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Article ; Online: Vesicle transport: Exocyst follows PIP

Langemeyer, Lars / Ungermann, Christian

2022 Volume 32, Issue 13, Page(s) R748–R750

Abstract: A new study uses reconstituted, functional octameric exocyst complex to provide new insights into the assembly of this tethering complex and reveal how the activity of the lipid kinase PIP5K1C stimulated by Arf6 on exocytic vesicles allows for exocyst- ... ...

Abstract	A new study uses reconstituted, functional octameric exocyst complex to provide new insights into the assembly of this tethering complex and reveal how the activity of the lipid kinase PIP5K1C stimulated by Arf6 on exocytic vesicles allows for exocyst-mediated tethering at the plasma membrane.
MeSH term(s)	Biological Transport ; Cytoplasm/metabolism ; Exocytosis ; Secretory Vesicles/metabolism ; Vesicular Transport Proteins/metabolism
Chemical Substances	Vesicular Transport Proteins
Language	English
Publishing date	2022-07-09
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.2022.05.026
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Article ; Online: Highlight: on the past and the future of cellular microcompartments.

Galic, Milos / Ungermann, Christian / Cosentino, Katia

Biological chemistry

2023 Volume 404, Issue 5, Page(s) 377–378

MeSH term(s)	Bacterial Proteins ; Organelles
Chemical Substances	Bacterial Proteins
Language	English
Publishing date	2023-03-24
Publishing country	Germany
Document type	Editorial
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2023-0153
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Article ; Online: Targeting of the Mon1-Ccz1 Rab guanine nucleotide exchange factor to distinct organelles by a synergistic protein and lipid code.

Herrmann, Eric / Langemeyer, Lars / Auffarth, Kathrin / Ungermann, Christian / Kümmel, Daniel

The Journal of biological chemistry

2023 Volume 299, Issue 3, Page(s) 102915

Abstract: Activation of the small GTPase Rab7 by its cognate guanine nucleotide exchange factor Mon1-Ccz1 (MC1) is a key step in the maturation of endosomes and autophagosomes. This process is tightly regulated and subject to precise spatiotemporal control of MC1 ... ...

Abstract	Activation of the small GTPase Rab7 by its cognate guanine nucleotide exchange factor Mon1-Ccz1 (MC1) is a key step in the maturation of endosomes and autophagosomes. This process is tightly regulated and subject to precise spatiotemporal control of MC1 localization, but the mechanisms that underly MC1 localization have not been fully elucidated. We here identify and characterize an amphipathic helix in Ccz1, which is required for the function of Mon-Ccz1 in autophagy, but not endosomal maturation. Furthermore, our data show that the interaction of the Ccz1 amphipathic helix with lipid packing defects, binding of Mon1 basic patches to positively charged lipids, and association of MC1 with recruiter proteins collectively govern membrane recruitment of the complex in a synergistic and redundant manner. Membrane binding enhances MC1 activity predominantly by increasing enzyme and substrate concentration on the membrane, but interaction with recruiter proteins can further stimulate the guanine nucleotide exchange factor. Our data demonstrate that specific protein and lipid cues convey the differential targeting of MC1 to endosomes and autophagosomes. In conclusion, we reveal the molecular basis for how MC1 is adapted to recognize distinct target compartments by exploiting the unique biophysical properties of organelle membranes and thus provide a model for how the complex is regulated and activated independently in different functional contexts.
MeSH term(s)	Vesicular Transport Proteins/metabolism ; Protein Transport ; rab GTP-Binding Proteins/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Endosomes/metabolism ; Lipids
Chemical Substances	Vesicular Transport Proteins ; rab GTP-Binding Proteins (EC 3.6.5.2) ; Guanine Nucleotide Exchange Factors ; Lipids
Language	English
Publishing date	2023-01-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.102915
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Article ; Online: Molecular insights into endolysosomal microcompartment formation and maintenance.

