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Proteins resident in the inner nuclear membrane and underlying nuclear lamina form a network that regulates nuclear functions. This review highlights a prominent family of nuclear lamina proteins that carries the LAP2-emerin-MAN1-domain (LEM-D). LEM-D proteins share an ability to bind lamins and tether repressive chromatin at the nuclear periphery.
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LEM-Domain proteins: new insights into lamin-interacting proteins. Int Rev Cytol2007;261:1-46. doi: 10.1016/S0074-7696 (07)61001-8. Department of Developmental Biology, Wenner-Gren Institute, Stockholm University, S-10691 Stockholm, Sweden. 10.1016/S0074-7696 (07)61001-8. LEM-domain proteins present a growing family of nonrelated inner nuclear.
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Following cell division, phase separation of the transmembrane adaptor LEM2 ensures that the ESCRT machinery remodels microtubules and seals the nuclear envelope.
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The nuclear lamina is an extensive protein network that lies underneath the inner membrane of the nuclear envelope. This network establishes mechanical support for the nucleus and provides a platform for protein interactions that contribute to gene regulation, DNA replication and genome stability [1, 2, 3]. The major constituents of the nuclear.
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LEM‐domain proteins present a growing family of nonrelated inner nuclear membrane and intranuclear proteins, including emerin, MAN1, LEM2, several alternatively spliced isoforms of LAP2, and various uncharacterized proteins in higher eukaryotes as well as the Drosophila‐specific proteins otefin and Bocksbeutel.LEM‐domain proteins are involved in diverse cellular processes including.