Evidence map›Paper›PMID 16855022›Full record

ArticleMolecular biology of the cell2006

Chs5/6 complex: a multiprotein complex that interacts with and conveys chitin synthase III from the trans-Golgi network to the cell surface.

Siraprapha Sanchatjate, Randy Schekman

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Conventional and Unconventional Protein Secretion in Yeast and Animal Cells.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  5. Article
  6. Article
  7. Chitin Synthesis in Yeast: A Matter of Trafficking.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Off the wall: The rhyme and reason ofCell surface (Amsterdam, Netherlands) · 2019
    Review
  13. Article
  14. Endosomal trafficking of yeast membrane proteins.Biochemical Society transactions · 2018
    Review
  15. Review
  16. Article
  17. 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

2 authors.

Siraprapha SanchatjateDepartment of Molecular and Cell Biology, Howard Hughes Medical Institute, Barker Hall, University of California, Berkeley, Berkeley, CA 94720, USA.
Randy Schekman

Funding

MOLECULAR STUDIES OF EUKARYOTIC CELL SURFACE GROWTHR01GM026755 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SCHEKMAN, RANDY W. · 1985 to 2005
$1.1M
NIGMS NIH HHS GM26755NIGMS NIH HHS R01 GM026755
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, the polysaccharide chitin is deposited at the mother bud junction by an integral membrane enzyme, chitin synthase 3 (Chs3p). The traffic of Chs3p to the cell surface from the trans-Golgi network (TGN) depends on two proteins, Chs5p and Chs6p, which sort selected cargo proteins into secretory vesicles. We have found that Chs5p forms a large higher-order complex of around 1 MDa with Chs6p and three Chs6 paralogs: Bch1p, Bud7p, and Bch2p. The Chs5/6 complex transiently interacts with its cargo, Chs3p, and the presence of Chs3p in the complex is dependent on every subunit. Chs5p and Chs6p have unique and crucial roles in Chs3p transport because either a chs5delta or chs6delta mutant drastically reduces the level of Chs3p bound to the remaining subunits of the complex. Bch1p and Bud7p appear to have a redundant function in Chs3p transport because deletion of both is necessary to displace Chs3p from the complex. The role of Bch2p in Chs3p binding is the least important. Chs5p is essential for structural integrity of the Chs5/6 complex and may act as a scaffold through which the other subunits assemble. Our results suggest a model of protein sorting at the TGN that involves a peripheral, possibly coat, complex that includes multiple related copies of a specificity determining subunit.

Indexed as

Adaptor Proteins, Vesicular TransportBiological TransportCarrier ProteinsCell MembraneChitin SynthaseFungal ProteinsGene Expression Regulation, FungalMultiprotein ComplexesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinstrans-Golgi NetworkAdaptor Proteins, Vesicular TransportCarrier ProteinsChitin SynthaseCHS6 protein, S cerevisiaeFungal ProteinsMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID16855022
PMCPMC1635352

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.