The molecular basis of emerin-emerin and emerin-BAF interactions.

TitleThe molecular basis of emerin-emerin and emerin-BAF interactions.
Publication TypeJournal Article
Year of Publication2014
JournalJournal of cell science
Volume127
IssuePt 18
Pagination3956-69
Date Published2014
ISSN0021-9533
Abstract

Emerin is a conserved membrane component of nuclear lamina structure. Here, we report an advance in understanding the molecular basis of emerin function: intermolecular emerin-emerin association. There were two modes: one mediated by association of residues 170-220 in one emerin molecule to residues 170-220 in another, and the second involving residues 170-220 and 1-132. Deletion analysis showed residues 187-220 contain a positive element essential for intermolecular association in cells. By contrast, deletion of residues 168-186 inactivated a proposed negative element, required to limit or control association. Association of GFP-emerin with nuclear BAF in cells required the LEM domain (residues 1-47) and the positive element. Emerin peptide arrays revealed direct binding of residues 170-220 to residues 206-225 (the proposed positive element), residues 147-174 (particularly P(153)MYGRDSAYQSITHYRP(169)) and the LEM domain. Emerin residues 1-132 and 159-220 were each sufficient to bind lamin A or B1 tails in vitro, identifying two independent regions of molecular contact with lamins. These results, and predicted emerin intrinsic disorder, support the hypothesis that there are multiple 'backbone' and LEM-domain configurations in a proposed intermolecular emerin network at the nuclear envelope.

URLhttp://jcs.biologists.org/cgi/pmidlookup?view=long&pmid=25052089
DOI10.1242/jcs.148247
Short TitleJ Cell Sci
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