Kümmel, Daniel / Herrmann, Eric / Langemeyer, Lars / Ungermann, Christian

Biological chemistry

2022 Volume 404, Issue 5, Page(s) 441–454

Abstract: The endolysosomal system of eukaryotic cells has a key role in the homeostasis of the plasma membrane, in signaling and nutrient uptake, and is abused by viruses and pathogens for entry. Endocytosis of plasma membrane proteins results in vesicles, which ... ...

Abstract	The endolysosomal system of eukaryotic cells has a key role in the homeostasis of the plasma membrane, in signaling and nutrient uptake, and is abused by viruses and pathogens for entry. Endocytosis of plasma membrane proteins results in vesicles, which fuse with the early endosome. If destined for lysosomal degradation, these proteins are packaged into intraluminal vesicles, converting an early endosome to a late endosome, which finally fuses with the lysosome. Each of these organelles has a unique membrane surface composition, which can form segmented membrane microcompartments by membrane contact sites or fission proteins. Furthermore, these organelles are in continuous exchange due to fission and fusion events. The underlying machinery, which maintains organelle identity along the pathway, is regulated by signaling processes. Here, we will focus on the Rab5 and Rab7 GTPases of early and late endosomes. As molecular switches, Rabs depend on activating guanine nucleotide exchange factors (GEFs). Over the last years, we characterized the Rab7 GEF, the Mon1-Ccz1 (MC1) complex, and key Rab7 effectors, the HOPS complex and retromer. Structural and functional analyses of these complexes lead to a molecular understanding of their function in the context of organelle biogenesis.
MeSH term(s)	rab GTP-Binding Proteins/metabolism ; Endosomes/metabolism ; Lysosomes/metabolism ; Biological Transport ; Cell Membrane/metabolism
Chemical Substances	rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-12-13
Publishing country	Germany
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2022-0294
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Article ; Online: vCLAMPs-an intimate link between vacuoles and mitochondria.

Ungermann, Christian

Current opinion in cell biology

2015 Volume 35, Page(s) 30–36

Abstract: Membrane contact sites connect various organelles of the cell without fusing their membranes, thus allowing the exchange of ions, metabolites and lipids across short distances between membranes that are independent of vesicular transport. Whereas ER- ... ...

Abstract	Membrane contact sites connect various organelles of the cell without fusing their membranes, thus allowing the exchange of ions, metabolites and lipids across short distances between membranes that are independent of vesicular transport. Whereas ER-mitochondrial contacts are long known, contacts between the endolysosomal system and mitochondria only recently came into the limelight. Within this review, I will provide recent insights into this contact site, it's possible regulation and cellular function.
MeSH term(s)	Animals ; Biological Transport ; Endoplasmic Reticulum/metabolism ; Endosomes/metabolism ; Humans ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Vacuoles/metabolism
Language	English
Publishing date	2015-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1026381-0
ISSN	1879-0410 ; 0955-0674
ISSN (online)	1879-0410
ISSN	0955-0674
DOI	10.1016/j.ceb.2015.03.006
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Article ; Online: Structure of the metazoan Rab7 GEF complex Mon1-Ccz1-Bulli.

Herrmann, Eric / Schäfer, Jan-Hannes / Wilmes, Stephan / Ungermann, Christian / Moeller, Arne / Kümmel, Daniel

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

2023 Volume 120, Issue 20, Page(s) e2301908120

Abstract: The endosomal system of eukaryotic cells represents a central sorting and recycling compartment linked to metabolic signaling and the regulation of cell growth. Tightly controlled activation of Rab GTPases is required to establish the different domains ... ...

