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- W2114597129 abstract "The nuclear envelope in eukaryotic cells has important roles in chromatin organization. The inner nuclear membrane contains over 60 transmembrane proteins. LEM [LAP2 (lamina-associated polypeptide 2)/emerin/MAN1] domain-containing proteins of the inner nuclear membrane are involved in tethering chromatin to the nuclear envelope and affect gene expression. They contain a common structural, bihelical motif, the so-called LEM domain, which mediates binding to a conserved chromatin protein, BAF (barrier to autointegration factor). Interestingly, this domain is highly related to other bihelical motifs, termed HeH (helix–extension–helix) and SAP {SAF (scaffold attachment factor)/acinus/PIAS [protein inhibitor of activated STAT (signal transducer and activator of transcription)]} motifs, which are directly linked to DNA. In the present paper, we summarize evidence that the LEM motif evolved from the HeH and SAP domains concomitantly with BAF. In addition, we discuss the potential evolution of HeH/SAP and LEM domain-containing proteins and their role in chromatin tethering and gene regulation from unicellular eukaryotes to mammals." @default.
- W2114597129 created "2016-06-24" @default.
- W2114597129 creator A5072994610 @default.
- W2114597129 creator A5081263278 @default.
- W2114597129 date "2011-11-21" @default.
- W2114597129 modified "2023-10-18" @default.
- W2114597129 title "Evolvement of LEM proteins as chromatin tethers at the nuclear periphery" @default.
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- W2114597129 doi "https://doi.org/10.1042/bst20110724" @default.
- W2114597129 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4333761" @default.
- W2114597129 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22103517" @default.
- W2114597129 hasPublicationYear "2011" @default.
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