Evidence map›Paper›PMID 31275332›Full record

ReviewFrontiers in plant science2019

Chloroplast Protein Degradation in Senescing Leaves: Proteases and Lytic Compartments.

Agustina Buet, M Lorenza Costa, Dana E Martínez, Juan J Guiamet

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in plant science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 57 citations in OpenAlex.

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  12. Characterization and expression analysis ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2022
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  17. HCells · 2019
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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

4 authors at 2 institutions in 1 country.

Agustina BuetInstituto de Fisiología Vegetal (INFIVE, CONICET-UNLP), La Plata, Argentina.
M Lorenza CostaInstituto de Fisiología Vegetal (INFIVE, CONICET-UNLP), La Plata, Argentina.
Dana E MartínezInstituto de Fisiología Vegetal (INFIVE, CONICET-UNLP), La Plata, Argentina.
Juan J GuiametInstituto de Fisiología Vegetal (INFIVE, CONICET-UNLP), La Plata, Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARInstituto de Fisiología Vegetal · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leaf senescence is characterized by massive degradation of chloroplast proteins, yet the protease(s) involved is(are) not completely known. Increased expression and/or activities of serine, cysteine, aspartic, and metalloproteases were detected in senescing leaves, but these studies have not provided information on the identities of the proteases responsible for chloroplast protein breakdown. Silencing some senescence-associated proteases has delayed progression of senescence symptoms, yet it is still unclear if these proteases are directly involved in chloroplast protein breakdown. At least four cellular pathways involved in the traffic of chloroplast proteins for degradation outside the chloroplast have been described (i.e., "Rubisco-containing bodies," "senescence-associated vacuoles," "ATI1-plastid associated bodies," and "CV-containing vesicles"), which differ in their dependence on the autophagic machinery, and the identity of the proteins transported and/or degraded. Finding out the proteases involved in, for example, the degradation of Rubisco, may require piling up mutations in several senescence-associated proteases. Alternatively, targeting a proteinaceous protein inhibitor to chloroplasts may allow the inhibitor to reach "Rubisco-containing bodies," "senescence-associated vacuoles," "ATI1-plastid associated bodies," and "CV-containing vesicles" in essentially the way as chloroplast-targeted fluorescent proteins re-localize to these vesicular structures. This might help to reduce proteolytic activity, thereby reducing or slowing down plastid protein degradation during senescence.

Indexed as

chloroplast protein degradationleaf senescenceproteaseSAG12senescence-associated vacuolesvacuole

Identifiers

PMID31275332
PMCPMC6593067
OpenAlexW2951017637

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.