Evidence map›Paper›PMID 25477521›Full record

ArticleThe Journal of biological chemistry2015

A lettuce (Lactuca sativa) homolog of human Nogo-B receptor interacts with cis-prenyltransferase and is necessary for natural rubber biosynthesis.

Yang Qu, Romit Chakrabarty, Hue T Tran, Eun-Joo G Kwon, Moonhyuk Kwon, Trinh-Don Nguyen, Dae-Kyun Ro

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.1field-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

46 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
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  7. The cis-prenyltransferase protein family in Taraxacum koksaghyz.The Plant journal : for cell and molecular biology · 2025
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  11. Review
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  18. Genome-wide detection and classification of terpene synthase genes inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  19. Article
  20. 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

7 authors at 1 institution in 1 country.

Yang QuFrom the Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada.
Romit ChakrabartyFrom the Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada.
Hue T TranFrom the Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada.
Eun-Joo G KwonFrom the Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada.
Moonhyuk KwonFrom the Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada.
Trinh-Don NguyenFrom the Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada.
Dae-Kyun RoFrom the Department of Biological Sciences, University of Calgary, Calgary, Alberta T2N 1N4, Canada daekyun.ro@ucalgary.ca.
University of Calgary · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural rubber (cis-1,4-polyisoprene) is an indispensable biopolymer used to manufacture diverse consumer products. Although a major source of natural rubber is the rubber tree (Hevea brasiliensis), lettuce (Lactuca sativa) is also known to synthesize natural rubber. Here, we report that an unusual cis-prenyltransferase-like 2 (CPTL2) that lacks the conserved motifs of conventional cis-prenyltransferase is required for natural rubber biosynthesis in lettuce. CPTL2, identified from the lettuce rubber particle proteome, displays homology to a human NogoB receptor and is predominantly expressed in latex. Multiple transgenic lettuces expressing CPTL2-RNAi constructs showed that a decrease of CPTL2 transcripts (3-15% CPTL2 expression relative to controls) coincided with the reduction of natural rubber as low as 5%. We also identified a conventional cis-prenyltransferase 3 (CPT3), exclusively expressed in latex. In subcellular localization studies using fluorescent proteins, cytosolic CPT3 was relocalized to endoplasmic reticulum by co-occurrence of CPTL2 in tobacco and yeast at the log phase. Furthermore, yeast two-hybrid data showed that CPTL2 and CPT3 interact. Yeast microsomes containing CPTL2/CPT3 showed enhanced synthesis of short cis-polyisoprenes, but natural rubber could not be synthesized in vitro. Intriguingly, a homologous pair CPTL1/CPT1, which displays ubiquitous expressions in lettuce, showed a potent dolichol biosynthetic activity in vitro. Taken together, our data suggest that CPTL2 is a scaffolding protein that tethers CPT3 on endoplasmic reticulum and is necessary for natural rubber biosynthesis in planta, but yeast-expressed CPTL2 and CPT3 alone could not synthesize high molecular weight natural rubber in vitro.

Indexed as

AgrobacteriumAmino Acid SequenceChromatography, Thin LayerDNAEndoplasmic ReticulumGreen Fluorescent ProteinsHeveaLactucaLatexMicroscopy, ConfocalMicrosomesMolecular Sequence DataMolecular WeightNicotianaPhenotypePlant Proteinscis-prenyl transferaseDNAGreen Fluorescent ProteinsLatexPlant ProteinsReceptors, Cell SurfaceRubberTransferasescis-Prenyltransferase, RNA InterferenceEnzyme CatalysisLettuceNatural RubberPlant BiochemistryProtein ComplexProteomicsTerpenoid

Identifiers

PMID25477521
PMCPMC4303647
OpenAlexW1992314154

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.