Evidence map›Paper›PMID 38587458›Full record

ArticleJournal of cell science2024

Caskin2 is a novel talin- and Abi1-binding protein that promotes cell motility.

Wei Wang, Paul Atherton, Maaike Kreft, Lisa Te Molder, Sabine van der Poel, Liesbeth Hoekman, Patrick Celie, Robbie P Joosten, Reinhard Fässler, Anastassis Perrakis and 1 more

Abstract read
In one paragraph

Article in Journal of cell science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. CASKIN2 mediates PTPσ-orchestrated transsynaptic mechanisms at excitatory synapses.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
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

11 authors.

Wei WangDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands.ORCID 0000-0003-4869-6716
Paul AthertonDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands.ORCID 0000-0003-3098-674X
Maaike KreftDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands.
Lisa Te MolderDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands.
Sabine van der PoelDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands.
Liesbeth HoekmanProteomics Facility, The Netherlands Cancer Institute, Amsterdam 1066 CX, The Netherlands.ORCID 0000-0002-3552-6390
Patrick CelieDivision of Biochemistry, The Netherlands Cancer Institute, Amsterdam 1066 CX, The Netherlands.ORCID 0000-0002-6557-078X
Robbie P JoostenDivision of Biochemistry, The Netherlands Cancer Institute, Amsterdam 1066 CX, The Netherlands.ORCID 0000-0002-2323-2686
Reinhard FässlerDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.ORCID 0000-0002-0145-6937
Anastassis PerrakisOncode Institute and Division of Biochemistry, The Netherlands Cancer Institute, Amsterdam 1066 CX, The Netherlands.ORCID 0000-0002-1151-6227
Arnoud SonnenbergDivision of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam 1066 CX, The Netherlands.ORCID 0000-0001-9585-468X

Funding

Dutch Cancer Society 12143National Natural Science Foundation of China 32300634Nederlandse Organisatie voor Wetenschappelijk Onderzoek 184.032.201Netherlands Cancer InstituteShanghai Rising-Star 23YF1443200Wellcome Trust
6 · The paper itself

Abstract

Talin (herein referring collectively to talin 1 and 2) couples the actomyosin cytoskeleton to integrins and transmits tension to the extracellular matrix. Talin also interacts with numerous additional proteins capable of modulating the actin-integrin linkage and thus downstream mechanosignaling cascades. Here, we demonstrate that the scaffold protein Caskin2 interacts directly with the R8 domain of talin through its C-terminal LD motif. Caskin2 also associates with the WAVE regulatory complex to promote cell migration in an Abi1-dependent manner. Furthermore, we demonstrate that the Caskin2-Abi1 interaction is regulated by growth factor-induced phosphorylation of Caskin2 on serine 878. In MCF7 and UACC893 cells, which contain an amplification of CASKIN2, Caskin2 localizes in plasma membrane-associated plaques and around focal adhesions in cortical microtubule stabilization complexes. Taken together, our results identify Caskin2 as a novel talin-binding protein that might not only connect integrin-mediated adhesion to actin polymerization but could also play a role in crosstalk between integrins and microtubules.

Indexed as

Adaptor Proteins, Signal TransducingCell MovementCytoskeletal ProteinsProtein BindingTalinFocal AdhesionsHumansIntegrinsMCF-7 CellsMicrotubulesPhosphorylationABI1 protein, humanAdaptor Proteins, Signal TransducingCytoskeletal ProteinsIntegrinsTalinAbiCaskin2Cortical microtubule stabilizing complexFocal adhesionKANKTalinTensionWAVE

Identifiers

PMID38587458
PMCPMC11166458

What Socratic 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 Socratic graph.