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Article ; Online: The autophagy-related protein ATG5 is a central mediator of a non-canonical autophagy pathway hijacked by HIV-1 to weaken the host's response to infection.

Judith, Delphine / Berlioz-Torrent, Clarisse

2023 Volume 20, Issue 4, Page(s) 973–975

Abstract: Understanding how viruses evade innate defenses to efficiently spread in their hosts is crucial in the fight against infections. In our study, we provided new insights on the first step initiating an LC3C (microtubule associated protein 1 light chain 3 ... ...

Abstract	Understanding how viruses evade innate defenses to efficiently spread in their hosts is crucial in the fight against infections. In our study, we provided new insights on the first step initiating an LC3C (microtubule associated protein 1 light chain 3 gamma)-associated degradative pathway exploited by HIV-1 (human immunodeficiency virus type 1) to overcome the antiviral action of the restriction factor BST2 (bone marrow stromal cell antigen 2)/tetherin. We have uncovered an unsuspected and unconventional function of the autophagy-related protein ATG5 in the recognition and engagement of BST2 molecules trapping viruses at the plasma membrane, and directing them toward this LC3C-associated pathway for degradation. Additionally, we highlighted that HIV-1 uses this LC3C-associated process to attenuate the inflammatory responses triggered by BST2-mediated sensing of viruses.
MeSH term(s)	Autophagy/physiology ; HIV-1/physiology ; HIV-1/metabolism ; Humans ; Autophagy-Related Protein 5/metabolism ; HIV Infections/virology ; HIV Infections/metabolism ; HIV Infections/immunology ; Microtubule-Associated Proteins/metabolism ; GPI-Linked Proteins/metabolism ; Antigens, CD/metabolism ; Host-Pathogen Interactions ; Bone Marrow Stromal Antigen 2
Chemical Substances	Autophagy-Related Protein 5 ; Microtubule-Associated Proteins ; GPI-Linked Proteins ; BST2 protein, human ; ATG5 protein, human ; Antigens, CD ; Bone Marrow Stromal Antigen 2
Language	English
Publishing date	2023-07-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2023.2232225
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Article ; Online: ATG9A supplies PtdIns4P to the autophagosome initiation site.

Judith, Delphine / Tooze, Sharon A

Autophagy

2019 Volume 15, Issue 9, Page(s) 1660–1661

Abstract: The identity of the platform supporting the initiation and formation of the nascent autophagosome, the phagophore, is not fully understood. Nucleation and expansion of the phagophore membrane requires a coordinated flux or activation of specific proteins ...

Abstract	The identity of the platform supporting the initiation and formation of the nascent autophagosome, the phagophore, is not fully understood. Nucleation and expansion of the phagophore membrane requires a coordinated flux or activation of specific proteins and membrane lipids at the initiation site. The transmembrane protein ATG9A is essential for macroautophagy/autophagy and proposed to be an initiator of the phagophore by directing or facilitating the delivery of proteins and lipids to the initiation site. Upon amino acid starvation, ATG9A-containing vesicles are formed from the Golgi complex and endosomal compartments and translocate to the initiation site. Unravelling the complement of proteins and lipids brought by ATG9A vesicles to the forming autophagosome is essential to further understand the initiation of autophagy.
MeSH term(s)	Autophagosomes ; Autophagy ; Autophagy-Related Proteins ; Phosphatidylinositol Phosphates
Chemical Substances	Autophagy-Related Proteins ; Phosphatidylinositol Phosphates ; phosphatidylinositol 4-phosphate
Language	English
Publishing date	2019-06-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2019.1632124
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Article ; Online: Proteomic analysis of SARS-CoV-2 particles unveils a key role of G3BP proteins in viral assembly.

Murigneux, Emilie / Softic, Laurent / Aubé, Corentin / Grandi, Carmen / Judith, Delphine / Bruce, Johanna / Le Gall, Morgane / Guillonneau, François / Schmitt, Alain / Parissi, Vincent / Berlioz-Torrent, Clarisse / Meertens, Laurent / Hansen, Maike M K / Gallois-Montbrun, Sarah

Nature communications

2024 Volume 15, Issue 1, Page(s) 640

Abstract: Considerable progress has been made in understanding the molecular host-virus battlefield during SARS-CoV-2 infection. Nevertheless, the assembly and egress of newly formed virions are less understood. To identify host proteins involved in viral ... ...

