RT Journal Article
SR Electronic
T1 LAP2alpha maintains a mobile and low assembly state of A-type lamins in the nuclear interior
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.09.25.313296
DO 10.1101/2020.09.25.313296
A1 Nana Naetar
A1 Konstantina Georgiou
A1 Christian Knapp
A1 Irena Bronshtein
A1 Elisabeth Zier
A1 Petra Fichtinger
A1 Thomas Dechat
A1 Yuval Garini
A1 Roland Foisner
YR 2020
UL http://biorxiv.org/content/early/2020/09/25/2020.09.25.313296.abstract
AB 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). We show that lamin A in the nuclear interior is formed from newly expressed pre-lamin A during processing and from soluble mitotic mature lamins in a LAP2α-independent manner. Binding of LAP2α to lamins A/C in the nuclear interior during interphase inhibits formation of higher order structures of lamin A/C in vitro and in vivo, keeping lamin A/C in a mobile low assembly state independent of lamin A/C S22 phosphorylation. Loss of LAP2α causes formation of larger, less mobile and biochemically stable lamin A/C structures in the nuclear interior, which reduce the mobility of chromatin. 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.Competing Interest StatementThe authors have declared no competing interest.