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Article ; Online: LC3B is a cofactor for LMX1B-mediated transcription of autophagy genes in dopaminergic neurons.

Kournoutis, Athanasios / Johansen, Terje

2023 Volume 222, Issue 5

Abstract: It is becoming increasingly clear that the Atg8 family of autophagy proteins have roles not only in the cytoplasm, but also in the cell nucleus. In this issue, Jiménez-Moreno et al. (2023. J. Cell Biol.https://doi.org/10.1083/jcb.201910133) report that ... ...

Abstract	It is becoming increasingly clear that the Atg8 family of autophagy proteins have roles not only in the cytoplasm, but also in the cell nucleus. In this issue, Jiménez-Moreno et al. (2023. J. Cell Biol.https://doi.org/10.1083/jcb.201910133) report that nuclear LC3B binds to the LIM homeodomain transcription factor LMX1B and acts as a cofactor for LMX1B-mediated transcription of autophagy genes, providing stress protection and ensuring survival of midbrain dopaminergic neurons.
MeSH term(s)	Dopaminergic Neurons/metabolism ; LIM-Homeodomain Proteins/genetics ; LIM-Homeodomain Proteins/metabolism ; DNA-Binding Proteins/metabolism ; Transcription Factors/metabolism ; Autophagy/genetics ; Homeodomain Proteins/genetics ; Homeodomain Proteins/metabolism
Chemical Substances	LIM-Homeodomain Proteins ; DNA-Binding Proteins ; Transcription Factors ; Homeodomain Proteins
Language	English
Publishing date	2023-04-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202303008
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Article ; Online: AlphaFold-multimer predicts ATG8 protein binding motifs crucial for autophagy research.

Olsvik, Hallvard Lauritz / Johansen, Terje

PLoS biology

2023 Volume 21, Issue 2, Page(s) e3002002

Abstract: In this issue of PLOS Biology, Ibrahim and colleagues demonstrate how AlphaFold-multimer, an artificial intelligence-based structure prediction tool, can be used to identify sequence motifs binding to the ATG8 family of proteins central to autophagy. ...

Abstract	In this issue of PLOS Biology, Ibrahim and colleagues demonstrate how AlphaFold-multimer, an artificial intelligence-based structure prediction tool, can be used to identify sequence motifs binding to the ATG8 family of proteins central to autophagy.
MeSH term(s)	Artificial Intelligence ; Protein Binding ; Autophagy ; Protein Domains
Language	English
Publishing date	2023-02-08
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.3002002
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Zs.A 6193: Show issues

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Article ; Online: Selective Autophagy: RNA Comes from the Vault to Regulate p62/SQSTM1.

Johansen, Terje

Current biology : CB

2019 Volume 29, Issue 8, Page(s) R297–R299

Abstract: A new study shows that the oligomerization of p62/Sequestosome-1 (SQSTM1) - a selective autophagy receptor and signaling adapter - is regulated directly by vault RNA. This riboregulation negatively affects the aggregation state of p62 and thereby its ... ...

Abstract	A new study shows that the oligomerization of p62/Sequestosome-1 (SQSTM1) - a selective autophagy receptor and signaling adapter - is regulated directly by vault RNA. This riboregulation negatively affects the aggregation state of p62 and thereby its autophagic degradation and its role as a selective autophagy receptor.
MeSH term(s)	Autophagy ; RNA ; RNA, Bacterial ; Sequestosome-1 Protein ; Signal Transduction
Chemical Substances	RNA I ; RNA, Bacterial ; Sequestosome-1 Protein ; RNA (63231-63-0)
Language	English
Publishing date	2019-05-18
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2019.03.008
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Zs.A 3208: Show issues

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Article ; Online: WDR83/MORG1 inhibits RRAG GTPase-MTORC1 signaling to facilitate basal autophagy.

Kournoutis, Athanasios / Lamark, Trond / Johansen, Terje / Abudu, Yakubu Princely

Autophagy

2024 , Page(s) 1–2

Abstract: Macroautophagy/autophagy is a conserved lysosomal degradation process composed of both selective and nonselective degradation pathways. The latter occurs upon nutrient depletion. Selective autophagy exerts quality control of damaged organelles and ... ...

