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Article

Tethering by lamin A stabilizes and targets the ING1 tumour suppressor.

Nature cell biology - 1 Nov 2008

Han Xijing, Feng Xiaolan, Rattner Jerome B, Smith Heather, Bose Pinaki, Suzuki Keiko, Soliman Mohamed A, Scott Michelle S, Burke Brian E, Riabowol Karl

Abstract excerpt

ING proteins interact with core histones through their plant homeodomains (PHDs) and with histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes to alter chromatin structure. Here we identify a lamin interaction domain (LID) found only in ING proteins, through which they bind to and colocalize with lamin A. Lamin knockout (LMNA(-/-)) cells show reduced levels of ING1 that mislocalize. Ectopic...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 18836436
DOI: 10.1038/ncb1792

Genes

ING1
LMNA

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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