Proteomics

Dataset Information

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Kansl2 dependent acetylome study in primary Kansl2 (fl/fl) murine embryonic fibroblasts

ABSTRACT: As one of the most important post-translational protein modifications, lysine acetylation is catalyzed by lysine acetyltransferases (KATs), which catalyze the covalent attachment of an acetyl group to the N epsilon–residue of lysine. The histone acetyltransferase MOF, which represents the main histone H4 lysine-16 specific acetyltransferase, is the KAT subunit of two mutually exclusive multiprotein complexes in metazoa, namely the MSL (male-specific lethal) and the NSL (non-specific lethal) complex. Depletion of both, MOF and the NSL complex subunit Kansl2 result in selective changes of the cellular acetylome. As a consequence, modulation of nuclear lamin lysine acetylations correlate with profound changes in nuclear morphology, like micronuclei formation.

INSTRUMENT(S): Q Exactive Plus, Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture, Fibroblast

SUBMITTER: Gerhard Mittler  

LAB HEAD: Gerhard Mittler

PROVIDER: PXD038521 | Pride | 2023-01-05

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
Acetyl__K_Sites.txt Txt
evidence.txt Txt
experimentalDesignTemplate.txt Txt
parameters.txt Txt
peptides.txt Txt
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Publications

While nuclear lamina abnormalities are hallmarks of human diseases, their interplay with epigenetic regulators and precise epigenetic landscape remain poorly understood. Here, we show that loss of the lysine acetyltransferase MOF or its associated NSL-complex members KANSL2 or KANSL3 leads to a stochastic accumulation of nuclear abnormalities with genomic instability patterns including chromothripsis. SILAC-based MOF and KANSL2 acetylomes identified lamin A/C as an acetylation target of MOF. HDA  ...[more]

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