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Interactome of Sec13 paralogs in Paradiplonema papillatum

ABSTRACT: The acquisition of new functions is frequently the result of gene duplication and is a major driver of evolutionary complexity. The β-propeller protein Sec13 plays roles in at least three distinct processes by virtue of being a component of the COPII endoplasmic reticulum export vesicle coat, the nuclear pore complex (NPC) and the Seh1-associated (SEA)/GATOR nutrient-sensing complex, suggesting that regulatory mechanisms coordinating these cellular activities may operate via Sec13. COPII, SEA and the NPC are ancient features of eukaryotic cells. We analyzed the Sec13 interactome in diplonemids, widespread marine protists, and found that Sec13 functions are divided between two paralogs, Sec13a and Sec13b. Sec13a interacts with COPII and the NPC, but by contrast Sec13b interacts with Sec16 and components of the SEA/GATOR complex. Hence, we infer that Sec13a is responsible for NPC functions and canonical anterograde transport activities while Sec13b acts within nutrient and autophagy-related pathways. Furthermore, duplication of Sec13 is near universal across the Euglenozoa, providing a potent exemplar of paralogy expansion and functional diversification.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Diplonema Papillatum

SUBMITTER: Corinna Benz

LAB HEAD: Julius Lukes

PROVIDER: PXD037122 | Pride | 2023-06-14

REPOSITORIES: Pride

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Project description:This experiment was conducted to identify mRNA transcripts alteration in liver of Ern1 liver specific knockout mice. The following abstract from the submitted manuscript describes the major findings of this work. The IRE1a-XBP1s axis regulates the COPII-mediated secretory program in response to nutrient availability. Lin Liu, Jie Cai, Xijun Liang, Qian Zhou, Huimin Wang, Chenyun Ding, Yuangang Zhu, Liwei Xiao, Tingting Fu, Zhisheng Xu, Jing Liu, Yujing Yin, Lei Fang, Bin Xue, Yan Wang, Aibin He, Yong Liu, Xiao-Wei Chen, and Zhenji Gan The cytoplasmic coat protein complex-II (COPII) is an evolutionarily conserved machinery that is essential for efficient trafficking of protein and lipid cargos. How the COPII machinery is regulated to meet the metabolic demand in response to alterations of nutritional state remains largely unexplored, however. Here, we show that dynamic changes of COPII-mediated secretion parallel the activation of XBP1s, the critical transcription factor in handling cellular ER stress, in both live cells and mouse liver upon physiological fluctuations of nutrient availability. Using live-cell imaging approaches, we demonstrate that XBP1s is sufficient to promote COPII-dependent secretion, mediating the nutrient stimulatory effects. ChIP-seq and RNA-seq analyses reveal that nutritional signals induce dynamic XBP1s occupancy of promoters of COPII secretion-related genes, thereby driving COPII-directed secretory process. Liver-specific disruption of the IRE1a-XBP1s signaling branch results in diminished COPII-mediated secretion. Reactivation of XBP1s in mice lacking hepatic IRE1a restores COPII-mediated lipoprotein secretion, and reverses the fatty liver and hypolipidemia phenotypes. Thus, our results demonstrate a previously unappreciated mechanism in the metabolic control of liver protein and lipid secretion: the IRE1a-XBP1s axis functions as a nutrient-sensing regulatory nexus that integrates nutritional states and the COPII secretory program.

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Interactome of Sec13 paralogs in Paradiplonema papillatum

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