Evidence map›Paper›PMID 37105961›Full record

ArticleNature communications2023

BICD2 phosphorylation regulates dynein function and centrosome separation in G2 and M.

Núria Gallisà-Suñé, Paula Sànchez-Fernàndez-de-Landa, Fabian Zimmermann, Marina Serna, Laura Regué, Joel Paz, Oscar Llorca, Jens Lüders, Joan Roig

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 23 citations in OpenAlex.

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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 3 institutions in 1 country.

Núria Gallisà-SuñéDepartment of Cells and Tissues, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri i Reixac 10-12, 08028, Barcelona, Spain.ORCID 0000-0003-2874-0345
Paula Sànchez-Fernàndez-de-LandaDepartment of Cells and Tissues, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri i Reixac 10-12, 08028, Barcelona, Spain.
Fabian ZimmermannMechanisms of Disease Programme, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10-12, 08028, Barcelona, Spain.
Marina SernaStructural Biology Programme, Spanish National Cancer Research Centre (CNIO), Melchor Fernández Almagro 3, E-28029, Madrid, Spain.
Laura ReguéDepartment of Cells and Tissues, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri i Reixac 10-12, 08028, Barcelona, Spain.
Joel PazMechanisms of Disease Programme, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10-12, 08028, Barcelona, Spain.
Oscar LlorcaStructural Biology Programme, Spanish National Cancer Research Centre (CNIO), Melchor Fernández Almagro 3, E-28029, Madrid, Spain.ORCID 0000-0001-5705-0699
Jens LüdersMechanisms of Disease Programme, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10-12, 08028, Barcelona, Spain.ORCID 0000-0002-9018-7977
Joan RoigDepartment of Cells and Tissues, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri i Reixac 10-12, 08028, Barcelona, Spain. jrabmc@ibmb.csic.es.ORCID 0000-0002-3872-4712
Institute for Research in Biomedicine · ESInstitut de Biologia Molecular de Barcelona · ESSpanish National Cancer Research Centre · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activity of dynein is regulated by a number of adaptors that mediate its interaction with dynactin, effectively activating the motor complex while also connecting it to different cargos. The regulation of adaptors is consequently central to dynein physiology but remains largely unexplored. We now describe that one of the best-known dynein adaptors, BICD2, is effectively activated through phosphorylation. In G2, phosphorylation of BICD2 by CDK1 promotes its interaction with PLK1. In turn, PLK1 phosphorylation of a single residue in the N-terminus of BICD2 results in a structural change that facilitates the interaction with dynein and dynactin, allowing the formation of active motor complexes. Moreover, modified BICD2 preferentially interacts with the nucleoporin RanBP2 once RanBP2 has been phosphorylated by CDK1. BICD2 phosphorylation is central for dynein recruitment to the nuclear envelope, centrosome tethering to the nucleus and centrosome separation in the G2 and M phases of the cell cycle. This work reveals adaptor activation through phosphorylation as crucial for the spatiotemporal regulation of dynein activity.

Indexed as

DyneinsMicrotubule-Associated ProteinsCell CycleCentrosomeDynactin ComplexPhosphorylationDynactin ComplexDyneinsMicrotubule-Associated Proteins

Identifiers

PMID37105961
PMCPMC10140047
OpenAlexW4367176084

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.