Evidence map›Paper›PMID 21646404›Full record

ArticleThe Journal of cell biology2011

SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase.

Babet van der Vaart, Cristina Manatschal, Ilya Grigoriev, Vincent Olieric, Susana Montenegro Gouveia, Sasa Bjelic, Jeroen Demmers, Ivan Vorobjev, Casper C Hoogenraad, Michel O Steinmetz and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed, 1 pooled it
4.5field-weighted citation impact, top 5% 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

81 citing papers in PubMed, 1 synthesis or guideline pooled it, 133 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. The dynamic duo of microtubule polymerase Mini spindles/XMAP215 and cytoplasmic dynein is essential for maintainingProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. bioRxiv : the preprint server for biology · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. eLife · 2022
    Article
  18. Article
  19. Article
  20. Article

21 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

11 authors at 5 institutions in 5 countries.

Babet van der VaartDepartment of Cell Biology, Erasmus Medical Center, 3000 CA Rotterdam, Netherlands.
Cristina Manatschal
Ilya Grigoriev
Vincent Olieric
Susana Montenegro Gouveia
Sasa Bjelic
Jeroen Demmers
Ivan Vorobjev
Casper C Hoogenraad
Michel O Steinmetz
Anna Akhmanova
Erasmus MC · NLMolecular Research Institute · USInstitute of Cell Biology · UALomonosov Moscow State University · RUSwiss Light Source

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ends of growing microtubules (MTs) accumulate a set of diverse factors known as MT plus end-tracking proteins (+TIPs), which control microtubule dynamics and organization. In this paper, we identify SLAIN2 as a key component of +TIP interaction networks. We showed that the C-terminal part of SLAIN2 bound to end-binding proteins (EBs), cytoplasmic linker proteins (CLIPs), and CLIP-associated proteins and characterized in detail the interaction of SLAIN2 with EB1 and CLIP-170. Furthermore, we found that the N-terminal part of SLAIN2 interacted with ch-TOG, the mammalian homologue of the MT polymerase XMAP215. Through its multiple interactions, SLAIN2 enhanced ch-TOG accumulation at MT plus ends and, as a consequence, strongly stimulated processive MT polymerization in interphase cells. Depletion or disruption of the SLAIN2-ch-TOG complex led to disorganization of the radial MT array. During mitosis, SLAIN2 became highly phosphorylated, and its interaction with EBs and ch-TOG was inhibited. Our study provides new insights into the molecular mechanisms underlying cell cycle-specific regulation of MT polymerization and the organization of the MT network.

Indexed as

Amino Acid SequenceAnimalsCell LineInterphaseMicrotubule-Associated ProteinsMicrotubulesModels, MolecularMolecular Sequence DataNeoplasm ProteinsProtein ConformationProteinsRecombinant Fusion ProteinsRNA, Small InterferingSequence Alignmentcytoplasmic linker protein 170EB1 microtubule binding proteinsMicrotubule-Associated ProteinsNeoplasm ProteinsProteinsRecombinant Fusion ProteinsRNA, Small InterferingSLAIN1 protein, humanSLAIN2 protein, human

Identifiers

PMID21646404
PMCPMC3115796
OpenAlexW1993016853

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.