title: Partners and post-translational modifications of nuclear lamins.
abstract: Nuclear intermediate filament networks formed by A- and B-type lamins are major components of the nucleoskeleton that are required for nuclear structure and function, with many links to human physiology. Mutations in lamins cause diverse human diseases ('laminopathies'). At least 54 partners interact with human A-type lamins directly or indirectly. The less studied human lamins B1 and B2 have 23 and seven reported partners, respectively. These interactions are likely to be regulated at least in part by lamin post-translational modifications. This review summarizes the binding partners and post-translational modifications of human lamins and discusses their known or potential implications for lamin function.
authors.affiliation: Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
authors.forename: Dan N
authors.initials: DN
authors.lastname: Simon
authors.forename: Katherine L
authors.initials: KL
authors.lastname: Wilson
mesh_terms: D002467:Cell Nucleus / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D034904:Lamin Type A / Q000235:genetics* / Q000378:metabolism; D034921:Lamin Type B / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D009685:Nuclear Envelope / Q000235:genetics / Q000378:metabolism; D015530:Nuclear Matrix / Q000378:metabolism; D011485:Protein Binding; D011499:Protein Processing, Post-Translational / Q000235:genetics*
chemical_list: D034904:Lamin Type A; D034921:Lamin Type B