{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T01:34:58Z","timestamp":1791423298831,"version":"4.3.3"},"reference-count":59,"publisher":"American Society for Cell Biology (ASCB)","issue":"3","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[2013,2]]},"abstract":"<jats:p> Lamin filaments are major components of the nucleoskeleton that bind LINC complexes and many nuclear membrane proteins. The tail domain of lamin A directly binds 21 known partners, including actin, emerin, and SREBP1, but how these interactions are regulated is unknown. We report small ubiquitin-like modifier 1 (SUMO1) as a major new posttranslational modification of the lamin A tail. Two SUMO1 modification sites were identified based on in vitro SUMOylation assays and studies of Cos-7 cells. One site (K420) matches the SUMO1 target consensus; the other (K486) does not. On the basis of the position of K486 on the lamin A Ig-fold, we hypothesize the SUMO1 E2 enzyme recognizes a folded structure\u2013dependent motif that includes residues genetically linked to familial partial lipodystrophy (FPLD). Supporting this model, SUMO1-modification of the lamin A tail is reduced by two FPLD-causing mutations, G465D and K486N, and by single mutations in acidic residues E460 and D461. These results suggest a novel mode of functional control over lamin A in cells. <\/jats:p>","DOI":"10.1091\/mbc.e12-07-0527","type":"journal-article","created":{"date-parts":[[2012,12,16]],"date-time":"2012-12-16T02:05:47Z","timestamp":1355623547000},"page":"342-350","source":"Crossref","is-referenced-by-count":46,"title":["Lamin A tail modification by SUMO1 is disrupted by familial partial lipodystrophy\u2013causing mutations"],"prefix":"10.1091","volume":"24","author":[{"given":"Dan N.","family":"Simon","sequence":"first","affiliation":[{"name":"Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tera","family":"Domaradzki","sequence":"additional","affiliation":[{"name":"Department of Physiology and Biophysics, University at Buffalo-State University of New York, Buffalo, NY 14214"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wilma 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