Abstract	Macroautophagy/autophagy is a conserved lysosomal degradation process composed of both selective and nonselective degradation pathways. The latter occurs upon nutrient depletion. Selective autophagy exerts quality control of damaged organelles and macromolecules and is going on also under nutrient-replete conditions. Proper regulation of autophagy is vital for cellular homeostasis and prevention of disease. During nutrient availability, autophagy is inhibited by the MTORC1 signaling pathway. However, selective, basal autophagy occurs continuously. How the MTORC1 pathway is fine-tuned to facilitate basal constitutive autophagy is unclear. Recently, we identified the WD-domain repeat protein WDR83/MORG1 as a negative regulator of MTORC1 signaling allowing basal, selective autophagy. WDR83 interacts with both the Ragulator and active RRAG GTPases to prevent recruitment of the MTORC1 complex to the lysosome. Consequently, WDR83 depletion leads to hyperactivation of the MTORC1 pathway and a strong decrease in basal autophagy. As a consequence of WDR83 depletion cell proliferation and migration increase and low levels of
Language	English
Publishing date	2024-03-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2024.2322457
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Zs.A 6741: Show issues

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Article ; Online: Mechanisms of Selective Autophagy.

Lamark, Trond / Johansen, Terje

Annual review of cell and developmental biology

2021 Volume 37, Page(s) 143–169

Abstract: Selective autophagy is the lysosomal degradation of specific intracellular components sequestered into autophagosomes, late endosomes, or lysosomes through the activity of selective autophagy receptors (SARs). SARs interact with autophagy-related (ATG)8 ... ...

Abstract	Selective autophagy is the lysosomal degradation of specific intracellular components sequestered into autophagosomes, late endosomes, or lysosomes through the activity of selective autophagy receptors (SARs). SARs interact with autophagy-related (ATG)8 family proteins via sequence motifs called LC3-interacting region (LIR) motifs in vertebrates and Atg8-interacting motifs (AIMs) in yeast and plants. SARs can be divided into two broad groups: soluble or membrane bound. Cargo or substrate selection may be independent or dependent of ubiquitin labeling of the cargo. In this review, we discuss mechanisms of mammalian selective autophagy with a focus on the unifying principles employed in substrate recognition, interaction with the forming autophagosome via LIR-ATG8 interactions, and the recruitment of core autophagy components for efficient autophagosome formation on the substrate.
MeSH term(s)	Animals ; Apoptosis Regulatory Proteins/metabolism ; Autophagosomes/metabolism ; Autophagy/genetics ; Autophagy-Related Protein 8 Family/genetics ; Autophagy-Related Protein 8 Family/metabolism ; Mammals/metabolism ; Microtubule-Associated Proteins/metabolism
Chemical Substances	Apoptosis Regulatory Proteins ; Autophagy-Related Protein 8 Family ; Microtubule-Associated Proteins
Language	English
Publishing date	2021-06-21
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1293750-2
ISSN	1530-8995 ; 1081-0706
ISSN (online)	1530-8995
ISSN	1081-0706
DOI	10.1146/annurev-cellbio-120219-035530
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Article ; Online: Autophagy and endocytosis - interconnections and interdependencies.

Birgisdottir, Åsa B / Johansen, Terje

Journal of cell science

2020 Volume 133, Issue 10

Abstract: Autophagy and endocytosis are membrane-vesicle-based cellular pathways for degradation and recycling of intracellular and extracellular components, respectively. These pathways have a common endpoint at the lysosome, where their cargo is degraded. In ... ...

Abstract	Autophagy and endocytosis are membrane-vesicle-based cellular pathways for degradation and recycling of intracellular and extracellular components, respectively. These pathways have a common endpoint at the lysosome, where their cargo is degraded. In addition, the two pathways intersect at different stages during vesicle formation, fusion and trafficking, and share parts of the molecular machinery. Accumulating evidence shows that autophagy is dependent upon endocytosis and vice versa. The emerging joint network of autophagy and endocytosis is of vital importance for cellular metabolism and signaling, and thus also highly relevant in disease settings. In this Review, we will discuss examples of how the autophagy machinery impacts on endocytosis and cell signaling, and highlight how endocytosis regulates the different steps in autophagy in mammalian cells. Finally, we will focus on the interplay of these pathways in the quality control of their common endpoint, the lysosome.
MeSH term(s)	Animals ; Autophagy ; Cell Membrane ; Endocytosis ; Lysosomes ; Signal Transduction
Language	English
Publishing date	2020-05-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.228114
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Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: MORG1 limits mTORC1 signaling by inhibiting Rag GTPases.

