Membrane tethering

Chia, Pei Zhi Cheryl; Gleeson, Paul A.

doi:10.12703/p6-74

Cited by 46 publications

(50 citation statements)

References 156 publications

(194 reference statements)

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“…More than 11 mammalian golgins have been identified localised throughout the Golgi stack . Collectively, golgins interact with a wide range of binding partners including small G proteins, Rabs and Arfs, SNAREs and microtubule and actin linker proteins and molecular motors .…”

Section: Membrane Scaffolds Of the Golgimentioning

confidence: 99%

Form and function of the Golgi apparatus: scaffolds, cytoskeleton and signalling

2019

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In addition to the classical functions of the Golgi in membrane transport and glycosylation, the Golgi apparatus of mammalian cells is now recognised to contribute to the regulation of a range of cellular processes, including mitosis, DNA repair, stress responses, autophagy, apoptosis and inflammation. These processes are often mediated, either directly or indirectly, by membrane scaffold molecules, such as golgins and GRASPs which are located on Golgi membranes. In many cases, these scaffold molecules also link the actin and microtubule cytoskeleton and influence Golgi morphology. An emerging theme is a strong relationship between the morphology of the Golgi and regulation of a variety of signalling pathways. Here, we review the molecular regulation of the morphology of the Golgi, especially the role of the golgins and other scaffolds in the interaction with the microtubule and actin networks. In addition, we discuss the impact of the modulation of the Golgi ribbon in various diseases, such as neurodegeneration and cancer, to the pathology of disease.

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Section: Membrane Scaffolds Of the Golgimentioning

confidence: 99%

Form and function of the Golgi apparatus: scaffolds, cytoskeleton and signalling

2019

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“…Tethering factors can be divided into two classes, long coiled-coil tethering factors and multi-subunit complexes (Lupashin and Sztul, 2005;Yu and Hughson, 2010). The long coiledcoil factors are large and can interact with vesicles at distances of up to 200 nm, whereas multi-subunit complexes consist of several protein subunits and can reach vesicles at distances of up to 30 nm (Jackson et al, 2012;Chia and Gleeson, 2014;Cheung and Pfeffer, 2016;Gillingham, 2018). In many cases, the exact mechanism of tethering factor function is still unclear.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of trans‐Golgi network t‐SNAREs rescues vacuolar trafficking and TGN morphology defects in a putative tethering factor mutant

et al. 2019

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Summary The trans‐Golgi network (TGN) is a major site for sorting of cargo to either the vacuole or apoplast. The TGN‐localized coiled‐coil protein TNO1 is a putative tethering factor that interacts with the TGN t‐SNARE SYP41 and is required for correct localization of the SYP61 t‐SNARE. An Arabidopsis thaliana tno1 mutant is hypersensitive to salt stress and partially mislocalizes vacuolar proteins to the apoplast, indicating a role in vacuolar trafficking. Here, we show that overexpression of SYP41 or SYP61 significantly increases SYP41–SYP61 complex formation in a tno1 mutant, and rescues the salt sensitivity and defective vacuolar trafficking of the tno1 mutant. The TGN is disrupted and vesicle budding from Golgi cisternae is reduced in the tno1 mutant, and these defects are also rescued by overexpression of SYP41 or SYP61. Our results suggest that the trafficking and Golgi morphology defects caused by loss of TNO1 can be rescued by increasing SYP41–SYP61 t‐SNARE complex formation, implicating TNO1 as a tethering factor mediating efficient vesicle fusion at the TGN.

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“…To maintain the fidelity of the secretory pathway, numerous conserved protein families regulate every step of the process 2 . Tethering factors, including the multi-subunit tethering complexes (MTCs), serve as the first, long-range, reversible connection between a vesicle and its target membrane 3,4 . However, in many cases experimental evidence demonstrating tethering by these factors is lacking 5 .…”

Section: Introductionmentioning

confidence: 99%

Subunit connectivity, assembly determinants and architecture of the yeast exocyst complex

Heider

Duffy

et al. 2015

Nat Struct Mol Biol

124

183

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The exocyst is a hetero-octameric complex proposed to serve as the tethering complex for exocytosis, although it remains poorly understood at the molecular level. Here, we purified endogenous exocyst from Saccharomyces cerevisiae, and show that the purified complexes are stable and consist of all eight subunits with equal stoichiometry. Using a combination of biochemical and auxin-induced degradation experiments in yeast, we mapped the subunit connectivity, identified two stable four-subunit modules within the octamer, and demonstrated that several known exocyst binding partners are not necessary for exocyst assembly and stability. Furthermore, we visualized the structure of the yeast complex using negative stain electron microscopy; our results indicate that exocyst exists predominantly as a stable, octameric complex with an elongated architecture that suggests the subunits are contiguous helical bundles packed together into a bundle of long rods.

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Membrane tethering

Cited by 46 publications

References 156 publications

Form and function of the Golgi apparatus: scaffolds, cytoskeleton and signalling

Form and function of the Golgi apparatus: scaffolds, cytoskeleton and signalling

Overexpression of trans‐Golgi network t‐SNAREs rescues vacuolar trafficking and TGN morphology defects in a putative tethering factor mutant

Subunit connectivity, assembly determinants and architecture of the yeast exocyst complex

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