Evidence map›Paper›PMID 33605210›Full record

ArticleeLife2021

LAP2alpha maintains a mobile and low assembly state of A-type lamins in the nuclear interior.

Nana Naetar, Konstantina Georgiou, Christian Knapp, Irena Bronshtein, Elisabeth Zier, Petra Fichtinger, Thomas Dechat, Yuval Garini, Roland Foisner

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 38 citations in OpenAlex.

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  18. Dexamethasone induces p21FEBS open bio · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Nana Naetar *Max Perutz Labs, Center for Medical Biochemistry, Medical University of Vienna, Vienna Biocenter Campus (VBC), Vienna, Austria.ORCID 0000-0002-8978-466X
Konstantina Georgiou *Max Perutz Labs, Center for Medical Biochemistry, Medical University of Vienna, Vienna Biocenter Campus (VBC), Vienna, Austria.
Christian KnappMax Perutz Labs, Center for Medical Biochemistry, Medical University of Vienna, Vienna Biocenter Campus (VBC), Vienna, Austria.ORCID 0000-0003-2463-5775
Irena BronshteinPhysics Department and Nanotechnology Institute, Bar Ilan University, Ramat Gan, Israel.
Elisabeth ZierMax Perutz Labs, Center for Medical Biochemistry, Medical University of Vienna, Vienna Biocenter Campus (VBC), Vienna, Austria.
Petra FichtingerMax Perutz Labs, Center for Medical Biochemistry, Medical University of Vienna, Vienna Biocenter Campus (VBC), Vienna, Austria.
Thomas DechatMax Perutz Labs, Center for Medical Biochemistry, Medical University of Vienna, Vienna Biocenter Campus (VBC), Vienna, Austria.ORCID 0000-0003-3236-7889
Yuval GariniPhysics Department and Nanotechnology Institute, Bar Ilan University, Ramat Gan, Israel.ORCID 0000-0002-8783-2015
Roland FoisnerMax Perutz Labs, Center for Medical Biochemistry, Medical University of Vienna, Vienna Biocenter Campus (VBC), Vienna, Austria.ORCID 0000-0003-4734-4647
Max Perutz Labs · ATBar-Ilan University · IL

Funding

Austrian Science Fund FWF P 29713Austrian Science Fund FWF P 32512Austrian Science Fund FWF W 1261
6 · The paper itself

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.

Indexed as

AnimalsCell LineCell NucleusDNA-Binding ProteinsLamin Type AMembrane ProteinsMiceDNA-Binding Proteinslamina-associated polypeptide 2Lamin Type ALmna protein, mouseMembrane Proteinsassemblycell biologyhumanlamin-associated polypeptide 2lamin dynamicslamin phosphorylationlamins in nuclear interiormousenuclear lamins

Identifiers

PMID33605210
PMCPMC7939549
OpenAlexW3130758184

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.