Abudu, Yakubu Princely / Kournoutis, Athanasios / Brenne, Hanne Britt / Lamark, Trond / Johansen, Terje

Molecular cell

2023 Volume 84, Issue 3, Page(s) 552–569.e11

Abstract: Autophagy, an important quality control and recycling process vital for cellular homeostasis, is tightly regulated. The mTORC1 signaling pathway regulates autophagy under conditions of nutrient availability and scarcity. However, how mTORC1 activity is ... ...

Abstract	Autophagy, an important quality control and recycling process vital for cellular homeostasis, is tightly regulated. The mTORC1 signaling pathway regulates autophagy under conditions of nutrient availability and scarcity. However, how mTORC1 activity is fine-tuned during nutrient availability to allow basal autophagy is unclear. Here, we report that the WD-domain repeat protein MORG1 facilitates basal constitutive autophagy by inhibiting mTORC1 signaling through Rag GTPases. Mechanistically, MORG1 interacts with active Rag GTPase complex inhibiting the Rag GTPase-mediated recruitment of mTORC1 to the lysosome. MORG1 depletion in HeLa cells increases mTORC1 activity and decreases autophagy. The autophagy receptor p62/SQSTM1 binds to MORG1, but MORG1 is not an autophagy substrate. However, p62/SQSTM1 binding to MORG1 upon re-addition of amino acids following amino acid's depletion precludes MORG1 from inhibiting the Rag GTPases, allowing mTORC1 activation. MORG1 depletion increases cell proliferation and migration. Low expression of MORG1 correlates with poor survival in several important cancers.
MeSH term(s)	Humans ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; HeLa Cells ; Sequestosome-1 Protein/metabolism ; Signal Transduction ; Mechanistic Target of Rapamycin Complex 1/genetics ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Lysosomes/metabolism ; Monomeric GTP-Binding Proteins/genetics ; Monomeric GTP-Binding Proteins/metabolism
Chemical Substances	GTP Phosphohydrolases (EC 3.6.1.-) ; Sequestosome-1 Protein ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2023-12-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2023.11.023
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Zs.A 5055: Show issues

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Article ; Online: NBR1: The archetypal selective autophagy receptor.

Rasmussen, Nikoline Lander / Kournoutis, Athanasios / Lamark, Trond / Johansen, Terje

The Journal of cell biology

2022 Volume 221, Issue 11

Abstract: NBR1 was discovered as an autophagy receptor not long after the first described vertebrate autophagy receptor p62/SQSTM1. Since then, p62 has currently been mentioned in >10,000 papers on PubMed, while NBR1 is mentioned in <350 papers. Nonetheless, ... ...

Abstract	NBR1 was discovered as an autophagy receptor not long after the first described vertebrate autophagy receptor p62/SQSTM1. Since then, p62 has currently been mentioned in >10,000 papers on PubMed, while NBR1 is mentioned in <350 papers. Nonetheless, evolutionary analysis reveals that NBR1, and likely also selective autophagy, was present already in the last eukaryotic common ancestor (LECA), while p62 appears first in the early Metazoan lineage. Furthermore, yeast-selective autophagy receptors Atg19 and Atg34 represent NBR1 homologs. NBR1 is the main autophagy receptor in plants that do not contain p62, while most animal taxa contain both NBR1 and p62. Mechanistic studies are starting to shed light on the collaboration between mammalian NBR1 and p62 in the autophagic degradation of protein aggregates (aggrephagy). Several domains of NBR1 are involved in cargo recognition, and the list of known substrates for NBR1-mediated selective autophagy is increasing. Lastly, roles of NBR1 in human diseases such as proteinopathies and cancer are emerging.
MeSH term(s)	Animals ; Humans ; Autophagy ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Macroautophagy ; Mammals ; Protein Aggregates ; Sequestosome-1 Protein/genetics ; Sequestosome-1 Protein/metabolism ; Plants
Chemical Substances	Carrier Proteins ; Intracellular Signaling Peptides and Proteins ; NBR1 protein, human ; Protein Aggregates ; Sequestosome-1 Protein
Language	English
Publishing date	2022-10-18
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202208092
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Article ; Online: Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors.

