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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.
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The nuclear lamina is an extensive protein network that contributes to nuclear structure and function. LEM domain (LAP2, emerin, MAN1 domain, LEM-D) proteins are components of the nuclear lamina, identified by a shared ∼45-amino-acid motif that binds Barrier-to-autointegration factor (BAF), a chromatin-interacting protein.Drosophila melanogaster has three nuclear lamina LEM-D proteins, named.
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Thyroid cancer (TC) is the most common type of endocrine malignancy in humans, and its relative incidence has increased continuously in recent years. However, the primary molecular mechanisms of thyroid tumorigenesis and progression remain unclear. Papillary TC (PTC) is the most common subtype of TC. Recent studies have reported that one of the tumorigenesis and progression mechanisms is.
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cl02649: LEM Superfamily. LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner nuclear membrane protein Man1 and similar proteins. The family corresponds to a group of inner nuclear membrane proteins containing LEM domain. Emerin occurs in four phosphorylated forms and plays a role in cell cycle-dependent.
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In metazoan cell nuclei, hundreds of large chromatin domains are in close contact with the nuclear lamina. Such lamina-associated domains (LADs) are thought to help organize chromosomes inside the nucleus and have been associated with gene repression..
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The LEM‐domain was initially described as a conserved globular module of approximately 40 amino acids. The three‐dimensional structure of this motif was determined in 2001 by Cai et al. and Laguri et al., who demonstrated that the LEM‐domain as well as the LEM‐like domain is composed of two parallel α‐helices that are connected by a.
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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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2007 (English) In: International Review of Cytology, ISSN 0074-7696, E-ISSN 2163-5854, Vol. 261, p. 1-+ Article, review/survey (Refereed) Published Abstract [en] 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.