Loss of GET pathway orthologs in
            <i>Arabidopsis thaliana</i>
            causes root hair growth defects and affects SNARE abundance

Xing, Shuping; Mehlhorn, Dietmar Gerald; Wallmeroth, Niklas; Asseck, Lisa Yasmin; Kar, Ritwika; Voss, Alessa; Denninger, Philipp; Schmidt, Vanessa A. F.; Schwarzländer, Markus; Stierhof, York‐Dieter; Großmann, Guido; Grefen, Christopher

doi:10.1073/pnas.1619525114

Cited by 54 publications

(119 citation statements)

References 70 publications

(79 reference statements)

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“…It was therefore surprising that mutants of get3 in Saccharomyces cerevisiae or Arabidopsis thaliana did not show any global growth defects [51]. Moreover, while many different TA proteins were found to employ the Get3/TRC40 system for successful membrane targeting in vitro , in vivo studies in yeast or tissue-specific knockout mice failed to identify more than a handful of proteins that show targeting defects [52].…”

Section: Get3: the Link To Redox-regulated Chaperones In Eukaryotesmentioning

confidence: 99%

Stress-Activated Chaperones: A First Line of Defense

Voth

Jakob

2017

Trends in Biochemical Sciences

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Proteins are constantly challenged by environmental stress conditions that threaten their structure and function. Especially problematic are oxidative, acid, or severe heat stress, which induce very rapid and widespread protein unfolding and generate conditions that make canonical chaperones and/or transcriptional responses inadequate to protect the proteome. Here, we review recent advances in identifying and characterizing stress-activated chaperones, which are inactive under non-stress conditions but become potent chaperones under specific protein-unfolding stress conditions. We discuss the posttranslational mechanisms by which these chaperones sense stress and consider the role intrinsic disorder plays in their regulation and function. We examine their physiological roles under both non-stress and stress conditions, their integration into the cellular proteostasis network, and their potential as novel therapeutic targets.

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Section: Get3: the Link To Redox-regulated Chaperones In Eukaryotesmentioning

confidence: 99%

Stress-Activated Chaperones: A First Line of Defense

Voth

Jakob

2017

Trends in Biochemical Sciences

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“…Although such Get3 homologs are also found in land plants, their function remains unknown. Moreover, land plants, Chlorophytes and red algae have been proposed or shown to have several Get3 homologs without an α‐crystallin domain as well, some of them in chloroplasts and mitochondria …”

Section: Structural Organization Of Arsa and Get3 Proteinsmentioning

confidence: 99%

“…Indeed, because the C‐terminal TMS of a TA protein emerges from the ribosome at the end of translation, TA proteins are targeted and inserted through post‐translational mechanisms. One such pathway, the guided entry of TA proteins (GET), identified a little over 10 years ago, has been shown to mediate the proper delivery of several TA proteins in mammals, budding yeast and more recently in plants …”

Section: Introductionmentioning

confidence: 99%

“…Despite the apparent complexity and necessity of the GET pathway to prevent aggregation of hydrophobic proteins, depletion of GET pathway components in budding yeast ( Saccharomyces cerevisiae ) and Arabidopsis thaliana is not lethal . Yet the functional importance of the GET pathway is highlighted by the fact that GET pathway deletion S. cerevisiae strains show increased heat and oxidative stress sensitivity, and the depletion of TRC40 is embryonically lethal in mice .…”

Section: Introductionmentioning

confidence: 99%

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The natural history of Get3‐like chaperones

Farkas

Laurentiis

Schwappach

2019

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Get3 in yeast or TRC40 in mammals is an ATPase that, in eukaryotes, is a central element of the GET or TRC pathway involved in the targeting of tail‐anchored proteins. Get3 has also been shown to possess chaperone holdase activity. A bioinformatic assessment was performed across all domains of life on functionally important regions of Get3 including the TRC40‐insert and the hydrophobic groove essential for tail‐anchored protein binding. We find that such a hydrophobic groove is much more common in bacterial Get3 homologs than previously appreciated based on a directed comparison of bacterial ArsA and yeast Get3. Furthermore, our analysis shows that the region containing the TRC40‐insert varies in length and methionine content to an unexpected extent within eukaryotes and also between different phylogenetic groups. In fact, since the TRC40‐insert is present in all domains of life, we suggest that its presence does not automatically predict a tail‐anchored protein targeting function. This opens up a new perspective on the function of organellar Get3 homologs in plants which feature the TRC40‐insert but have not been demonstrated to function in tail‐anchored protein targeting. Our analysis also highlights a large diversity of the ways Get3 homologs dimerize. Thus, based on the structural features of Get3 homologs, these proteins may have an unexplored functional diversity in all domains of life.

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“…Posttranslational insertion is required for a class of tail-anchored (TA) proteins, which are characterized by a transmembrane domain (TMD) near their C terminus, for their correct targeting to the destined membrane (1). In PNAS, Xing et al uncover a pathway for TA protein insertion into the endoplasmic reticulum (ER) in the model plant Arabidopsis thaliana, which plays an unexpected role in root hair growth (2). The authors identify several key components in the guided entry of tail-anchored protein (GET) complex that has a conserved function in regulating TA protein insertion.…”

mentioning

confidence: 99%