Johansen, Terje / Lamark, Trond

Journal of molecular biology

2019 Volume 432, Issue 1, Page(s) 80–103

Abstract: Selective autophagy relies on soluble or membrane-bound cargo receptors that recognize cargo and bring about autophagosome formation at the cargo. The cargo-bound receptors interact with lipidated ATG8 family proteins anchored in the membrane at the ... ...

Abstract	Selective autophagy relies on soluble or membrane-bound cargo receptors that recognize cargo and bring about autophagosome formation at the cargo. The cargo-bound receptors interact with lipidated ATG8 family proteins anchored in the membrane at the concave side of the forming autophagosome. The interaction is mediated by 15- to 20-amino-acid-long sequence motifs called LC3-interacting region (LIR) motifs that bind to the LIR docking site (LDS) of ATG8 proteins. In this review, we focus on LIR-ATG8 interactions and the soluble mammalian selective autophagy receptors. We discuss the roles of ATG8 family proteins as membrane scaffolds in autophagy and the LIR-LDS interaction and how specificity for binding to GABARAP or LC3 subfamily proteins is achieved. We also discuss atypical LIR-LDS interactions and a novel LIR-independent interaction. Recently, it has become clear that several of the soluble cargo receptors are able to recruit components of the core autophagy apparatus to aid in assembling autophagosome formation at the site of cargo sequestration. A model on phagophore recruitment and expansion on a selective autophagy receptor-coated cargo incorporating the latest findings is presented.
MeSH term(s)	Animals ; Apoptosis Regulatory Proteins/analysis ; Apoptosis Regulatory Proteins/metabolism ; Autophagosomes/chemistry ; Autophagosomes/metabolism ; Autophagy ; Autophagy-Related Protein 8 Family/analysis ; Autophagy-Related Protein 8 Family/metabolism ; Humans ; Macroautophagy ; Microtubule-Associated Proteins/analysis ; Microtubule-Associated Proteins/metabolism ; Protein Interaction Domains and Motifs ; Protein Interaction Maps
Chemical Substances	Apoptosis Regulatory Proteins ; Autophagy-Related Protein 8 Family ; GABARAP protein, human ; MAP1LC3A protein, human ; Microtubule-Associated Proteins
Language	English
Publishing date	2019-07-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2019.07.016
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Zs.A 867: Show issues

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Article: Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors

Johansen, Terje / Lamark, Trond

Journal of molecular biology. 2019 July 05,

2019

Abstract	Selective autophagy relies on soluble or membrane-bound cargo receptors that recognize cargo and bring about autophagosome formation at the cargo. The cargo-bound receptors interact with lipidated ATG8 family proteins anchored in the membrane at the concave side of the forming autophagosome. The interaction is mediated by 15- to 20-amino-acid-long sequence motifs called LC3-interacting region (LIR) motifs that bind to the LIR docking site (LDS) of ATG8 proteins. In this review, we focus on LIR–ATG8 interactions and the soluble mammalian selective autophagy receptors. We discuss the roles of ATG8 family proteins as membrane scaffolds in autophagy and the LIR–LDS interaction and how specificity for binding to GABARAP or LC3 subfamily proteins is achieved. We also discuss atypical LIR–LDS interactions and a novel LIR-independent interaction. Recently, it has become clear that several of the soluble cargo receptors are able to recruit components of the core autophagy apparatus to aid in assembling autophagosome formation at the site of cargo sequestration. A model on phagophore recruitment and expansion on a selective autophagy receptor-coated cargo incorporating the latest findings is presented.
Keywords	autophagy ; mammals ; models ; receptors
Language	English
Dates of publication	2019-0705
Publishing place	Elsevier Ltd
Document type	Article
Note	Pre-press version
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2019.07.016
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