Evidence map›Paper›PMID 36107127›Full record

ArticleThe Journal of cell biology2022

Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin.

Ennio A d'Amico, Misbha Ud Din Ahmad, Verena Cmentowski, Mathias Girbig, Franziska Müller, Sabine Wohlgemuth, Andreas Brockmeyer, Stefano Maffini, Petra Janning, Ingrid R Vetter and 3 more

Abstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors.

Ennio A d'AmicoDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0002-1451-6273
Misbha Ud Din Ahmad *Oncode Institute and Department of Biochemistry, The Netherlands Cancer Institute, Amsterdam, The Netherlands.ORCID 0000-0002-4892-7337
Verena Cmentowski *Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0003-4194-8108
Mathias GirbigMRC Laboratory of Molecular Biology, Cambridge, UK.
Franziska MüllerDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0002-4880-9269
Sabine WohlgemuthDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Andreas BrockmeyerDepartment of Chemical Biology, Max-Planck-Institute of Molecular Physiology, Dortmund, Germany.
Stefano MaffiniDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0001-6380-6560
Petra JanningDepartment of Chemical Biology, Max-Planck-Institute of Molecular Physiology, Dortmund, Germany.
Ingrid R VetterDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0002-1722-425X
Andrew P CarterMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0001-7292-5430
Anastassis PerrakisOncode Institute and Department of Biochemistry, The Netherlands Cancer Institute, Amsterdam, The Netherlands.ORCID 0000-0002-1151-6227
Andrea MusacchioDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0003-2362-8784

Funding

Deutsche Forschungsgemeinschaft SFB1430European Research Council 951439Marie-Curie Training Network 675737Max Planck SocietyMedical Research Council MC_UP_A025_1011Wellcome Trust 210711/Z/18/Z
6 · The paper itself

Abstract

Cytoplasmic Dynein 1, or Dynein, is a microtubule minus end-directed motor. Dynein motility requires Dynactin and a family of activating adaptors that stabilize the Dynein-Dynactin complex and promote regulated interactions with cargo in space and time. How activating adaptors limit Dynein activation to specialized subcellular locales is unclear. Here, we reveal that Spindly, a mitotic Dynein adaptor at the kinetochore corona, exists natively in a closed conformation that occludes binding of Dynein-Dynactin to its CC1 box and Spindly motif. A structure-based analysis identified various mutations promoting an open conformation of Spindly that binds Dynein-Dynactin. A region of Spindly downstream from the Spindly motif and not required for cargo binding faces the CC1 box and stabilizes the intramolecular closed conformation. This region is also required for robust kinetochore localization of Spindly, suggesting that kinetochores promote Spindly activation to recruit Dynein. Thus, our work illustrates how specific Dynein activation at a defined cellular locale may require multiple factors.

Indexed as

Cell Cycle ProteinsCytoplasmic DyneinsDynactin ComplexKinetochoresProtein ConformationCell Cycle ProteinsCytoplasmic DyneinsDynactin Complex

Identifiers

PMID36107127
PMCPMC9481740

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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.