Literature DB >> 27257966

Correction: Caenorhabditis elegans PAQR-2 and IGLR-2 Protect against Glucose Toxicity by Modulating Membrane Lipid Composition.

Emma Svensk, Ranjan Devkota, Marcus Ståhlman, Parmida Ranji, Manish Rauthan, Fredrik Magnusson, Sofia Hammarsten, Maja Johansson, Jan Borén, Marc Pilon.   

Abstract

[This corrects the article DOI: 10.1371/journal.pgen.1005982.].

Entities:  

Year:  2016        PMID: 27257966      PMCID: PMC4892886          DOI: 10.1371/journal.pgen.1006112

Source DB:  PubMed          Journal:  PLoS Genet        ISSN: 1553-7390            Impact factor:   5.917


Some ORF names, lengths and mutations in Table 1 are incorrect. Specifically, the ORF names and ORF lengths listed for the paqr-2(et36) and paqr-2(et35) alleles, and the ORF names and mutations listed for the iglr-2(et34), iglr-2(et37) and iglr-2(et38) alleles. The shift by one amino acid position in the mutation column also applies to the iglr-2 mutations indicated in Fig 2. Please see the corrected Table 1 and Fig 2 here.
Table 1

Description of the novel paqr-2 and iglr-2 alleles.

Gene(allele)ORF nameORF lengthMutation
paqr-2(et36)Y32H12A.5581 aaD(GAT)282N(AAT)
paqr-2(et35)Y32H12A.5581 aaG(GGA)533R(AGA)
iglr-2(et34)ZC262.3a773 aaW(TGG)84STOP(TAG)
iglr-2(et37)ZC262.3a773 aaG(GGT)498D(GAT)
iglr-2(et38)ZC262.3a773 aaQ(CAA)594STOP(TAA)
Fig 2

Novel alleles of PAQR-2 and IGLR-2, and interaction of IGLR-2 with PAQR-2.

(A) Schematic structures of the IGLR-2 and PAQR-2 proteins, with novel mutations indicated by red arrowheads. The VC155 and VN173 fragments added to the C and N terminal ends of IGLR-2 and PAQR-2, respectively, allows reconstitution of a full and fluorescent VENUS YFP protein if the two proteins come into close proximity. (B) Result of the BiFC experiment showing that IGLR-2 and PAQR-2 contact each other on cellular membranes. The top two panels show a transgenic worm co-expressing the fusion proteins depicted in (A); note the clear membrane-localized fluorescence indicative of IGLR-2 and PAQR-2 interaction. The middle two panels show a transgenic worm co-expressing the tagged IGLR-2 and a tagged PAQR-1 protein; note that only autofluorescent gut granules emit a signal, indicating that IGLR-2 and PAQR-1 do not interact with each other. The bottom two panels show a transgenic animal carrying the two empty vectors used in the BiFC experiments; note again that only autofluorescent gut granules emit a signal.

Novel alleles of PAQR-2 and IGLR-2, and interaction of IGLR-2 with PAQR-2.

(A) Schematic structures of the IGLR-2 and PAQR-2 proteins, with novel mutations indicated by red arrowheads. The VC155 and VN173 fragments added to the C and N terminal ends of IGLR-2 and PAQR-2, respectively, allows reconstitution of a full and fluorescent VENUS YFP protein if the two proteins come into close proximity. (B) Result of the BiFC experiment showing that IGLR-2 and PAQR-2 contact each other on cellular membranes. The top two panels show a transgenic worm co-expressing the fusion proteins depicted in (A); note the clear membrane-localized fluorescence indicative of IGLR-2 and PAQR-2 interaction. The middle two panels show a transgenic worm co-expressing the tagged IGLR-2 and a tagged PAQR-1 protein; note that only autofluorescent gut granules emit a signal, indicating that IGLR-2 and PAQR-1 do not interact with each other. The bottom two panels show a transgenic animal carrying the two empty vectors used in the BiFC experiments; note again that only autofluorescent gut granules emit a signal.
  1 in total

1.  Caenorhabditis elegans PAQR-2 and IGLR-2 Protect against Glucose Toxicity by Modulating Membrane Lipid Composition.

Authors:  Emma Svensk; Ranjan Devkota; Marcus Ståhlman; Parmida Ranji; Manish Rauthan; Fredrik Magnusson; Sofia Hammarsten; Maja Johansson; Jan Borén; Marc Pilon
Journal:  PLoS Genet       Date:  2016-04-15       Impact factor: 5.917

  1 in total

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