Evidence map›Paper›PMID 25059720›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Structural basis for the extended CAP-Gly domains of p150(glued) binding to microtubules and the implication for tubulin dynamics.

Qianmin Wang, Alvaro H Crevenna, Ines Kunze, Naoko Mizuno

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Conformational Flexibility of p150Biophysical journal · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. TheJournal of developmental biology · 2017
    Article
  18. Article
  19. Article
  20. Article
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

4 authors.

Qianmin WangCellular and Membrane Trafficking, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany; and.
Alvaro H CrevennaPhysical Chemistry, Department for Chemistry and Biochemistry and Center for NanoScience, Ludwig-Maximilians-Universität München, D-81377 Munich, Germany.
Ines KunzeCellular and Membrane Trafficking, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany; and.
Naoko MizunoCellular and Membrane Trafficking, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany; and mizuno@biochem.mpg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

p150(glued) belongs to a group of proteins accumulating at microtubule plus ends (+TIPs). It plays a key role in initiating retrograde transport by recruiting and tethering endosomes and dynein to microtubules. p150(glued) contains an N-terminal microtubule-binding cytoskeleton-associated protein glycine-rich (CAP-Gly) domain that accelerates tubulin polymerization. Although this copolymerization is well-studied using light microscopic techniques, structural consequences of this interaction are elusive. Here, using electron-microscopic and spectroscopic approaches, we provide a detailed structural view of p150(glued) CAP-Gly binding to microtubules and tubulin. Cryo-EM 3D reconstructions of p150(glued)-CAP-Gly complexed with microtubules revealed the recognition of the microtubule surface, including tubulin C-terminal tails by CAP-Gly. These binding surfaces differ from other retrograde initiation proteins like EB1 or dynein, which could facilitate the simultaneous attachment of all accessory components. Furthermore, the CAP-Gly domain, with its basic extensions, facilitates lateral and longitudinal interactions of tubulin molecules by covering the tubulin acidic tails. This shielding effect of CAP-Gly and its basic extensions may provide a molecular basis of the roles of p150(glued) in microtubule dynamics.

Indexed as

Cold TemperatureCryoelectron MicroscopyDynactin ComplexDyneinsGuanosine TriphosphateHydrolysisImage Processing, Computer-AssistedKineticsMicrotubule-Associated ProteinsMicrotubulesPeptidesPolymerizationProtein BindingProtein MultimerizationProtein Structure, TertiarySequence DeletionDynactin ComplexDyneinsGuanosine TriphosphateMicrotubule-Associated ProteinsPeptidesTubulincytoskeletondynactindynamic instabilityelectron microscopy

Identifiers

PMID25059720
PMCPMC4128117

What OpenQuestion holds

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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.