Evidence map›Paper›PMID 33158857›Full record

ArticleScience advances2020

F-actin disassembly factor MICAL1 binding to Myosin Va mediates cargo unloading during cytokinesis.

Fengfeng Niu, Kang Sun, Wenjie Wei, Cong Yu, Zhiyi Wei

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structural basis of MICAL autoinhibition.Nature communications · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Mechanics and regulation of cytokinetic abscission.Frontiers in cell and developmental biology · 2022
    Review
  18. MICAL2 fine-tunes Arp2/3 for actin branching.The Journal of cell biology · 2021
    Article
  19. Article
  20. Review
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

5 authors at 1 institution in 1 country.

Fengfeng NiuDepartment of Biology, Southern University of Science and Technology, Shenzhen, Guangdong, China.ORCID 0000-0001-7029-4989
Kang SunDepartment of Biology, Southern University of Science and Technology, Shenzhen, Guangdong, China.ORCID 0000-0003-4632-0176
Wenjie WeiDepartment of Biology, Southern University of Science and Technology, Shenzhen, Guangdong, China.
Cong YuDepartment of Biology, Southern University of Science and Technology, Shenzhen, Guangdong, China. weizy@sustech.edu.cn yuc@sustech.edu.cn.ORCID 0000-0003-2912-6347
Zhiyi WeiDepartment of Biology, Southern University of Science and Technology, Shenzhen, Guangdong, China. weizy@sustech.edu.cn yuc@sustech.edu.cn.ORCID 0000-0002-4446-6502
Southern University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Motor-mediated intracellular trafficking requires motors to position cargoes at proper locations. Myosin Va (MyoVa), an actin-based motor, is a classic model for studying cargo transport. However, the molecular basis underlying cargo unloading in MyoVa-mediated transport has remained enigmatic. We have identified MICAL1, an F-actin disassembly regulator, as a binding partner of MyoVa and shown that MICAL1-MyoVa interaction is critical for localization of MyoVa at the midbody. By binding to MICAL1, MyoVa-mediated transport is terminated, resulting in vesicle unloading at the midbody for efficient cytokinesis. The MyoVa/MICAL1 complex structure reveals that MICAL1 and F-actin assembly factors, Spires, share an overlapped binding surface on MyoVa, suggesting a regulatory role of F-actin dynamics in cargo unloading. Down-regulating F-actin disassembly by a MICAL1 mutant significantly reduces MyoVa and vesicles accumulating at the midbody. Collectively, our findings demonstrate that MyoVa binds to MICAL1 at the midbody destination and triggers F-actin disassembly to unload the vesicle cargo.

Identifiers

PMID33158857
PMCPMC7673715
OpenAlexW3094753719

What OpenQuestion holds

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LicenceCC BY-NC
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.