Rab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins

Abstract Background Rab32 is a small GTPase associated with multiple organelles but is particularly enriched at the endoplasmic reticulum (ER). Here, it controls targeting to mitochondria-ER contacts (MERCs), thus influencing composition of the mitochondria-associated membrane (MAM). Moreover, Rab32...

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Autores principales:	Maria Sol Herrera-Cruz, Megan C. Yap, Nasser Tahbaz, Keelie Phillips, Laurel Thomas, Gary Thomas, Thomas Simmen
Formato:	article
Lenguaje:	EN
Publicado:	BMC 2021
Materias:	Rab32 Mitochondria-associated membrane (MAM) Autophagy ER-phagy Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/a331bf03648046b0ae7fd0d42d92e7f2
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spelling	oai:doaj.org-article:a331bf03648046b0ae7fd0d42d92e7f22021-11-14T12:08:43ZRab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins10.1186/s13062-021-00311-91745-6150https://doaj.org/article/a331bf03648046b0ae7fd0d42d92e7f22021-11-01T00:00:00Zhttps://doi.org/10.1186/s13062-021-00311-9https://doaj.org/toc/1745-6150Abstract Background Rab32 is a small GTPase associated with multiple organelles but is particularly enriched at the endoplasmic reticulum (ER). Here, it controls targeting to mitochondria-ER contacts (MERCs), thus influencing composition of the mitochondria-associated membrane (MAM). Moreover, Rab32 regulates mitochondrial membrane dynamics via its effector dynamin-related protein 1 (Drp1). Rab32 has also been reported to induce autophagy, an essential pathway targeting intracellular components for their degradation. However, no autophagy-specific effectors have been identified for Rab32. Similarly, the identity of the intracellular membrane targeted by this small GTPase and the type of autophagy it induces are not known yet. Results To investigate the target of autophagic degradation mediated by Rab32, we tested a large panel of organellar proteins. We found that a subset of MERC proteins, including the thioredoxin-related transmembrane protein TMX1, are specifically targeted for degradation in a Rab32-dependent manner. We also identified the long isoform of reticulon-3 (RTN3L), a known ER-phagy receptor, as a Rab32 effector. Conclusions Rab32 promotes degradation of mitochondrial-proximal ER membranes through autophagy with the help of RTN3L. We propose to call this type of selective autophagy “MAM-phagy”.Maria Sol Herrera-CruzMegan C. YapNasser TahbazKeelie PhillipsLaurel ThomasGary ThomasThomas SimmenBMCarticleRab32Mitochondria-associated membrane (MAM)AutophagyER-phagyBiology (General)QH301-705.5ENBiology Direct, Vol 16, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Rab32 Mitochondria-associated membrane (MAM) Autophagy ER-phagy Biology (General) QH301-705.5
spellingShingle	Rab32 Mitochondria-associated membrane (MAM) Autophagy ER-phagy Biology (General) QH301-705.5 Maria Sol Herrera-Cruz Megan C. Yap Nasser Tahbaz Keelie Phillips Laurel Thomas Gary Thomas Thomas Simmen Rab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins
description	Abstract Background Rab32 is a small GTPase associated with multiple organelles but is particularly enriched at the endoplasmic reticulum (ER). Here, it controls targeting to mitochondria-ER contacts (MERCs), thus influencing composition of the mitochondria-associated membrane (MAM). Moreover, Rab32 regulates mitochondrial membrane dynamics via its effector dynamin-related protein 1 (Drp1). Rab32 has also been reported to induce autophagy, an essential pathway targeting intracellular components for their degradation. However, no autophagy-specific effectors have been identified for Rab32. Similarly, the identity of the intracellular membrane targeted by this small GTPase and the type of autophagy it induces are not known yet. Results To investigate the target of autophagic degradation mediated by Rab32, we tested a large panel of organellar proteins. We found that a subset of MERC proteins, including the thioredoxin-related transmembrane protein TMX1, are specifically targeted for degradation in a Rab32-dependent manner. We also identified the long isoform of reticulon-3 (RTN3L), a known ER-phagy receptor, as a Rab32 effector. Conclusions Rab32 promotes degradation of mitochondrial-proximal ER membranes through autophagy with the help of RTN3L. We propose to call this type of selective autophagy “MAM-phagy”.
format	article
author	Maria Sol Herrera-Cruz Megan C. Yap Nasser Tahbaz Keelie Phillips Laurel Thomas Gary Thomas Thomas Simmen
author_facet	Maria Sol Herrera-Cruz Megan C. Yap Nasser Tahbaz Keelie Phillips Laurel Thomas Gary Thomas Thomas Simmen
author_sort	Maria Sol Herrera-Cruz
title	Rab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins
title_short	Rab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins
title_full	Rab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins
title_fullStr	Rab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins
title_full_unstemmed	Rab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins
title_sort	rab32 uses its effector reticulon 3l to trigger autophagic degradation of mitochondria-associated membrane (mam) proteins
publisher	BMC
publishDate	2021
url	https://doaj.org/article/a331bf03648046b0ae7fd0d42d92e7f2
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Rab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins

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