Evidence map›Paper›PMID 23045692›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes.

Michael A Hadders, Monica Agromayor, Takayuki Obita, Olga Perisic, Anna Caballe, Magdalena Kloc, Meindert H Lamers, Roger L Williams, Juan Martin-Serrano

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Exosome: an overview on enhanced biogenesis by small molecules.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    Review
  2. Article
  3. MITD1 is a brain-specific interferon-inducible factor that inhibits flavivirus replication.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Omics Analyses ofGenes · 2022
    Article
  9. Mechanics and regulation of cytokinetic abscission.Frontiers in cell and developmental biology · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. The many functions of ESCRTs.Nature reviews. Molecular cell biology · 2020
    Review
  14. Review
  15. ESCRT-dependent control of membrane remodelling during cell division.Seminars in cell & developmental biology · 2018
    Review
  16. Article
  17. Article
  18. Review
  19. Molecular mechanisms of the membrane sculpting ESCRT pathway.Cold Spring Harbor perspectives in biology · 2013
    Review
  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

9 authors at 4 institutions in 1 country.

Michael A HaddersLaboratory of Molecular Biology, Medical Research Council, Cambridge CB2 0QH, United Kingdom.
Monica Agromayor
Takayuki Obita
Olga Perisic
Anna Caballe
Magdalena Kloc
Meindert H Lamers
Roger L Williams
Juan Martin-Serrano
MRC Laboratory of Molecular Biology · GBKing's College London · GBKing's College School · GBMedical Research Council · GB

Funding

Biotechnology and Biological Sciences Research Council 083639/Z/07/ZMedical Research Council G0802777Medical Research Council MC_U105184308Medical Research Council MC_U105197143Wellcome TrustWellcome Trust WT093056MA
6 · The paper itself

Abstract

The endosomal sorting complexes required for transport (ESCRT) proteins have a critical function in abscission, the final separation of the daughter cells during cytokinesis. Here, we describe the structure and function of a previously uncharacterized ESCRT-III interacting protein, MIT-domain containing protein 1 (MITD1). Crystal structures of MITD1 reveal a dimer, with a microtubule-interacting and trafficking (MIT) domain at the N terminus and a unique, unanticipated phospholipase D-like (PLD) domain at the C terminus that binds membranes. We show that the MIT domain binds to a subset of ESCRT-III subunits and that this interaction mediates MITD1 recruitment to the midbody during cytokinesis. Depletion of MITD1 causes a distinct cytokinetic phenotype consistent with destabilization of the midbody and abscission failure. These results suggest a model whereby MITD1 coordinates the activity of ESCRT-III during abscission with earlier events in the final stages of cell division.

Indexed as

Crystallography, X-RayCytokinesisEndosomal Sorting Complexes Required for TransportHeLa CellsHumansMembrane ProteinsMicrotubule-Associated ProteinsModels, MolecularPhospholipase DProtein BindingProtein FoldingEndosomal Sorting Complexes Required for TransportMembrane ProteinsMicrotubule-Associated ProteinsMITD1 protein, humanPhospholipase D

Identifiers

PMID23045692
PMCPMC3491508
OpenAlexW1973362849

What OpenQuestion holds

Textmetadata
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.