{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T10:25:16Z","timestamp":1770978316540,"version":"3.50.1"},"reference-count":58,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2012,1,3]],"date-time":"2012-01-03T00:00:00Z","timestamp":1325548800000},"content-version":"vor","delay-in-days":854,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biology of the Cell"],"published-print":{"date-parts":[[2009,9]]},"abstract":"<jats:p><jats:italic>Background information<\/jats:italic>. Emerin is a nuclear envelope protein that contributes to nuclear architecture, chromatin structure, and gene expression through its interaction with various nuclear proteins. In particular, emerin is molecularly connected with the nuclear lamina, a protein meshwork composed of lamins and lamin\u2010binding proteins underlying the inner nuclear membrane. Among nuclear lamina components, lamin A is a major emerin partner. Lamin A, encoded by the <jats:italic>LMNA<\/jats:italic> gene (lamin A\/C gene), is produced as a precursor protein (prelamin A) that is post\u2010transcriptionally modified at its C\u2010terminal region where the CaaX motif triggers a sequence of modifications, including farnesylation, carboxymethylation, and proteolytic cleavage by ZMPSTE 24 (zinc metalloproteinase Ste24) metalloproteinase. Impairment of the lamin A maturation pathway causing lamin A precursor accumulation is linked to the development of rare diseases such as familial partial lipodystrophy, MADA (mandibuloacral dysplasia), the Werner syndrome, Hutchinson\u2014Gilford progeria syndrome and RD (restrictive dermopathy).<\/jats:p><jats:p><jats:italic>Results<\/jats:italic>. In the present study, we show that emerin and different prelamin A forms influence each other's localization. We show that the accumulation of non\u2010farnesylated as well as farnesylated carboxymethylated lamin A precursors in human fibroblasts modifies emerin localization. On the contrary, emerin absence at the inner nuclear membrane leads to unprocessed (non\u2010farnesylated) prelamin A aberrant localization only. Moreover, we observe that the restoration of emerin expression in emerin\u2010null cells induces the recovery of non\u2010farnesylated prelamin A localization.<\/jats:p><jats:p><jats:italic>Conclusion<\/jats:italic>. These results indicate that emerin\u2014prelamin A interplay influences nuclear organization. This finding may be relevant to the understanding of laminopathies.<\/jats:p>","DOI":"10.1042\/bc20080175","type":"journal-article","created":{"date-parts":[[2009,3,30]],"date-time":"2009-03-30T12:16:37Z","timestamp":1238415397000},"page":"541-554","source":"Crossref","is-referenced-by-count":24,"title":["Emerin\u2014prelamin A interplay in human fibroblasts"],"prefix":"10.1111","volume":"101","author":[{"given":"Cristina","family":"Capanni","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rosalba","family":"Del Coco","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elisabetta","family":"Mattioli","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daria","family":"Camozzi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marta","family":"Columbaro","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elisa","family":"Schena","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luciano","family":"Merlini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stefano","family":"Squarzoni","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nadir Mario","family":"Maraldi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Giovanna","family":"Lattanzi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2012,1,3]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/ng1294-323"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/nsmb989"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1985.tb03679.x"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200502062"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1474-9726.2008.00393.x"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-4827(03)00395-1"},{"key":"e_1_2_8_8_1","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/ddi158"},{"key":"e_1_2_8_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.yexcr.2008.09.026"},{"key":"e_1_2_8_10_1","doi-asserted-by":"publisher","DOI":"10.1093\/hmg\/6.13.2257"},{"key":"e_1_2_8_11_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00018-005-5318-6"},{"key":"e_1_2_8_12_1","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.01529"},{"key":"e_1_2_8_13_1","doi-asserted-by":"publisher","DOI":"10.1101\/gad.1652708"},{"key":"e_1_2_8_14_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200801096"},{"key":"e_1_2_8_15_1","doi-asserted-by":"crossref","first-page":"2571","DOI":"10.1242\/jcs.112.15.2571","article-title":"The Emery\u2014Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane","volume":"112","author":"Fairley E.A.","year":"1999","journal-title":"J. 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