Abstract	Considerable progress has been made in understanding the molecular host-virus battlefield during SARS-CoV-2 infection. Nevertheless, the assembly and egress of newly formed virions are less understood. To identify host proteins involved in viral morphogenesis, we characterize the proteome of SARS-CoV-2 virions produced from A549-ACE2 and Calu-3 cells, isolated via ultracentrifugation on sucrose cushion or by ACE-2 affinity capture. Bioinformatic analysis unveils 92 SARS-CoV-2 virion-associated host factors, providing a valuable resource to better understand the molecular environment of virion production. We reveal that G3BP1 and G3BP2 (G3BP1/2), two major stress granule nucleators, are embedded within virions and unexpectedly favor virion production. Furthermore, we show that G3BP1/2 participate in the formation of cytoplasmic membrane vesicles, that are likely virion assembly sites, consistent with a proviral role of G3BP1/2 in SARS-CoV-2 dissemination. Altogether, these findings provide new insights into host factors required for SARS-CoV-2 assembly with potential implications for future therapeutic targeting.
MeSH term(s)	Humans ; SARS-CoV-2/metabolism ; Virus Replication ; DNA Helicases/metabolism ; Proteomics ; RNA Recognition Motif Proteins/metabolism ; COVID-19/metabolism ; RNA Helicases/metabolism ; Poly-ADP-Ribose Binding Proteins/metabolism ; Virus Assembly ; Virion/metabolism
Chemical Substances	DNA Helicases (EC 3.6.4.-) ; RNA Recognition Motif Proteins ; RNA Helicases (EC 3.6.4.13) ; Poly-ADP-Ribose Binding Proteins ; G3BP1 protein, human (EC 3.6.4.12)
Language	English
Publishing date	2024-01-20
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-44958-0
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Article ; Online: ATG5 selectively engages virus-tethered BST2/tetherin in an LC3C-associated pathway.

Judith, Delphine / Versapuech, Margaux / Bejjani, Fabienne / Palaric, Marjory / Verlhac, Pauline / Kuster, Aurelia / Lepont, Leslie / Gallois-Montbrun, Sarah / Janvier, Katy / Berlioz-Torrent, Clarisse

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 20, Page(s) e2217451120

Abstract: Bone marrow stromal antigen 2 (BST2)/tetherin is a restriction factor that reduces HIV-1 dissemination by tethering virus at the cell surface. BST2 also acts as a sensor of HIV-1 budding, establishing a cellular antiviral state. The HIV-1 Vpu protein ... ...

Abstract	Bone marrow stromal antigen 2 (BST2)/tetherin is a restriction factor that reduces HIV-1 dissemination by tethering virus at the cell surface. BST2 also acts as a sensor of HIV-1 budding, establishing a cellular antiviral state. The HIV-1 Vpu protein antagonizes BST2 antiviral functions via multiple mechanisms, including the subversion of an LC3C-associated pathway, a key cell intrinsic antimicrobial mechanism. Here, we describe the first step of this viral-induced LC3C-associated process. This process is initiated at the plasma membrane through the recognition and internalization of virus-tethered BST2 by ATG5, an autophagy protein. ATG5 and BST2 assemble as a complex, independently of the viral protein Vpu and ahead of the recruitment of the ATG protein LC3C. The conjugation of ATG5 with ATG12 is dispensable for this interaction. ATG5 recognizes cysteine-linked homodimerized BST2 and specifically engages phosphorylated BST2 tethering viruses at the plasma membrane, in an LC3C-associated pathway. We also found that this LC3C-associated pathway is used by Vpu to attenuate the inflammatory responses mediated by virion retention. Overall, we highlight that by targeting BST2 tethering viruses, ATG5 acts as a signaling scaffold to trigger an LC3C-associated pathway induced by HIV-1 infection.
MeSH term(s)	Antiviral Agents/metabolism ; Bone Marrow Stromal Antigen 2 ; Cell Membrane/metabolism ; GPI-Linked Proteins/genetics ; GPI-Linked Proteins/metabolism ; Human Immunodeficiency Virus Proteins/genetics ; Human Immunodeficiency Virus Proteins/metabolism ; Viral Proteins/metabolism ; Viral Regulatory and Accessory Proteins/genetics ; Viral Regulatory and Accessory Proteins/metabolism ; Viruses/metabolism ; Humans
Chemical Substances	Antiviral Agents ; Bone Marrow Stromal Antigen 2 ; GPI-Linked Proteins ; Human Immunodeficiency Virus Proteins ; Viral Proteins ; Viral Regulatory and Accessory Proteins ; ATG5 protein, human ; MAP1LC3C protein, human
Language	English
Publishing date	2023-05-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2217451120
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Article ; Online: ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIIβ.

