Corrigendum to: Nup42 and IP 6 coordinate Gle1 stimulation of Dbp5/DDX19B for mRNA export in yeast and human cells (Traffic, (2017), 18, 12, (776-790), 10.1111/tra.12526)

Rebecca L. Adams, Aaron C. Mason, Laura Glass, Aditi, Susan R. Wente

Research output: Contribution to journalComment/debatepeer-review

Abstract

The authors wish to replace Figure in their paper with the figure below. Figure panel C is incorrectly labeled in the original and is corrected here. (Figure presented.) hGle1B interactions with hNup42 and IP6 enhances stimulation of DDX19B activity and are required for mRNA export. (A) Purified recombinant human proteins used in ATPase assays. 1 μg indicated purified proteins were resolved by SDS-PAGE and Coomassie stained. (B) hGle1B and hNup42 stimulate DDX19B ATPase activity in absence of IP6. PK/LDH-coupled ATPase assays were performed with H6-DDX19B (500 nM, expressed in insect cells) in the presence of 1 μM A30 RNA and 2 mM ATP. hgle1B-CTD or hgle1B-CTDQKED > AAAA (250 nM), IP6 (1 μM), and varying amounts of hnup42-CTD (250, 500, or 750 nM) were added as indicated. Reactions preformed as in Figure 3D. Mean shown for n = 3, and SE is indicated by error bars. (C) hGle1B-IP6 interaction is conserved in human proteins. PK/LDH-coupled ATPase assays were performed with H6-DDX19B (500 nM) in the presence of 1 μM A30 RNA and 2 mM ATP, hgle1B-CTD, hgle1B-CTDKK > QQ, or hgle1B-CTDKKKK > QQQQ (250 nM), and hnup42-CTD (750 nM) or IP6 (1 μM) were added as indicated. Purified proteins are shown in 6A. Reactions performed as in Figure 3D. Mean shown for n = 3, and SE is indicated by error bars. (D) hGle1B-IP6 interaction is required for mRNA export. HeLa cells were transfected with vehicle or GFP-hGLE1BR, GFP-hgle1BR-KK > QQ, or GFP-hgle1BR-KKKK > QQQQ plasmids following CTRL or hGLE1 knockdown. Nuclear:cytoplasmic mean fluorescence intensity of oligo d(T) signal was quantified as in Figure 5F.

Original languageEnglish (US)
Pages (from-to)650
Number of pages1
JournalTraffic
Volume19
Issue number8
DOIs
StatePublished - Aug 2018
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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