Evidence map›Paper›PMID 17142567›Full record

ArticleEukaryotic cell2007

Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III activity and chitin chain length.

Kariona A Grabińska, Paula Magnelli, Phillips W Robbins

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Role of paracoccin onVirulence · 2023
    Article
  5. Article
  6. Chitin Synthesis in Yeast: A Matter of Trafficking.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
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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

3 authors at 1 institution in 1 country.

Kariona A GrabińskaDepartment of Molecular and Cell Biology, School of Dental Medicine, Boston University, 715 Albany Street, Evans 408, Boston, MA 02118, USA. karionag@bu.edu
Paula Magnelli
Phillips W Robbins
Boston University · US

Funding

ROBBINS Glycosylation and Glycosidases-Cell and Molecular BiologyR01GM031318 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAMUELSON, JOHN C. · 1985 to 2011
$4.1M
PROTEIN GLYCOSYLATION - CELLULAR AND MOLECULAR BIOLOGYR37GM031318 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ROBBINS, PHILLIPS W · 1988 to 1997
–
NIGMS NIH HHS GM31318NIGMS NIH HHS R01 GM031318
6 · The paper itself

Abstract

Chs4p (Cal2/Csd4/Skt5) was identified as a protein factor physically interacting with Chs3p, the catalytic subunit of chitin synthase III (CSIII), and is indispensable for its enzymatic activity in vivo. Chs4p contains a putative farnesyl attachment site at the C-terminal end (CVIM motif) conserved in Chs4p of Saccharomyces cerevisiae and other fungi. Several previous reports questioned the role of Chs4p prenylation in chitin biosynthesis. In this study we reinvestigated the function of Chs4p prenylation. We provide evidence that Chs4p is farnesylated by showing that purified Chs4p is recognized by anti-farnesyl antibody and is a substrate for farnesyl transferase (FTase) in vitro and that inactivation of FTase increases the amount of unmodified Chs4p in yeast cells. We demonstrate that abolition of Chs4p prenylation causes a approximately 60% decrease in CSIII activity, which is correlated with a approximately 30% decrease in chitin content and with increased resistance to the chitin binding compound calcofluor white. Furthermore, we show that lack of Chs4p prenylation decreases the average chain length of the chitin polymer. Prenylation of Chs4p, however, is not a factor that mediates plasma membrane association of the protein. Our results provide evidence that the prenyl moiety attached to Chs4p is a factor modulating the activity of CSIII both in vivo and in vitro.

Indexed as

Gene Expression Regulation, FungalProtein PrenylationChitinChitin SynthaseFungal ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubcellular FractionsChitinChitin SynthaseFungal ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID17142567
PMCPMC1797950
OpenAlexW2133630735

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.