Judith, Delphine / Jefferies, Harold B J / Boeing, Stefan / Frith, David / Snijders, Ambrosius P / Tooze, Sharon A

The Journal of cell biology

2019 Volume 218, Issue 5, Page(s) 1634–1652

Abstract: ATG9A is a multispanning membrane protein essential for autophagy. Normally resident in Golgi membranes and endosomes, during amino acid starvation, ATG9A traffics to sites of autophagosome formation. ATG9A is not incorporated into autophagosomes but is ... ...

Abstract	ATG9A is a multispanning membrane protein essential for autophagy. Normally resident in Golgi membranes and endosomes, during amino acid starvation, ATG9A traffics to sites of autophagosome formation. ATG9A is not incorporated into autophagosomes but is proposed to supply so-far-unidentified proteins and lipids to the autophagosome. To address this function of ATG9A, a quantitative analysis of ATG9A-positive compartments immunoisolated from amino acid-starved cells was performed. These ATG9A vesicles are depleted of Golgi proteins and enriched in BAR-domain containing proteins, Arfaptins, and phosphoinositide-metabolizing enzymes. Arfaptin2 regulates the starvation-dependent distribution of ATG9A vesicles, and these ATG9A vesicles deliver the PI4-kinase, PI4KIIIβ, to the autophagosome initiation site. PI4KIIIβ interacts with ATG9A and ATG13 to control PI4P production at the initiation membrane site and the autophagic response. PI4KIIIβ and PI4P likely function by recruiting the ULK1/2 initiation kinase complex subunit ATG13 to nascent autophagosomes.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Autophagosomes/metabolism ; Autophagy ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Endosomes/metabolism ; HEK293 Cells ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/genetics ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Protein Transport ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism
Chemical Substances	ARFIP2 protein, human ; ATG13 protein, human ; Adaptor Proteins, Signal Transducing ; ATG9A protein, human ; Autophagy-Related Proteins ; Membrane Proteins ; Phosphatidylinositol Phosphates ; Vesicular Transport Proteins ; phosphatidylinositol 4-phosphate ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; phosphatidylinositol 4-kinase IIIbeta, human (EC 2.7.1.67)
Language	English
Publishing date	2019-03-27
Publishing country	United States
Document type	Journal Article ; 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.201901115
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Article: Unraveling membrane properties at the organelle-level with LipidDyn.

Scrima, Simone / Tiberti, Matteo / Campo, Alessia / Corcelle-Termeau, Elisabeth / Judith, Delphine / Foged, Mads Møller / Clemmensen, Knut Kristoffer Bundgaard / Tooze, Sharon A / Jäättelä, Marja / Maeda, Kenji / Lambrughi, Matteo / Papaleo, Elena

Computational and structural biotechnology journal

2022 Volume 20, Page(s) 3604–3614

Abstract: Cellular membranes are formed from different lipids in various amounts and proportions depending on the subcellular localization. The lipid composition of membranes is sensitive to changes in the cellular environment, and its alterations are linked to ... ...

Abstract	Cellular membranes are formed from different lipids in various amounts and proportions depending on the subcellular localization. The lipid composition of membranes is sensitive to changes in the cellular environment, and its alterations are linked to several diseases. Lipids not only form lipid-lipid interactions but also interact with other biomolecules, including proteins. Molecular dynamics (MD) simulations are a powerful tool to study the properties of cellular membranes and membrane-protein interactions on different timescales and resolutions. Over the last few years, software and hardware for biomolecular simulations have been optimized to routinely run long simulations of large and complex biological systems. On the other hand, high-throughput techniques based on lipidomics provide accurate estimates of the composition of cellular membranes at the level of subcellular compartments. Lipidomic data can be analyzed to design biologically relevant models of membranes for MD simulations. Similar applications easily result in a massive amount of simulation data where the bottleneck becomes the analysis of the data. In this context, we developed
Language	English
Publishing date	2022-06-30
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2694435-2
ISSN	2001-0370
ISSN	2001-0370
DOI	10.1016/j.csbj.2022.06.054
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Article: Unraveling membrane properties at the organelle-level with LipidDyn

Scrima, Simone / Tiberti, Matteo / Campo, Alessia / Corcelle-Termeau, Elisabeth / Judith, Delphine / Foged, Mads Møller / Clemmensen, Knut Kristoffer Bundgaard / Tooze, Sharon A. / Jäättelä, Marja / Maeda, Kenji / Lambrughi, Matteo / Papaleo, Elena

