title: Lamina-associated polypeptide 1: protein interactions and tissue-selective functions.
abstract: Mutations in genes encoding widely expressed nuclear envelope proteins often lead to diseases that manifest in specific tissues. Lamina-associated polypeptide 1 (LAP1) is an integral protein of the inner nuclear membrane that is expressed in most cells and tissues. Within the nuclear envelope, LAP1 interacts physically with lamins, torsinA and emerin, suggesting it may serve as a key node for transducing signals across the inner nuclear membrane. Indeed, recent in vivo studies in genetically modified mice strongly support functional links between LAP1 and both torsinA (in neurons) and emerin (in muscle). These studies suggest that tissue-selective diseases caused by mutations in genes encoding nuclear envelope proteins may result, at least in part, from the selective disruption of discrete nuclear envelope protein complexes.
authors: Department of Medicine, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA; Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA.
authors: Ji-Yeon
authors: JY
authors: Shin
authors: Department of Neurology, University of Michigan Medical School, 109 Zina Pitcher Place, Ann Arbor, MI, 48109, USA; Department of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, Ann Arbor, MI, 48109, USA. Electronic address: dauer@med.mich.edu.
authors: William T
authors: WT
authors: Dauer
authors: Department of Medicine, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA; Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY, 10032, USA. Electronic address: hjw14@columbia.edu.
authors: Howard J
authors: HJ
authors: Worman
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D003598:Cytoskeletal Proteins; D006801:Humans; D034882:Lamins / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism*; D051379:Mice; D018832:Molecular Chaperones / Q000378:metabolism; D009136:Muscular Dystrophies / Q000235:genetics* / Q000473:pathology; D009154:Mutation; D009685:Nuclear Envelope / Q000502:physiology*; D009687:Nuclear Proteins / Q000235:genetics* / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D002352:Carrier Proteins; D003598:Cytoskeletal Proteins; D034882:Lamins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D009687:Nuclear Proteins; C108175:TOR1A protein, human; C486250:TOR1AIP1 protein, human; C500006:TOR1AIP2 protein, human; C092710:emerin
keywords: Dystonia; Lamin; Muscular dystrophy; Nuclear envelope; Nuclear membrane