weinert, B. T., Breinholt Bekker-Jensen, D., Secher, A., Skovgaard, T., Kelstrup, C., Dmytriyev, A., Choudhary, C. R., Lundby, C., & Olsen, J. V. (2012). Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Cell Reports, 2(2), 419-431. https://doi.org/10.1016/j.celrep.2012.07.006

Vancouver

Lundby A, Hansen KL, Weinert BT, Breinholt Bekker-Jensen D, Secher A, Skovgaard T et al. Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Cell Reports. 2012 Aug 30;2(2):419-431. https://doi.org/10.1016/j.celrep.2012.07.006

Author

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. / Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. In: Cell Reports. 2012 ; Vol. 2, No. 2. pp. 419-431.

Bibtex

@article{7f7dca4c000b4fb19f5f5da3586e4fd9,

title = "Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns",

abstract = "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.",

keywords = "Faculty of Health and Medical Sciences",

author = "Alicia Lundby and Hansen, {Kasper Lage} and Weinert, {Brian Tate} and {Breinholt Bekker-Jensen}, Dorte and Anna Secher and Tine Skovgaard and Christian Kelstrup and Anatoliy Dmytriyev and Choudhary, {Chuna Ram} and Carsten Lundby and Olsen, {Jesper Velgaard}",

year = "2012",

month = aug,

day = "30",

doi = "10.1016/j.celrep.2012.07.006",

language = "English",

volume = "2",

pages = "419--431",

journal = "Cell Reports",

issn = "2211-1247",

publisher = "Cell Press",

number = "2",

}

RIS

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

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

Department of Public Health