LAP2alpha maintains a mobile and low assembly state of A-type lamins in the nuclear interior.
Elife
; 102021 02 19.
Article
em En
| MEDLINE
| ID: mdl-33605210
ABSTRACT
Lamins form stable filaments at the nuclear periphery in metazoans. Unlike B-type lamins, lamins A and C localize also in the nuclear interior, where they interact with lamin-associated polypeptide 2 alpha (LAP2α). Using antibody labeling, we previously observed a depletion of nucleoplasmic A-type lamins in mouse cells lacking LAP2α. Here, we show that loss of LAP2α actually causes formation of larger, biochemically stable lamin A/C structures in the nuclear interior that are inaccessible to lamin A/C antibodies. While nucleoplasmic lamin A forms from newly expressed pre-lamin A during processing and from soluble mitotic lamins in a LAP2α-independent manner, binding of LAP2α to lamin A/C during interphase inhibits formation of higher order structures, keeping nucleoplasmic lamin A/C in a mobile state independent of lamin A/C S22 phosphorylation. We propose that LAP2α is essential to maintain a mobile lamin A/C pool in the nuclear interior, which is required for proper nuclear functions.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Lamina Tipo A
/
Proteínas de Ligação a DNA
/
Proteínas de Membrana
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article