PXD008539

PXD008539 is an original dataset announced via ProteomeXchange.

Title	Lamin A acetylation shapes nuclear architecture and safeguards genomic integrity
Description	The nuclear lamina constitutes more than a structural scaffold for the nucleus and plays a crucial role in protection of genomic integrity. Here we report that the loss of the lysine acetyl-transferase (KAT) MOF leads to nuclear architecture defects during interphase including micronuclei formation. We identify Lamin A/C, a major component of the nuclear lamina, to be an acetylation target of MOF. A point mutation in Lamin A phenocopies nuclear morphology defects observed upon Mof-deletion. Through single cell DNA sequencing, we reveal that either loss of Mof or Lamin A mutation result in extensive genomic instability, including chromothripsis. Our work establishes MOF-dependent Lamin acetylation as a key regulator of nuclear architecture maintenance in mammals.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:13:45.203.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Witold Szymanski
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	acetylated residue; iodoacetamide derivatized residue; deamidated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-12-22 00:06:01	ID requested
1	2019-08-16 06:35:05	announced
2	2019-10-25 04:53:15	announced	2019-10-25: Updated publication reference for PubMed record(s): 31576060.
⏵ 3	2024-10-22 04:13:46	announced	2024-10-22: Updated project metadata.

Karoutas A, Szymanski W, Rausch T, Guhathakurta S, Rog-Zielinska EA, Peyronnet R, Seyfferth J, Chen HR, de Leeuw R, Herquel B, Kimura H, Mittler G, Kohl P, Medalia O, Korbel JO, Akhtar A, The NSL complex maintains nuclear architecture stability via lamin A/C acetylation. Nat Cell Biol, 21(10):1248-1260(2019) [pubmed]

10.1038/s41556-019-0397-z;

curator keyword: Biological

submitter keyword: acetylation, mouse, QExactive,LC-MSMS

Gerhard Mittler
contact affiliation	Max Planck Institute of Immunobiology and Epigenetics, Stübeweg 51, 79108 Freiburg im Breisgau
contact email	mittler@ie-freiburg.mpg.de
lab head
Witold Szymanski
contact affiliation	Max Planck Institute for Terrestrial Microbiology
contact email	szymanski@ie-freiburg.mpg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/08/PXD008539

PRIDE project URI

• PRIDE
  1. PXD008539
     1. Label: PRIDE project
     2. Name: Lamin A acetylation shapes nuclear architecture and safeguards genomic integrity