Evidence map›Paper›PMID 35993897›Full record

ArticlePlant physiology2022

The trans-Golgi-localized protein BICAT3 regulates manganese allocation and matrix polysaccharide biosynthesis.

Jie He, Bo Yang, Gerd Hause, Nico Rössner, Tina Peiter-Volk, Martin H Schattat, Cătălin Voiniciuc, Edgar Peiter

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

5 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. 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

8 authors at 3 institutions in 2 countries.

Jie HePlant Nutrition Laboratory, Institute of Agricultural and Nutritional Sciences, Faculty of Natural Sciences III, Martin Luther University Halle-Wittenberg, Halle (Saale), 06120, Germany.ORCID 0000-0002-3177-1612
Bo YangIndependent Junior Research Group-Designer Glycans, Leibniz Institute of Plant Biochemistry, Halle (Saale), 06120, Germany.ORCID 0000-0003-4446-0415
Gerd HauseBiocentre, Martin Luther University Halle-Wittenberg, Halle (Saale), 06120, Germany.ORCID 0000-0003-0242-3923
Nico RössnerPlant Nutrition Laboratory, Institute of Agricultural and Nutritional Sciences, Faculty of Natural Sciences III, Martin Luther University Halle-Wittenberg, Halle (Saale), 06120, Germany.ORCID 0000-0002-7732-8712
Tina Peiter-VolkPlant Nutrition Laboratory, Institute of Agricultural and Nutritional Sciences, Faculty of Natural Sciences III, Martin Luther University Halle-Wittenberg, Halle (Saale), 06120, Germany.ORCID 0000-0001-9889-7415
Martin H SchattatPlant Physiology, Institute of Biology, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), 06120, Germany.ORCID 0000-0002-1995-1960
Cătălin VoiniciucIndependent Junior Research Group-Designer Glycans, Leibniz Institute of Plant Biochemistry, Halle (Saale), 06120, Germany.ORCID 0000-0001-9105-014X
Edgar PeiterPlant Nutrition Laboratory, Institute of Agricultural and Nutritional Sciences, Faculty of Natural Sciences III, Martin Luther University Halle-Wittenberg, Halle (Saale), 06120, Germany.ORCID 0000-0002-9104-3238
Martin Luther University Halle-Wittenberg · DELeibniz Institute of Plant Biochemistry · DEUniversity of Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Manganese (Mn2+) is essential for a diversity of processes, including photosynthetic water splitting and the transfer of glycosyl moieties. Various Golgi-localized glycosyltransferases that mediate cell wall matrix polysaccharide biosynthesis are Mn2+ dependent, but the supply of these enzymes with Mn2+ is not well understood. Here, we show that the BIVALENT CATION TRANSPORTER 3 (BICAT3) localizes specifically to trans-cisternae of the Golgi. In agreement with a role in Mn2+ and Ca2+ homeostasis, BICAT3 rescued yeast (Saccharomyces cerevisiae) mutants defective in their translocation. Arabidopsis (Arabidopsis thaliana) knockout mutants of BICAT3 were sensitive to low Mn2+ and high Ca2+ availability and showed altered accumulation of these cations. Despite reduced cell expansion and leaf size in Mn2+-deficient bicat3 mutants, their photosynthesis was improved, accompanied by an increased Mn content of chloroplasts. Growth defects of bicat3 corresponded with an impaired glycosidic composition of matrix polysaccharides synthesized in the trans-Golgi. In addition to the vegetative growth defects, pollen tube growth of bicat3 was heterogeneously aberrant. This was associated with a severely reduced and similarly heterogeneous pectin deposition and caused diminished seed set and silique length. Double mutant analyses demonstrated that the physiological relevance of BICAT3 is distinct from that of ER-TYPE CA2+-ATPASE 3, a Golgi-localized Mn2+/Ca2+-ATPase. Collectively, BICAT3 is a principal Mn2+ transporter in the trans-Golgi whose activity is critical for specific glycosylation reactions in this organelle and for the allocation of Mn2+ between Golgi apparatus and chloroplasts.

Indexed as

Arabidopsis ProteinsGolgi Matrix ProteinsManganeseArabidopsisCalciumCalcium-Transporting ATPasesCationsGolgi ApparatusPolysaccharidesSaccharomyces cerevisiaeArabidopsis ProteinsCalciumCalcium-Transporting ATPasesCationsGolgi Matrix ProteinsManganesePolysaccharides

Identifiers

PMID35993897
PMCPMC9706472
OpenAlexW4292649608

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.