Evidence map›Paper›PMID 22106867›Full record

ArticleTraffic (Copenhagen, Denmark)2012

In vivo roles of the basic domain of dynactin p150 in microtubule plus-end tracking and dynein function.

Xuanli Yao, Jun Zhang, Henry Zhou, Eric Wang, Xin Xiang

Abstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020
    Review
  10. Article
  11. Article
  12. Nuclear movement in fungi.Seminars in cell & developmental biology · 2018
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Cytoplasmic dynein and early endosome transport.Cellular and molecular life sciences : CMLS · 2015
    Review
  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

5 authors at 1 institution in 1 country.

Xuanli YaoDepartment of Biochemistry and Molecular Biology, The Uniformed Services University, Bethesda, MD, USA.
Jun Zhang
Henry Zhou
Eric Wang
Xin Xiang
Uniformed Services University of the Health Sciences · US

Funding

Dissecting the interaction between dynein and early endosomesR01GM097580 · NIGMS · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI XIANG, XIN · 2011 to 2014
$1.2M
NIGMS NIH HHS 1R01GM097580-01NIGMS NIH HHS R01 GM097580
6 · The paper itself

Abstract

Microtubule (MT) plus-end-tracking proteins accumulate at MT plus ends for various cellular functions, but their targeting mechanisms are not fully understood (Akhmanova A and Steinmetz MO. Tracking the ends: a dynamic protein network controls the fate of microtubule tips. Nat Rev Mol Cell Biol 2008;9:309-322.). Here, we tested in the filamentous fungus Aspergillus nidulans the requirement for plus-end localization of dynactin p150, a protein essential for dynein function. Deletion of the N-terminal MT-binding region of p150 significantly diminishes the MT plus-end accumulation of both dynein heavy chain and p150, and causes a partial defect in nuclear distribution. Surprisingly, within the MT-binding region, the basic domain is more critical than the CAP-Gly (cytoskeleton-associated protein glycine-rich) domain for maintaining plus-end tracking of p150, as well as for the functions of dynein in nuclear distribution and early endosome movement. Our results show that the basic domain of A. nidulans p150 is important for p150-MT interaction both in vivo and in vitro, and the basic amino acids within this domain are crucial for the plus-end accumulation of p150 in the wild-type background and for the p150-MT interaction in the ΔkinA (kinesin-1) background. We suggest that the basic amino acids are required for the electrostatic interaction between p150 and MTs, which is important for kinesin-1-mediated plus-end targeting of dynactin and dynein in A. nidulans.

Indexed as

Amino Acid SequenceAspergillus nidulansBlotting, WesternDynactin ComplexDyneinsMicrotubule-Associated ProteinsMicrotubulesMolecular Sequence DataSequence AlignmentDynactin ComplexDyneinsMicrotubule-Associated Proteins

Identifiers

PMID22106867
PMCPMC3276731
OpenAlexW1582861467

What OpenQuestion holds

Textmetadata
LicenceTDM
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.