Linked Life Data

11792821

Source:http://linkedlifedata.com/resource/pubmed/id/11792821

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 24
pubmed:dateCreated
2002-1-16
pubmed:abstractText
Loss of emerin, a lamin-binding nuclear membrane protein, causes Emery-Dreifuss muscular dystrophy. We analyzed 13 site-directed mutations, and four disease-causing mutations that do not disrupt emerin stability or localization. We show that emerin binds directly to barrier-to-autointegration factor (BAF), a DNA-bridging protein, and that this binding to BAF requires conserved residues in the LEM-motif of emerin. Emerin has two distinct functional domains: the LEM-domain at the N-terminus, which mediates binding to BAF, and a second functional domain in the central region, which mediates binding to lamin A. Disease mutation Delta95-99 mapped to the lamin-binding domain and disrupted lamin A binding in vitro. Two other disease-linked residues, Ser54 and Pro183, mapped outside the BAF and lamin-binding domains, suggesting that emerin may have additional functional domains relevant to disease. The disease-linked emerin proteins all remained active for binding to BAF, both in vitro and in vivo, suggesting that disease can result from the loss of specific molecular interactions between emerin and either lamin A or putative novel partner(s). The demonstration that emerin binds directly to BAF, coupled to similar results for LAP2, provides proof in principle that all LEM-domain nuclear proteins can interact with BAF, with interesting implications for chromatin attachment to the nuclear envelope.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4567-73
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11792821-Amino Acid Sequence, pubmed-meshheading:11792821-DNA-Binding Proteins, pubmed-meshheading:11792821-Gene Deletion, pubmed-meshheading:11792821-HeLa Cells, pubmed-meshheading:11792821-Humans, pubmed-meshheading:11792821-Lamin Type A, pubmed-meshheading:11792821-Lamins, pubmed-meshheading:11792821-Membrane Proteins, pubmed-meshheading:11792821-Molecular Sequence Data, pubmed-meshheading:11792821-Muscular Dystrophy, Emery-Dreifuss, pubmed-meshheading:11792821-Mutagenesis, Site-Directed, pubmed-meshheading:11792821-Nuclear Proteins, pubmed-meshheading:11792821-Point Mutation, pubmed-meshheading:11792821-Protein Binding, pubmed-meshheading:11792821-Protein Structure, Tertiary, pubmed-meshheading:11792821-Recombinant Proteins, pubmed-meshheading:11792821-Thymopoietins
pubmed:year
2001
pubmed:articleTitle
Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF.
pubmed:affiliation
Department of Cell Biology, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't