Evidence map›Paper›PMID 36173669›Full record

ArticleJournal of experimental botany2023

Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases.

Douglas J Orr, Alice K J Robijns, Christopher R Baker, Krishna K Niyogi, Elizabete Carmo-Silva

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  4. Rubisco kinetic acclimation at the holoenzyme level.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

5 authors at 2 institutions in 2 countries.

Douglas J OrrLancaster Environment Centre, Lancaster University, Lancaster LA1 4YQ, UK.ORCID 0000-0003-1217-537X
Alice K J RobijnsLancaster Environment Centre, Lancaster University, Lancaster LA1 4YQ, UK.ORCID 0000-0002-4271-5587
Christopher R BakerHoward Hughes Medical Institute, Department of Plant and Microbial Biology, University of California, Berkeley, CA, USA.ORCID 0000-0001-9539-4775
Krishna K NiyogiHoward Hughes Medical Institute, Department of Plant and Microbial Biology, University of California, Berkeley, CA, USA.ORCID 0000-0001-7229-2071
Elizabete Carmo-SilvaLancaster Environment Centre, Lancaster University, Lancaster LA1 4YQ, UK.ORCID 0000-0001-6059-9359
Lancaster University · GBHoward Hughes Medical Institute · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Regulating the central CO2-fixing enzyme Rubisco is as complex as its ancient reaction mechanism and involves interaction with a series of cofactors and auxiliary proteins that activate catalytic sites and maintain activity. A key component among the regulatory mechanisms is the binding of sugar phosphate derivatives that inhibit activity. Removal of inhibitors via the action of Rubisco activase is required to restore catalytic competency. In addition, specific phosphatases dephosphorylate newly released inhibitors, rendering them incapable of binding to Rubisco catalytic sites. The best studied inhibitor is 2-carboxy-d-arabinitol 1-phosphate (CA1P), a naturally occurring nocturnal inhibitor that accumulates in most species during darkness and low light, progressively binding to Rubisco. As light increases, Rubisco activase removes CA1P from Rubisco, and the specific phosphatase CA1Pase dephosphorylates CA1P to CA, which cannot bind Rubisco. Misfire products of Rubisco's complex reaction chemistry can also act as inhibitors. One example is xylulose-1,5-bisphosphate (XuBP), which is dephosphorylated by XuBPase. Here we revisit key findings related to sugar phosphate derivatives and their specific phosphatases, highlighting outstanding questions and how further consideration of these inhibitors and their role is important for better understanding the regulation of carbon assimilation.

Indexed as

Ribulose-Bisphosphate CarboxylaseTissue Plasminogen ActivatorPhosphoric Monoester HydrolasesPhosphoric Monoester HydrolasesRibulose-Bisphosphate CarboxylaseTissue Plasminogen ActivatorCA1PCA1Pasedynamic regulationRubiscoRubisco activasesugar phosphatesXuBPXuBPase

Identifiers

PMID36173669
PMCPMC9833046
OpenAlexW4297964747

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.