2016
DOI: 10.1016/j.bbrc.2016.01.145
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Arabidopsis tRNA ligase completes the cytoplasmic splicing of bZIP60 mRNA in the unfolded protein response

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Cited by 26 publications
(27 citation statements)
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“…The pAtRNL::cAtRNL‐sYFP construct used carries the claimed both first and second translation initiation sites. Consistent with our observations, another biochemical analysis also showed that AtRNL is localized primarily in the soluble fraction of the cell extracts (Nagashima et al ). In addition, transgenic expression of the claimed shorter version of cAtRNL under the control of the CaMV 35S promoter is effective and sufficient to complement the zyg3 mutant (Nagashima et al ).…”
Section: Discussionsupporting
confidence: 92%
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“…The pAtRNL::cAtRNL‐sYFP construct used carries the claimed both first and second translation initiation sites. Consistent with our observations, another biochemical analysis also showed that AtRNL is localized primarily in the soluble fraction of the cell extracts (Nagashima et al ). In addition, transgenic expression of the claimed shorter version of cAtRNL under the control of the CaMV 35S promoter is effective and sufficient to complement the zyg3 mutant (Nagashima et al ).…”
Section: Discussionsupporting
confidence: 92%
“…Consistent with our observations, another biochemical analysis also showed that AtRNL is localized primarily in the soluble fraction of the cell extracts (Nagashima et al ). In addition, transgenic expression of the claimed shorter version of cAtRNL under the control of the CaMV 35S promoter is effective and sufficient to complement the zyg3 mutant (Nagashima et al ). We therefore suggest that the unexpected localizations observed by Englert et al () may have been caused by over‐accumulation of GFP when expressed under the control of CaMV 35S promoter.…”
Section: Discussionsupporting
confidence: 92%
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“…In Arabidopsis ( Arabidopsis thaliana ), two basic leucine zipper (bZIP) transcription factors, bZIP60 and bZIP28, have been known to induce ER chaperone gene expression (Angelos, Ruberti, Kim, & Brandizzi, ; Howell, ; Iwata & Koizumi, ). bZIP60 is activated by cytoplasmic splicing through the ER membrane‐localized kinase/ribonuclease IRE1 and the tRNA ligase Rlg1(Deng et al., ; Nagashima, Iwata, Mishiba, & Koizumi, ; Nagashima et al., ). bZIP28 is an ER membrane‐bound transcription factor that is activated by proteolysis within its transmembrane domain by the Golgi‐localized metalloprotease site‐2 protease (S2P) (Iwata et al., ; Srivastava, Chen, Deng, Brandizzi, & Howell, ).…”
Section: Introductionmentioning
confidence: 99%
“…Upon IRE1A or/and IRE1B activation by ER stress, a 23-bp fragment of bZIP60 U is spliced out to generate the spliced bZIP60 (bZIP60 S)142628. The cleaved 5′ and 3′ fragments can be rejoined in vitro by the Arabidopsis tRNA ligase RLG129. The bZIP60 S protein differs in bZIP60 U by lacking the single transmembrane domain (TMD) and thus becomes an active transcription factor that up-regulates the UPR target genes142628.…”
mentioning
confidence: 99%