Evidence map›Paper›PMID 19010779›Full record

ArticleThe Journal of biological chemistry2009

Hermansky-Pudlak syndrome protein complexes associate with phosphatidylinositol 4-kinase type II alpha in neuronal and non-neuronal cells.

Gloria Salazar, Stephanie Zlatic, Branch Craige, Andrew A Peden, Jan Pohl, Victor Faundez

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Genetic dissection of theMolecular biology of the cell · 2025
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Melanosome Biogenesis in the Pigmentation of Mammalian Skin.Integrative and comparative biology · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. GABARAPs regulate PI4P-dependent autophagosome:lysosome fusion.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. Article

3 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

6 authors.

Gloria SalazarDepartment of Cell Biology and Medicine, Emory University, Atlanta, Georgia 30322, USA.
Stephanie Zlatic
Branch Craige
Andrew A Peden
Jan Pohl
Victor Faundez

Funding

Cellular Mechanisms of Neuronal Metal Transport and ToxicityR01GM077569 · NIGMS · EMORY UNIVERSITY · PI FAUNDEZ, VICTOR · 2006 to 2016
$2.6M
Mechanisms of Endosome Trafficking in NeuronsR01NS042599 · NINDS · EMORY UNIVERSITY · PI FAUNDEZ, VICTOR · 2003 to 2012
$2.5M
Mechanisms of Endosome Trafficking in NeuronsR56NS042599 · NINDS · EMORY UNIVERSITY · PI FAUNDEZ, VICTOR · 2008 to 2008
$339k
NIGMS NIH HHS GM 077569NIGMS NIH HHS R01 GM077569NINDS NIH HHS NS42599NINDS NIH HHS R01 NS042599NINDS NIH HHS R56 NS042599
6 · The paper itself

Abstract

The Hermansky-Pudlak syndrome is a disorder affecting endosome sorting. Disease is triggered by defects in any of 15 mouse gene products, which are part of five distinct cytosolic molecular complexes: AP-3, homotypic fusion and vacuole protein sorting, and BLOC-1, -2, and -3. To identify molecular associations of these complexes, we used in vivo cross-linking followed by purification of cross-linked AP-3 complexes and mass spectrometric identification of associated proteins. AP-3 was co-isolated with BLOC-1, BLOC-2, and homotypic fusion and vacuole protein sorting complex subunits; clathrin; and phosphatidylinositol-4-kinase type II alpha (PI4KIIalpha). We previously reported that this membrane-anchored enzyme is a regulator of AP-3 recruitment to membranes and a cargo of AP-3 ( Craige, B., Salazar, G., and Faundez, V. (2008) Mol. Biol. Cell 19, 1415-1426 ). Using cells deficient in different Hermansky-Pudlak syndrome complexes, we identified that BLOC-1, but not BLOC-2 or BLOC-3, deficiencies affect PI4KIIalpha inclusion into AP-3 complexes. BLOC-1, PI4KIIalpha, and AP-3 belong to a tripartite complex, and down-regulation of either PI4KIIalpha, BLOC-1, or AP-3 complexes led to similar LAMP1 phenotypes. Our analysis indicates that BLOC-1 complex modulates the association of PI4KIIalpha with AP-3. These results suggest that AP-3 and BLOC-1 act, either in concert or sequentially, to specify sorting of PI4KIIalpha along the endocytic route.

Indexed as

Adaptor Protein Complex 3AnimalsEndocytosisEndosomesHermanski-Pudlak SyndromeHumansMembrane ProteinsMiceMultiprotein ComplexesNeuronsPhosphotransferases (Alcohol Group Acceptor)Adaptor Protein Complex 3HPS1 protein, humanHps1 protein, mouseMembrane ProteinsMultiprotein ComplexesPhosphotransferases (Alcohol Group Acceptor)PIP4K2A protein, human

Identifiers

PMID19010779
PMCPMC2615517

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.