2015
DOI: 10.1038/ncomms7843
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Cytosolic targeting factor AKR2A captures chloroplast outer membrane-localized client proteins at the ribosome during translation

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Cited by 31 publications
(20 citation statements)
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“…Systematic functional analyses of rp paralog mutants need to account for such extra-ribosomal functions of RPs. For instance, uL23 recruits a nascent protein to its future localization in the chloroplast by coupling with its receptor ( Kim et al., 2015 ). Whether the differential uL23 paralog phenotypes are influenced by both moonlighting and ribosomal functions remains an open discussion.…”
Section: Functional Heterogeneity Of Rp Paralogsmentioning
confidence: 99%
“…Systematic functional analyses of rp paralog mutants need to account for such extra-ribosomal functions of RPs. For instance, uL23 recruits a nascent protein to its future localization in the chloroplast by coupling with its receptor ( Kim et al., 2015 ). Whether the differential uL23 paralog phenotypes are influenced by both moonlighting and ribosomal functions remains an open discussion.…”
Section: Functional Heterogeneity Of Rp Paralogsmentioning
confidence: 99%
“…In addition to the TOC complex, potential AIMs were also identified in the outer envelope protein (OEP) complex, which serves as an alternative pathway for chloroplast protein import (Lee et al, 2014). OEP7 and OEP9 have been shown to function together with heat shock protein Hsp17.8 and AKR2A cofactors in targeting membrane proteins to plastid outer membranes under normal physiological conditions (Niehaus et al, 2014; Kim et al, 2015). To enable the efficient recognition by the autophagosomal or vacuolar membrane, it is possible that these chloroplast outer membrane proteins might serve as receptors by binding to the ATG or non-ATG chlorophagy regulators.…”
Section: Chlorophagy-related Membrane Receptors In Plantsmentioning
confidence: 99%
“…Ankyrin-repeat containing protein 2 A (AKR2A) is an essential molecular chaperone that binds to hydrophobic amino acid residues, which prevents membrane proteins from aggregating after translation in the cytoplasm 6 8 . akr2a mutants display a chilling-sensitive phenotype, suggesting that AKR2A plays important roles in the plant network responding to cold stress.…”
Section: Introductionmentioning
confidence: 99%