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Chromosoma (2013) 122:1331
DOI 10.1007/s00412-013-0399-8
REVIEW ARTICLE
Partners and post-translational modifications of nuclear lamins
Dan N. Simon & Katherine L. Wilson
Received: 18 October 2012 /Revised: 7 February 2013 /Accepted: 8 February 2013 /Published online: 12 March 2013 # Springer-Verlag Berlin Heidelberg 2013
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.
Keywords Lamin . Phosphorylation . Acetylation .
O-GlcNAcylation . Ubiquitylation . SUMOylation . Oxidation . Nucleoskeleton . Nuclear envelope .Laminopathy
Introduction
Lamins are major components of the nucleoskeleton in multicellular animals (metazoans), not found in plants or fungi (Dittmer and Misteli 2011). Lamins tether chromatin, bind signaling proteins and support epigenetic regulation, mechanotransduction, development, transcription, replication and DNA damage repair (Dechat et al. 2008; Dittmer and Misteli 2011; Simon and Wilson 2011). How lamins
contribute to such a remarkable range of activities is for the most part unknown: a new saga in biology that begins with a seemingly simple structural polymer. Lamins form highly stable filament networks near the inner membrane of the nuclear envelope and are also distributed throughout the nucleoplasm except for the nucleolus (Gerace and Huber 2012; Dittmer and Misteli 2011; Simon and Wilson 2011). Mammals express two types of lamins, the B-type (lamins B1, B2 and B3) encoded by LMNB1 and LMNB2 (Dittmer and Misteli 2011; Schumacher et al. 2006), and A-type (lamins A, C, A10, C2, and A50, also known as progerin) generated by alternative splicing of LMNA (Dittmer and Misteli 2011; Bokenkamp et al. 2011).
Mutations in lamins cause a variety of diseases, collectively termed laminopathies (Worman 2012; Butin-Israeli et al. 2012). So far nearly 400 different disease-causing mutations in A-type lamins have been identified, underscoring their significance to cell and tissue biology...