Evidence map›Paper›PMID 28406398›Full record

ArticleeLife2017

Lissencephaly-1 is a context-dependent regulator of the human dynein complex.

Janina Baumbach, Andal Murthy, Mark A McClintock, Carly I Dix, Ruta Zalyte, Ha Thi Hoang, Simon L Bullock

Abstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Non-transport functions of motor proteins in corticogenesis.Frontiers in cell and developmental biology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. CCSer2 gates dynein activity at the cell periphery.bioRxiv : the preprint server for biology · 2024
    Article
  13. Article
  14. Article
  15. VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. New pieces for the Lis1-dynein puzzle.Nature structural & molecular biology · 2023
    Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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

7 authors.

Janina BaumbachDivision of Cell Biology, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Andal MurthyDivision of Cell Biology, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Mark A McClintockDivision of Cell Biology, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Carly I DixDivision of Cell Biology, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Ruta ZalyteDivision of Structural Studies, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Ha Thi HoangDivision of Cell Biology, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Simon L BullockDivision of Cell Biology, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0001-9491-4548

Funding

Medical Research Council MC_U105178790
6 · The paper itself

Abstract

The cytoplasmic dynein-1 (dynein) motor plays a central role in microtubule organisation and cargo transport. These functions are spatially regulated by association of dynein and its accessory complex dynactin with dynamic microtubule plus ends. Here, we elucidate in vitro the roles of dynactin, end-binding protein-1 (EB1) and Lissencephaly-1 (LIS1) in the interaction of end tracking and minus end-directed human dynein complexes with these sites. LIS1 promotes dynactin-dependent tracking of dynein on both growing and shrinking plus ends. LIS1 also increases the frequency and velocity of processive dynein movements that are activated by complex formation with dynactin and a cargo adaptor. This stimulatory effect of LIS1 contrasts sharply with its documented ability to inhibit the activity of isolated dyneins. Collectively, our findings shed light on how mammalian dynein complexes associate with dynamic microtubules and help clarify how LIS1 promotes the plus-end localisation and cargo transport functions of dynein in vivo.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseDynactin ComplexDyneinsHumansMicrotubule-Associated ProteinsModels, BiologicalProtein BindingProtein Multimerization1-Alkyl-2-acetylglycerophosphocholine EsteraseDynactin ComplexDyneinsMAPRE1 protein, humanMicrotubule-Associated ProteinsPAFAH1B1 protein, humancargo adaptorcell biologydynactindynamic microtubulesdyneinEB1lissencephaly-1none

Identifiers

PMID28406398
PMCPMC5413349

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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.