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er exit pathways and the control of proteostasis:Crucial role of the UPR,COPII,and ER-phagy in the secretory pathway

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BIOCELL 2022年第5期46卷 1131-1137页

作者： GIUSEPPINA AMODIO VALENTINA PAGLIARA PAOLO REMONDELLI ORNELLA MOLTEDO Dipartimento di Medicina Chirurgia e Odontoiatria“Scuola Medica Salernitana”Universitàdegli Studi di SalernoBaronissi84034Italy2 Dipartimento di FarmaciaUniversitàdegli Studi di SalernoFisciano84084Italy

The endoplasmic reticulum(er)is the site of entry of all proteins that function in the secretory pathway including the extracellular environment.Because it controls the folding of newly synthesized secretory proteins,the er is indispensable for the maintenance of proteostasis in the secretory pathway.Within the er and,in part,in post-er compartments,the quality control of protein folding is under the regulation of the unfolded protein response(UPR)pathways.The UPR strategy is to enhance protein folding,increase the er degradation pathway of misfolded proteins,and allow the exit from the er of only correctly folded proteins.The latter is controlled by the multimeric complex COPII,which also provides some of the components for ER-phagy the only route for the disposal of protein aggregates.In this overview,we wish to contribute to the introduction of new perspectives in the study of the mechanisms underlying the control of proteostasis within the secretory pathway.

关键词： Proteostasis er stress Unfolded protein response COPII ER-phagy

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Real-time tracking of er turnover during erLAD by a rhenium complex via lifetime imaging

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National Science Review 2022年第7期9卷 80-87页

作者： Liang Hao Yu-Yi Ling Zhi-Xin Huang Zheng-Yin Pan Cai-Ping Tan Zong-Wan Mao MOE Key Laboratory of Bioinorganic and Synthetic Chemistry School of ChemistryState Key Laboratory of Oncology in South China Sun Yat-Sen University

Endoplasmic reticulum(er) degradation by autophagy(ER-phagy) is a recently revealed selective autophagy pathway that plays important roles in organelle turnover and protein degradation,but the biological functions of ER-phagy are largely unknown.Here,we present an er-targeting Re(I) tricarbonyl complex(Re-erLAD) that can accumulate in the er,induce er-to-lys osome-associated degradation(erLAD) upon visible light irradiation,and label er buds and track their morphological alterations during ER-phagy.The emission of Re-erLAD is sensitive to viscosity,which is a key parameter reflecting the amount of unfolded protein in the er.Quantitative detection using two-photon fluorescence lifetime imaging microscopy shows that er viscosity initially increases and then decreases during erLAD,which reveals that erLAD is a pathway for alleviating er stress caused by unfolded proteins.In conclusion,our work presents the first specific photoinducer and tracker of erLAD,which can be used in studying the regulatory mechanism and function of this process.

关键词： rhenium ER-phagy viscosity TPFLIM

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