2018
DOI: 10.1105/tpc.18.00275
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PUX10 Is a CDC48A Adaptor Protein That Regulates the Extraction of Ubiquitinated Oleosins from Seed Lipid Droplets in Arabidopsis

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Cited by 75 publications
(90 citation statements)
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References 86 publications
(125 reference statements)
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“…These distinct motifs designate oleosins toward different degradation pathways according to the ubiquitination type. Deruyffelaere et al further confirmed that PUX10 localized to OBs interacts directly with ubiquitinated oleosins and mediates dislocation of oleosins by the AAA ATPase CDC48A (Deruyffelaere et al, 2018;Kretzschmar et al, 2018).…”
Section: Interactions Between Ob-associated Proteins and Other Proteinsmentioning
confidence: 87%
See 1 more Smart Citation
“…These distinct motifs designate oleosins toward different degradation pathways according to the ubiquitination type. Deruyffelaere et al further confirmed that PUX10 localized to OBs interacts directly with ubiquitinated oleosins and mediates dislocation of oleosins by the AAA ATPase CDC48A (Deruyffelaere et al, 2018;Kretzschmar et al, 2018).…”
Section: Interactions Between Ob-associated Proteins and Other Proteinsmentioning
confidence: 87%
“…PUX10 localizes to OBs and binds to the ubiquitinated oleosins via its hydrophobic domain and interacts with ubiquitin and CDC48A via its UBA and UBX domains, respectively. As an adaptor, PUX10 recruits CDC48A to ubiquitinated oleosins, leading to dislocation of oleosins from OBs via the segregase activity of CDC48A (Deruyffelaere et al, 2018;Kretzschmar et al, 2018).…”
Section: Oleosins Play An Important Role In Ob Formation and Degradationmentioning
confidence: 99%
“…It seems possible, therefore, that the slight enlargement of LBs during bud development is based on the continuation of TAG biosynthesis at free cytosolic LBs [28]. In mature buds, some LBs might show coalescence (Figure 1e,g), which could be caused either by LB expansion and the resulting changes in LB surface tension [4,10], or by gradual degradation of OLEOSINs [73,74].…”
Section: Discussionmentioning
confidence: 99%
“…1). The most abundant LD protein, oleosin, is embedded in the LD membrane and helps maintain LD structure and regulates lipid mobilization via its extraction and turnover by the ubiquitin-proteasome system (Pyc et al, 2017;Deruyffelaere et al, 2018).…”
Section: Discovering Lipid Droplet Proteins: From Seeds To Seedlingsmentioning
confidence: 99%
“…It has been suggested that LD proteins act to shield TAGs from lipolytic enzymes; when removed, accessible lipids are extracted and mobilized. Alternatively, LD proteins may interact with cytoplasmic lipases and other regulatory proteins to stimulate lipolysis (Deruyffelaere et al, 2018).…”
Section: Discovering Lipid Droplet Proteins: From Seeds To Seedlingsmentioning
confidence: 99%