Computational and Structural Biotechnology Journal. 2022, v. 20

2022

Abstract	Cellular membranes are formed from different lipids in various amounts and proportions depending on the subcellular localization. The lipid composition of membranes is sensitive to changes in the cellular environment, and its alterations are linked to several diseases. Lipids not only form lipid-lipid interactions but also interact with other biomolecules, including proteins. Molecular dynamics (MD) simulations are a powerful tool to study the properties of cellular membranes and membrane-protein interactions on different timescales and resolutions. Over the last few years, software and hardware for biomolecular simulations have been optimized to routinely run long simulations of large and complex biological systems. On the other hand, high-throughput techniques based on lipidomics provide accurate estimates of the composition of cellular membranes at the level of subcellular compartments. Lipidomic data can be analyzed to design biologically relevant models of membranes for MD simulations. Similar applications easily result in a massive amount of simulation data where the bottleneck becomes the analysis of the data. In this context, we developed LipidDyn, a Python-based pipeline to streamline the analyses of MD simulations of membranes of different compositions. Once the simulations are collected, LipidDyn provides average properties and time series for several membrane properties such as area per lipid, thickness, order parameters, diffusion motions, lipid density, and lipid enrichment/depletion. The calculations exploit parallelization, and the pipeline includes graphical outputs in a publication-ready form. We applied LipidDyn to different case studies to illustrate its potential, including membranes from cellular compartments and transmembrane protein domains. LipidDyn is available free of charge under the GNU General Public License from https://github.com/ELELAB/LipidDyn.
Keywords	biotechnology ; computer software ; lipid composition ; lipidomics ; lipids ; molecular dynamics ; time series analysis ; transmembrane proteins
Language	English
Size	p. 3604-3614.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	2694435-2
ISSN	2001-0370
ISSN	2001-0370
DOI	10.1016/j.csbj.2022.06.054
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Article ; Online: Contribution of the Cytoplasmic Determinants of Vpu to the Expansion of Virus-Containing Compartments in HIV-1-Infected Macrophages.

Leymarie, Olivier / Lepont, Leslie / Versapuech, Margaux / Judith, Delphine / Abelanet, Sophie / Janvier, Katy / Berlioz-Torrent, Clarisse

Journal of virology

2019 Volume 93, Issue 11

Abstract: HIV-1 infection of macrophages leads to the sequestration of newly formed viruses in intracellular plasma membrane-connected structures termed virus-containing compartments (VCCs), where virions remain infectious and hidden from immune surveillance. The ... ...

Abstract	HIV-1 infection of macrophages leads to the sequestration of newly formed viruses in intracellular plasma membrane-connected structures termed virus-containing compartments (VCCs), where virions remain infectious and hidden from immune surveillance. The cellular restriction factor bone marrow stromal cell antigen 2 (BST2), which prevents HIV-1 dissemination by tethering budding viral particles at the plasma membrane, can be found in VCCs. The HIV-1 accessory protein Vpu counteracts the restriction factor BST2 by downregulating its expression and removing it from viral budding sites. Numerous studies described these Vpu countermeasures in CD4
MeSH term(s)	Antigens, CD/metabolism ; Bone Marrow Stromal Antigen 2/metabolism ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; GPI-Linked Proteins/genetics ; GPI-Linked Proteins/metabolism ; Gene Expression Regulation, Viral/genetics ; HEK293 Cells ; HIV Core Protein p24/metabolism ; HIV Infections/metabolism ; HIV Infections/virology ; HIV Seropositivity ; HIV-1/immunology ; HIV-1/metabolism ; HIV-1/pathogenicity ; HeLa Cells ; Human Immunodeficiency Virus Proteins/metabolism ; Human Immunodeficiency Virus Proteins/physiology ; Humans ; Macrophages/metabolism ; Macrophages/virology ; Viral Regulatory and Accessory Proteins/metabolism ; Viral Regulatory and Accessory Proteins/physiology ; Virion/metabolism ; Virus Assembly/physiology ; Virus Release/physiology
Chemical Substances	Antigens, CD ; Bone Marrow Stromal Antigen 2 ; GPI-Linked Proteins ; HIV Core Protein p24 ; Human Immunodeficiency Virus Proteins ; Viral Regulatory and Accessory Proteins ; vpu protein, Human immunodeficiency virus 1
Language	English
Publishing date	2019-05-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00020-19
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Article ; Online: Assessing mammalian autophagy.

Tooze, Sharon A / Dooley, Hannah C / Jefferies, Harold B J / Joachim, Justin / Judith, Delphine / Lamb, Christopher A / Razi, Minoo / Wirth, Martina

Methods in molecular biology (Clifton, N.J.)

2015 Volume 1270, Page(s) 155–165

Abstract: Autophagy (self-eating) is a highly conserved, vesicular pathway that cells use to eat pieces of themselves, including damaged organelles, protein aggregates or invading pathogens, for self-preservation and survival (Choi et al., N Engl J Med 368:651-662, ...

