Evidence map›Paper›PMID 11160821›Full record

ArticleMolecular biology of the cell2001

Vps41p function in the alkaline phosphatase pathway requires homo-oligomerization and interaction with AP-3 through two distinct domains.

T Darsow, D J Katzmann, C R Cowles, S D Emr

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

44 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Adaptor protein-3 produces synaptic vesicles that release phasic dopamine.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Article
  8. TbVps41 regulates trafficking of endocytic but not biosynthetic cargo to lysosomes of bloodstream forms of Trypanosoma brucei.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. The Role of Deubiquitinating Enzymes in the Various Forms of Autophagy.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Chaperoning SNARE assembly and disassembly.Nature reviews. Molecular cell biology · 2016
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  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

4 authors at 2 institutions in 1 country.

T DarsowDepartment of Cellular and Molecular Medicine and Division of Biology, Howard Hughes Medical Institute, University of California, San Diego, School of Medicine, La Jolla, California 92093-0668, USA.
D J Katzmann
C R Cowles
S D Emr
Howard Hughes Medical Institute · USUniversity of California, San Diego · US

Funding

VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI BALCH, WILLIAM E · 1993 to 2002
$5.0M
NCI NIH HHS CA58689
6 · The paper itself

Abstract

Transport of proteins through the ALP (alkaline phosphatase) pathway to the vacuole requires the function of the AP-3 adaptor complex and Vps41p. However, unlike other adaptor protein-dependent pathways, the ALP pathway has not been shown to require additional accessory proteins or coat proteins, such as membrane recruitment factors or clathrin. Two independent genetic approaches have been used to identify new mutants that affect transport through the ALP pathway. These screens yielded new mutants in both VPS41 and the four AP-3 subunit genes. Two new VPS41 alleles exhibited phenotypes distinct from null mutants of VPS41, which are defective in vacuolar morphology and protein transport through both the ALP and CPY sorting pathways. The new alleles displayed severe ALP sorting defects, normal vacuolar morphology, and defects in ALP vesicle formation at the Golgi complex. Sequencing analysis of these VPS41 alleles revealed mutations encoding amino acid changes in two distinct domains of Vps41p: a conserved N-terminal domain and a C-terminal clathrin heavy-chain repeat (CHCR) domain. We demonstrate that the N-terminus of Vps41p is required for binding to AP-3, whereas the C-terminal CHCR domain directs homo-oligomerization of Vps41p. These data indicate that a homo-oligomeric form of Vps41p is required for the formation of ALP containing vesicles at the Golgi complex via interactions with AP-3.

Indexed as

Monomeric Clathrin Assembly ProteinsNuclear ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAdaptor Proteins, Vesicular TransportAlkaline PhosphataseAllelesAmino Acid SequenceBinding SitesCarrier ProteinsClathrinClathrin Heavy ChainsDimerizationFungal ProteinsMembrane ProteinsMolecular Sequence DataAdaptor Proteins, Vesicular TransportAlkaline PhosphataseCarrier ProteinsClathrinclathrin assembly protein AP180Clathrin Heavy ChainsFungal ProteinsMembrane ProteinsMonomeric Clathrin Assembly ProteinsNPL3 protein, S cerevisiaeNuclear ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsVPS41 protein, S cerevisiae

Identifiers

PMID11160821
PMCPMC30566
OpenAlexW2159424335

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.