Abstract	The endosomal system of eukaryotic cells represents a central sorting and recycling compartment linked to metabolic signaling and the regulation of cell growth. Tightly controlled activation of Rab GTPases is required to establish the different domains of endosomes and lysosomes. In metazoans, Rab7 controls endosomal maturation, autophagy, and lysosomal function. It is activated by the guanine nucleotide exchange factor (GEF) complex Mon1-Ccz1-Bulli (MCBulli) of the tri-longin domain (TLD) family. While the Mon1 and Ccz1 subunits have been shown to constitute the active site of the complex, the role of Bulli remains elusive. We here present the cryo-electron microscopy (cryo-EM) structure of MCBulli at 3.2 Å resolution. Bulli associates as a leg-like extension at the periphery of the Mon1 and Ccz1 heterodimers, consistent with earlier reports that Bulli does not impact the activity of the complex or the interactions with recruiter and substrate GTPases. While MCBulli shows structural homology to the related ciliogenesis and planar cell polarity effector (Fuzzy-Inturned-Wdpcp) complex, the interaction of the TLD core subunits Mon1-Ccz1 and Fuzzy-Inturned with Bulli and Wdpcp, respectively, is remarkably different. The variations in the overall architecture suggest divergent functions of the Bulli and Wdpcp subunits. Based on our structural analysis, Bulli likely serves as a recruitment platform for additional regulators of endolysosomal trafficking to sites of Rab7 activation.
MeSH term(s)	Animals ; Vesicular Transport Proteins/metabolism ; Cryoelectron Microscopy ; Protein Transport ; rab GTP-Binding Proteins/metabolism ; Endosomes/metabolism ; Guanine Nucleotide Exchange Factors/metabolism
Chemical Substances	Vesicular Transport Proteins ; rab GTP-Binding Proteins (EC 3.6.5.2) ; Guanine Nucleotide Exchange Factors
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.2301908120
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Zs.A 1148: Show issues

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Article ; Online: An online gathering about the latest on molecular membrane biology.

Bottanelli, Francesca / Spang, Anne / Stefan, Chris / Ungermann, Christian

The Journal of biological chemistry

2021 Volume 297, Issue 5, Page(s) 101237

MeSH term(s)	Cell Membrane ; Congresses as Topic ; Humans ; Molecular Biology
Language	English
Publishing date	2021-09-24
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.101237
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Article ; Online: Who's in control? Principles of Rab GTPase activation in endolysosomal membrane trafficking and beyond.

Borchers, Ann-Christin / Langemeyer, Lars / Ungermann, Christian

The Journal of cell biology

2021 Volume 220, Issue 9

Abstract: The eukaryotic endomembrane system consists of multiple interconnected organelles. Rab GTPases are organelle-specific markers that give identity to these membranes by recruiting transport and trafficking proteins. During transport processes or along ... ...

Abstract	The eukaryotic endomembrane system consists of multiple interconnected organelles. Rab GTPases are organelle-specific markers that give identity to these membranes by recruiting transport and trafficking proteins. During transport processes or along organelle maturation, one Rab is replaced by another, a process termed Rab cascade, which requires at its center a Rab-specific guanine nucleotide exchange factor (GEF). The endolysosomal system serves here as a prime example for a Rab cascade. Along with endosomal maturation, the endosomal Rab5 recruits and activates the Rab7-specific GEF Mon1-Ccz1, resulting in Rab7 activation on endosomes and subsequent fusion of endosomes with lysosomes. In this review, we focus on the current idea of Mon1-Ccz1 recruitment and activation in the endolysosomal and autophagic pathway. We compare identified principles to other GTPase cascades on endomembranes, highlight the importance of regulation, and evaluate in this context the strength and relevance of recent developments in in vitro analyses to understand the underlying foundation of organelle biogenesis and maturation.
MeSH term(s)	Animals ; Autophagosomes/genetics ; Autophagosomes/metabolism ; Biological Transport ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Conserved Sequence ; Endosomes/genetics ; Endosomes/metabolism ; Gene Expression Regulation ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Lysosomes/genetics ; Lysosomes/metabolism ; Organelle Biogenesis ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism ; rab5 GTP-Binding Proteins/genetics ; rab5 GTP-Binding Proteins/metabolism ; rab7 GTP-Binding Proteins
Chemical Substances	Ccz1 protein, S cerevisiae ; Guanine Nucleotide Exchange Factors ; Mon1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Vesicular Transport Proteins ; rab7 GTP-Binding Proteins ; rab7 GTP-binding proteins, human ; rab GTP-Binding Proteins (EC 3.6.5.2) ; rab5 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2021-08-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202105120
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Article ; Online: Structure of membrane tethers and their role in fusion.

