Evidence map›Paper›PMID 26917684›Full record

ArticlePlant physiology2016

Composition, Assembly, and Trafficking of a Wheat Xylan Synthase Complex.

Nan Jiang, Richard E Wiemels, Aaron Soya, Rebekah Whitley, Michael Held, Ahmed Faik

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
16.4field-weighted citation impact, top 1% 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

24 citing papers in PubMed, 55 citations in OpenAlex.

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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 1 institution in 1 country.

Nan JiangDepartment of Environmental and Plant Biology (N.J., R.E.W., A.S., R.W., A.F.) and Department of Chemistry and Biochemistry (M.H.), Ohio University, Athens, Ohio 45701.
Richard E WiemelsDepartment of Environmental and Plant Biology (N.J., R.E.W., A.S., R.W., A.F.) and Department of Chemistry and Biochemistry (M.H.), Ohio University, Athens, Ohio 45701.
Aaron SoyaDepartment of Environmental and Plant Biology (N.J., R.E.W., A.S., R.W., A.F.) and Department of Chemistry and Biochemistry (M.H.), Ohio University, Athens, Ohio 45701.
Rebekah WhitleyDepartment of Environmental and Plant Biology (N.J., R.E.W., A.S., R.W., A.F.) and Department of Chemistry and Biochemistry (M.H.), Ohio University, Athens, Ohio 45701.
Michael HeldDepartment of Environmental and Plant Biology (N.J., R.E.W., A.S., R.W., A.F.) and Department of Chemistry and Biochemistry (M.H.), Ohio University, Athens, Ohio 45701.
Ahmed FaikDepartment of Environmental and Plant Biology (N.J., R.E.W., A.S., R.W., A.F.) and Department of Chemistry and Biochemistry (M.H.), Ohio University, Athens, Ohio 45701 faik@ohio.edu.
Ohio University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xylans play an important role in plant cell wall integrity and have many industrial applications. Characterization of xylan synthase (XS) complexes responsible for the synthesis of these polymers is currently lacking. We recently purified XS activity from etiolated wheat (Triticum aestivum) seedlings. To further characterize this purified activity, we analyzed its protein composition and assembly. Proteomic analysis identified six main proteins: two glycosyltransferases (GTs) TaGT43-4 and TaGT47-13; two putative mutases (TaGT75-3 and TaGT75-4) and two non-GTs; a germin-like protein (TaGLP); and a vernalization related protein (TaVER2). Coexpression of TaGT43-4, TaGT47-13, TaGT75-3, and TaGT75-4 in Pichia pastoris confirmed that these proteins form a complex. Confocal microscopy showed that all these proteins interact in the endoplasmic reticulum (ER) but the complexes accumulate in Golgi, and TaGT43-4 acts as a scaffold protein that holds the other proteins. Furthermore, ER export of the complexes is dependent of the interaction between TaGT43-4 and TaGT47-13. Immunogold electron microscopy data support the conclusion that complex assembly occurs at specific areas of the ER before export to the Golgi. A di-Arg motif and a long sequence motif within the transmembrane domains were found conserved at the NH2-terminal ends of TaGT43-4 and homologous proteins from diverse taxa. These conserved motifs may control the forward trafficking of the complexes and their accumulation in the Golgi. Our findings indicate that xylan synthesis in grasses may involve a new regulatory mechanism linking complex assembly with forward trafficking and provide new insights that advance our understanding of xylan biosynthesis and regulation in plants.

Indexed as

Amino Acid MotifsAmino Acid SequenceConserved SequenceEndoplasmic ReticulumGolgi ApparatusImmunoblottingIntracellular SpaceLikelihood FunctionsMicrosomesMultienzyme ComplexesMultigene FamilyNicotianaPentosyltransferasesPhylogenyPichiaPlant Epidermis1,4-beta-D-xylan synthaseMultienzyme ComplexesPentosyltransferasesPlant ProteinsProtein Sorting SignalsRecombinant Fusion Proteins

Identifiers

PMID26917684
PMCPMC4825154
OpenAlexW2281583904

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.