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| Verfasst von: | Avci, Dönem [VerfasserIn]  |
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| | Malchus, Nicole Susanne [VerfasserIn] |
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| | Heidasch, Ronny [VerfasserIn] |
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| | Lorenz, Holger [VerfasserIn] |
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| | Richter, Karsten [VerfasserIn] |
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| | Neßling, Michelle [VerfasserIn] |
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| | Lemberg, Marius [VerfasserIn] |
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| Titel: | The intramembrane protease SPP impacts morphology of the endoplasmic reticulum by triggering degradation of morphogenic proteins |
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| Verf.angabe: | Dönem Avci, Nicole S. Malchus, Ronny Heidasch, Holger Lorenz, Karsten Richter, Michelle Neßling, and Marius K. Lemberg |
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| Jahr: | 2019 |
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| Jahr des Originals: | 2018 |
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| Umfang: | 15 S. |
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| Fussnoten: | First published on December 21, 2018 ; Gesehen am 15.04.2019 |
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| Titel Quelle: | Enthalten in: The journal of biological chemistry |
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| Ort Quelle: | Bethesda, Md. : Soc., 1905 |
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| Jahr Quelle: | 2019 |
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| Band/Heft Quelle: | 294(2019), 8, Seite 2786-2800 |
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| ISSN Quelle: | 1083-351X |
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| Abstract: | The endoplasmic reticulum (ER), as a multifunctional organelle, plays crucial roles in lipid biosynthesis and calcium homeostasis as well as the synthesis and folding of secretory and membrane proteins. Therefore, it is of high importance to maintain ER homeostasis and to adapt ER function and morphology to cellular needs. Here, we show that signal peptide peptidase (SPP) modulates the ER shape through degradation of morphogenic proteins. Elevating SPP activity induces rapid rearrangement of the ER and formation of dynamic ER clusters. Inhibition of SPP activity rescues the phenotype without the need for new protein synthesis, and this rescue depends on a pre-existing pool of proteins in the Golgi. With the help of organelle proteomics, we identified certain membrane proteins to be diminished upon SPP expression and further show that the observed morphology changes depend on SPP-mediated cleavage of ER morphogenic proteins, including the SNARE protein syntaxin-18. Thus, we suggest that SPP-mediated protein abundance control by a regulatory branch of ER-associated degradation (ERAD-R) has a role in shaping the early secretory pathway. |
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| DOI: | doi:10.1074/jbc.RA118.005642 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1074/jbc.RA118.005642 |
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| | Volltext: http://www.jbc.org/content/294/8/2786 |
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| | DOI: https://doi.org/10.1074/jbc.RA118.005642 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | cellular regulation |
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| | endoplasmic reticulum-associated protein degradation (ERAD) |
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| | intramembrane proteolysis |
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| | organelle |
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| | organelle morphology |
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| | proteolysis |
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| | substrate identification |
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| | tail-anchored protein |
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| K10plus-PPN: | 166325821X |
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| Verknüpfungen: | → Zeitschrift |
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¬The¬ intramembrane protease SPP impacts morphology of the endoplasmic reticulum by triggering degradation of morphogenic proteins / Avci, Dönem [VerfasserIn]; 2019 (Online-Ressource)