Ungermann, Christian / Kümmel, Daniel

Traffic (Copenhagen, Denmark)

2019 Volume 20, Issue 7, Page(s) 479–490

Abstract: Vesicular transport between different membrane compartments is a key process in cell biology required for the exchange of material and information. The complex machinery that executes the formation and delivery of transport vesicles has been intensively ... ...

Abstract	Vesicular transport between different membrane compartments is a key process in cell biology required for the exchange of material and information. The complex machinery that executes the formation and delivery of transport vesicles has been intensively studied and yielded a comprehensive view of the molecular principles that underlie the budding and fusion process. Tethering also represents an essential step in each trafficking pathway. It is mediated by Rab GTPases in concert with so-called tethering factors, which constitute a structurally diverse family of proteins that share a similar role in promoting vesicular transport. By simultaneously binding to proteins and/or lipids on incoming vesicles and the target compartment, tethers are thought to bridge donor and acceptor membrane. They thus provide specificity while also promoting fusion. However, how tethering works at a mechanistic level is still elusive. We here discuss the recent advances in the structural and biochemical characterization of tethering complexes that provide novel insight on how these factors might contribute the efficiency of fusion.
MeSH term(s)	Animals ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Humans ; Membrane Fusion ; Transport Vesicles/chemistry ; Transport Vesicles/metabolism ; Vesicular Transport Proteins/chemistry ; Vesicular Transport Proteins/metabolism
Chemical Substances	Vesicular Transport Proteins
Language	English
Publishing date	2019-05-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12655
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Zs.A 5634: Show issues

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Article ; Online: Cargo induces retromer-mediated membrane remodeling on membranes.

Purushothaman, Latha Kallur / Ungermann, Christian

Molecular biology of the cell

2018 Volume 29, Issue 22, Page(s) 2709–2719

Abstract: Endosomes serve as a central sorting station of lipids and proteins that arrive via vesicular carrier from the plasma membrane and the Golgi complex. At the endosome, retromer complexes sort selected receptors and membrane proteins into tubules or ... ...

Abstract	Endosomes serve as a central sorting station of lipids and proteins that arrive via vesicular carrier from the plasma membrane and the Golgi complex. At the endosome, retromer complexes sort selected receptors and membrane proteins into tubules or vesicles that bud off the endosome. The mature endosome finally fuses with the lysosome. Retromer complexes consist of a cargo selection complex (CSC) and a membrane remodeling part (sorting nexin [SNX]-Bin/amphiphysin/Rvs [BAR], or Snx3 in yeast) and different assemblies of retromer mediate recycling of different cargoes. Due to this complexity, the exact order of events that results in carrier formation is not yet understood. Here, we reconstituted this process on giant unilamellar vesicles together with purified retromer complexes from yeast and selected cargoes. Our data reveal that the membrane remodeling activity of both Snx3 and the SNX-BAR complex is strongly reduced at low concentrations, which can be reactivated by CSC. At even lower concentrations, these complexes still associate with membranes, but only remodel membranes in the presence of their specific cargoes. Our data thus favor a simple model, where cargo functions as a specific trigger of retromer-mediated sorting on endosomes.
MeSH term(s)	Cell Membrane/metabolism ; Multiprotein Complexes/metabolism ; Nerve Tissue Proteins/metabolism ; Protein Transport ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Sorting Nexins/metabolism
Chemical Substances	Multiprotein Complexes ; Nerve Tissue Proteins ; Saccharomyces cerevisiae Proteins ; Sorting Nexins ; amphiphysin (147954-52-7)
Language	English
Publishing date	2018-09-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E18-06-0339
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