Evidence map›Paper›PMID 24917610›Full record

ArticleMolecular & cellular proteomics : MCP2014

The global phosphoproteome of Chlamydomonas reinhardtii reveals complex organellar phosphorylation in the flagella and thylakoid membrane.

Hongxia Wang, Brian Gau, William O Slade, Matthew Juergens, Ping Li, Leslie M Hicks

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

57 citing papers in PubMed, 129 citations in OpenAlex.

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  19. The short flagella 1 (SHF1) gene inMolecular biology of the cell · 2022
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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

6 authors at 4 institutions in 2 countries.

Hongxia WangFrom the ‡Donald Danforth Plant Science Center, 975 North Warson Road, St Louis, Missouri 63132; §National Center of Biomedical Analysis, 27 Taiping Road, Beijing, 100850, China;
Brian GauFrom the ‡Donald Danforth Plant Science Center, 975 North Warson Road, St Louis, Missouri 63132; ¶Sigma-Aldrich, 2909 Laclede Ave., St. Louis, Missouri 63103;
William O Slade‖Department of Chemistry, University of North Carolina at Chapel Hill, 125 South Road, Chapel Hill, North Carolina 27599;
Matthew Juergens**Department of Plant Biology, Michigan State University, 612 Wilson Road, East Lansing, Missouri 48824.
Ping Li§National Center of Biomedical Analysis, 27 Taiping Road, Beijing, 100850, China;
Leslie M HicksFrom the ‡Donald Danforth Plant Science Center, 975 North Warson Road, St Louis, Missouri 63132; ‖Department of Chemistry, University of North Carolina at Chapel Hill, 125 South Road, Chapel Hill, North Carolina 27599; lmhicks@unc.edu.
National Center of Biomedical Analysis · CNUniversity of North Carolina at Chapel Hill · USDonald Danforth Plant Science Center · USMichigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chlamydomonas reinhardtii is the most intensively-studied and well-developed model for investigation of a wide-range of microalgal processes ranging from basic development through understanding triacylglycerol production. Although proteomic technologies permit interrogation of these processes at the protein level and efforts to date indicate phosphorylation-based regulation of proteins in C. reinhardtii is essential for its underlying biology, characterization of the C. reinhardtii phosphoproteome has been limited. Herein, we report the richest exploration of the C. reinhardtii proteome to date. Complementary enrichment strategies were used to detect 4588 phosphoproteins distributed among every cellular component in C. reinhardtii. Additionally, we report 18,160 unique phosphopeptides at <1% false discovery rate, which comprise 15,862 unique phosphosites - 98% of which are novel. Given that an estimated 30% of proteins in a eukaryotic cell are subject to phosphorylation, we report the majority of the phosphoproteome (23%) of C. reinhardtii. Proteins in key biological pathways were phosphorylated, including photosynthesis, pigment production, carbon assimilation, glycolysis, and protein and carbohydrate metabolism, and it is noteworthy that hyperphosphorylation was observed in flagellar proteins. This rich data set is available via ProteomeXchange (ID: PXD000783) and will significantly enhance understanding of a range of regulatory mechanisms controlling a variety of cellular process and will serve as a critical resource for the microalgal community.

Indexed as

Algal ProteinsChlamydomonas reinhardtiiChromatography, LiquidFlagellaPhosphoproteinsPhosphorylationPolymersProteomicsTandem Mass SpectrometryThylakoidsTitaniumAlgal ProteinsPhosphoproteinsPolymersTitaniumtitanium dioxide

Identifiers

PMID24917610
PMCPMC4159653
OpenAlexW2114881225

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.