Evidence map›Paper›PMID 21057110›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin alpha1.

Yufeng Tong, Wolfram Tempel, Hui Wang, Kaori Yamada, Limin Shen, Guillermo A Senisterra, Farrell MacKenzie, Athar H Chishti, Hee-Won Park

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

35 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  5. Specific kinesin and dynein molecules participate in the unconventional protein secretion of transmembrane proteins.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. 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

9 authors at 4 institutions in 2 countries.

Yufeng TongStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Wolfram Tempel
Hui Wang
Kaori Yamada
Limin Shen
Guillermo A Senisterra
Farrell MacKenzie
Athar H Chishti
Hee-Won Park
University of Toronto · CAStructural Genomics Consortium · CATufts University · USUniversity of Illinois Chicago · US

Funding

Cytoskeletal Interactions of Human Dlg ProteinR01CA094414 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHISHTI, ATHAR H. · 2002 to 2006
$1.4M
CIHRNCI NIH HHS CA094414NCI NIH HHS R01 CA094414Wellcome Trust
6 · The paper itself

Abstract

Phosphatidylinositol 3,4,5-triphosphate (PIP3) plays a key role in neuronal polarization and axon formation. PIP3-containing vesicles are transported to axon tips by the kinesin KIF13B via an adaptor protein, centaurin α1 (CENTA1). KIF13B interacts with CENTA1 through its forkhead-associated (FHA) domain. We solved the crystal structures of CENTA1 in ligand-free, KIF13B-FHA domain-bound, and PIP3 head group (IP4)-bound conformations, and the CENTA1/KIF13B-FHA/IP4 ternary complex. The first pleckstrin homology (PH) domain of CENTA1 specifically binds to PIP3, while the second binds to both PIP3 and phosphatidylinositol 3,4-biphosphate (PI(3,4)P(2)). The FHA domain of KIF13B interacts with the PH1 domain of one CENTA1 molecule and the ArfGAP domain of a second CENTA1 molecule in a threonine phosphorylation-independent fashion. We propose that full-length KIF13B and CENTA1 form heterotetramers that can bind four phosphoinositide molecules in the vesicle and transport it along the microtubule.

Indexed as

Models, MolecularProtein ConformationAdaptor Proteins, Signal TransducingAxonsBiological TransportCalorimetryChromatography, AffinityChromatography, GelCloning, MolecularComputational BiologyCrystallographyElectrophoresis, Polyacrylamide GelGlutathione TransferaseHumansKinesinsModels, ChemicalADAP1 protein, humanAdaptor Proteins, Signal TransducingGlutathione TransferaseKIF13B protein, humanKinesinsNerve Tissue Proteinsphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol Phosphates

Identifiers

PMID21057110
PMCPMC2996657
OpenAlexW1988243126

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.