Abstract	Autophagy (self-eating) is a highly conserved, vesicular pathway that cells use to eat pieces of themselves, including damaged organelles, protein aggregates or invading pathogens, for self-preservation and survival (Choi et al., N Engl J Med 368:651-662, 2013; Lamb et al., Nat Rev Mol Cell Biol 14:759-774, 2013). Autophagy can be delineated into three major vesicular compartments (the phagophore, autophagosome, autolysosome, see Fig. 1). The initial stages of the pathway involve the formation of phagophores (also called isolation membranes), which are open, cup-shaped membranes that expand and sequester the cytosolic components, including organelles and aggregated proteins or intracellular pathogens. Closure of the phagophore creates an autophagosome, which is a double-membrane vesicle. Fusion of the autophagosome with the lysosome, to form an autolysosome, delivers the content of the autophagosome into the lysosomal lumen and allows degradation to occur.Autophagy is a dynamic process that is initiated within 15 min of amino acid starvation in cell culture systems (Köchl et al., Traffic 7:129-145, 2006) and is likely to occur as rapidly in vivo (Mizushima et al., J Cell Biol 152:657-668, 2001). To initiate studies on the formation of the autophagosomes, and trafficking to and from the autophagic pathway, an ideal starting approach is to do a morphological analysis in fixed cells. Additional validation of the morphological data can be obtained using simple Western blot analysis. Here we describe the most commonly used morphological technique to study autophagy, in particular, using the most reliable marker, microtubule-associated protein 1A/1B-light chain 3 (LC3). In addition, we describe a second immunofluorescence assay to determine if autophagy is being induced, using an antibody to WD repeat domain, phosphoinositide interacting 2 (WIPI2), an effector of the phosphatidylinositol (3)-phosphate (PI3P) produced during autophagosome formation.
MeSH term(s)	Animals ; Autophagy/physiology ; Blotting, Western ; Humans ; Lysosomes/metabolism ; Microscopy, Fluorescence ; Microtubule-Associated Proteins/metabolism ; Phagosomes/metabolism
Chemical Substances	Microtubule-Associated Proteins
Language	English
Publishing date	2015-02-16
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-2309-0_12
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Article ; Online: Activation of ULK Kinase and Autophagy by GABARAP Trafficking from the Centrosome Is Regulated by WAC and GM130.

Joachim, Justin / Jefferies, Harold B J / Razi, Minoo / Frith, David / Snijders, Ambrosius P / Chakravarty, Probir / Judith, Delphine / Tooze, Sharon A

Molecular cell

2015 Volume 60, Issue 6, Page(s) 899–913

Abstract: Starvation-induced autophagy requires activation of the ULK complex at the phagophore. Two Golgi proteins, WAC and GM130, regulate autophagy, however their mechanism of regulation is unknown. In search of novel interaction partners of WAC, we found that ... ...

Abstract	Starvation-induced autophagy requires activation of the ULK complex at the phagophore. Two Golgi proteins, WAC and GM130, regulate autophagy, however their mechanism of regulation is unknown. In search of novel interaction partners of WAC, we found that GM130 directly interacts with WAC, and this interaction is required for autophagy. WAC is bound to the Golgi by GM130. WAC and GM130 interact with the Atg8 homolog GABARAP and regulate its subcellular localization. GABARAP is on the pericentriolar matrix, and this dynamic pool contributes to autophagosome formation. Tethering of GABARAP to the Golgi by GM130 inhibits autophagy, demonstrating an unexpected role for a golgin. WAC suppresses GM130 binding to GABARAP, regulating starvation-induced centrosomal GABARAP delivery to the phagophore. GABARAP, unlipidated and lipidated, but not LC3B, GABARAPL1, and GATE-16, specifically promotes ULK kinase activation dependent on the ULK1 LIR motif, elucidating a unique non-hierarchical role for GABARAP in starvation-induced activation of autophagy.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Apoptosis Regulatory Proteins ; Autoantigens/metabolism ; Autophagy ; Cell Line ; Centrosome/metabolism ; Embryonic Stem Cells/cytology ; Embryonic Stem Cells/metabolism ; HCT116 Cells ; HEK293 Cells ; HeLa Cells ; Humans ; Membrane Proteins/metabolism ; Mice ; Microtubule-Associated Proteins/metabolism ; Protein Serine-Threonine Kinases/metabolism ; Protein Transport
Chemical Substances	Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; Autoantigens ; GABARAP protein, human ; Golgin subfamily A member 2 ; Membrane Proteins ; Microtubule-Associated Proteins ; WAC protein, human ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2015-12-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2015.11.018
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