5
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      ER remodeling via ER-phagy

      review-article
      1 , 1 , 2 , 3 ,
      Molecular Cell
      Cell Press

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Summary

          The endoplasmic reticulum (ER) is a hotspot for many essential cellular functions. The ER membrane is highly dynamic, which affects many cellular processes that take place within the ER. One such process is ER-phagy, a selective degradation of ER fragments (including membranes and luminal content), which serves to preserve the size of ER while adapting its morphology under basal and stress conditions. In order to be degraded, the ER undergoes selective fragmentation facilitated by specialized ER-shaping proteins that also act as ER-phagy receptors. Their ability to sense and induce membrane curvature, as well as to bridge the ER with autophagy machinery, allows for a successful ER fragmentation and delivery of these fragments to the lysosome for degradation and recycling. In this review, we provide insights into ER-phagy from the perspective of membrane remodeling. We highlight the importance of ER membrane dynamics during ER-phagy and emphasize how its dysregulation reflects on human physiology and pathology.

          Graphical abstract

          Abstract

          In this review, Gubas and Dikic highlight the importance of ER membrane remodeling during the process of selective ER degradation. The authors focus on reticulon-homology-domain-containing proteins and their involvement in ER membrane budding and vesicle formation.

          Related collections

          Most cited references88

          • Record: found
          • Abstract: found
          • Article: found
          Is Open Access

          Double-slit photoelectron interference in strong-field ionization of the neon dimer

          Wave-particle duality is an inherent peculiarity of the quantum world. The double-slit experiment has been frequently used for understanding different aspects of this fundamental concept. The occurrence of interference rests on the lack of which-way information and on the absence of decoherence mechanisms, which could scramble the wave fronts. Here, we report on the observation of two-center interference in the molecular-frame photoelectron momentum distribution upon ionization of the neon dimer by a strong laser field. Postselection of ions, which are measured in coincidence with electrons, allows choosing the symmetry of the residual ion, leading to observation of both, gerade and ungerade, types of interference.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Mitofusin 2 tethers endoplasmic reticulum to mitochondria.

            Juxtaposition between endoplasmic reticulum (ER) and mitochondria is a common structural feature, providing the physical basis for intercommunication during Ca(2+) signalling; yet, the molecular mechanisms controlling this interaction are unknown. Here we show that mitofusin 2, a mitochondrial dynamin-related protein mutated in the inherited motor neuropathy Charcot-Marie-Tooth type IIa, is enriched at the ER-mitochondria interface. Ablation or silencing of mitofusin 2 in mouse embryonic fibroblasts and HeLa cells disrupts ER morphology and loosens ER-mitochondria interactions, thereby reducing the efficiency of mitochondrial Ca(2+) uptake in response to stimuli that generate inositol-1,4,5-trisphosphate. An in vitro assay as well as genetic and biochemical evidences support a model in which mitofusin 2 on the ER bridges the two organelles by engaging in homotypic and heterotypic complexes with mitofusin 1 or 2 on the surface of mitochondria. Thus, mitofusin 2 tethers ER to mitochondria, a juxtaposition required for efficient mitochondrial Ca(2+) uptake.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              A class of membrane proteins shaping the tubular endoplasmic reticulum.

              How is the characteristic shape of a membrane bound organelle achieved? We have used an in vitro system to address the mechanism by which the tubular network of the endoplasmic reticulum (ER) is generated and maintained. Based on the inhibitory effect of sulfhydryl reagents and antibodies, network formation in vitro requires the integral membrane protein Rtn4a/NogoA, a member of the ubiquitous reticulon family. Both in yeast and mammalian cells, the reticulons are largely restricted to the tubular ER and are excluded from the continuous sheets of the nuclear envelope and peripheral ER. Upon overexpression, the reticulons form tubular membrane structures. The reticulons interact with DP1/Yop1p, a conserved integral membrane protein that also localizes to the tubular ER. These proteins share an unusual hairpin topology in the membrane. The simultaneous absence of the reticulons and Yop1p in S. cerevisiae results in disrupted tubular ER. We propose that these "morphogenic" proteins partition into and stabilize highly curved ER membrane tubules.
                Bookmark

                Author and article information

                Contributors
                Journal
                Mol Cell
                Mol Cell
                Molecular Cell
                Cell Press
                1097-2765
                1097-4164
                21 April 2022
                21 April 2022
                : 82
                : 8
                : 1492-1500
                Affiliations
                [1 ]Institute of Biochemistry II, Faculty of Medicine, Goethe University Frankfurt, Frankfurt, Germany
                [2 ]Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, Germany
                [3 ]Max Planck Institute of Biophysics, Frankfurt, Germany
                Author notes
                []Corresponding author dikic@ 123456biochem2.uni-frankfurt.de
                Article
                S1097-2765(22)00156-3
                10.1016/j.molcel.2022.02.018
                9098120
                35452617
                f0877d0a-dee7-4773-86db-67f220f6bde7
                © 2022 The Authors. Published by Elsevier Inc.

                This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

                History
                Categories
                Review

                Molecular biology
                Molecular biology

                Comments

                Comment on this article