COPI selectively drives maturation of the early Golgi

Papanikou, Effrosyni; Day, Kasey J.; Austin, Jotham R.; Glick, Benjamin S.

doi:10.7554/elife.13232

Cited by 76 publications

(124 citation statements)

References 150 publications

(205 reference statements)

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“…Aberrant Golgi morphology has been observed under conditions that alter ER to Golgi traffic and traffic through and from the Golgi, probably because of a disequilibrium between protein and lipid input and output ratios (Ward et al 2001;Bhave et al 2014;Papanikou et al 2015). We have found physical and functional interaction between exomer and AP-1, but not between exomer and COPI and COPII.…”

Section: Discussionmentioning

confidence: 61%

“…Also, secretion of acid phosphatase is efficient in exomer mutants (results not shown). Nevertheless, although the role of COPI in vesicle trafficking is well-established, COPI-deficient S. cerevisiae mutants exhibit aberrant Golgi apparatuses able to promote secretion to almost WT levels (Papanikou et al 2015); thus, the fact that secretion is efficient in S. pombe exomer mutants does not necessarily imply that the role of exomer in protein trafficking is not relevant.…”

Section: Discussionmentioning

confidence: 99%

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Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast

et al. 2017

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Despite its biological and medical relevance, traffic from the Golgi to the plasma membrane (PM) is one of the least understood steps of secretion. Exomer is a protein complex that mediates the trafficking of certain cargoes from the trans-Golgi network/early endosomes to the PM in budding yeast. Here, we show that in Schizosaccharomyces pombe the Cfr1 and Bch1 proteins constitute the simplest form of an exomer. Cfr1 co-immunoprecipitates with Assembly Polypeptide adaptor 1 (AP-1), AP-2, and Golgi-localized, gamma-adaptin ear domain homology, ARF-binding (GGA) subunits, and cfr1 + interacts genetically with AP-1 and GGA genes. Exomer-defective cells exhibit multiple mild defects, including alterations in the morphology of Golgi stacks and the distribution of the synaptobrevin-like Syb1 protein, carboxypeptidase missorting, and stress sensitivity. S. pombe apm1D cells exhibit a defect in trafficking through the early endosomes that is severely aggravated in the absence of exomer. apm1D cfr1D cells exhibit a dramatic disorganization of intracellular compartments, including massive accumulation of electron-dense tubulovesicular structures. While the trans-Golgi network/early endosomes are severely disorganized in the apm1D cfr1D strain, gga21D gga22D cfr1D cells exhibit a significant disturbance of the prevacuolar/vacuolar compartments. Our findings show that exomer collaborates with clathrin adaptors in trafficking through diverse cellular compartments, and that this collaboration is important to maintain their integrity. These results indicate that the effect of eliminating exomer is more pervasive than that described to date, and suggest that exomer complexes might participate in diverse steps of vesicle transport in other organisms.

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Section: Discussionmentioning

confidence: 61%

Section: Discussionmentioning

confidence: 99%

Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast

et al. 2017

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“…Full-length myosin VI was incorporated into baculovirus for expression in SF9 cells using the BestBac system by Expression Systems, according to the manufacturer's guidelines. An mCherry2B (62) with an N-terminal FLAG tag was first incorporated at the myosin VI N terminus within the pET vector before insertion into a modified pBlueBac plasmid via SLiCE cloning due to the large sizes of the fragments (63). We fused mCherry2B to it to improve solubility, reduce dimerization, and increase fluorescence of the protein over mCherry (62).…”

Section: Methodsmentioning

confidence: 99%

Investigations of human myosin VI targeting using optogenetically controlled cargo loading

French

Sosnick

Rock

2017

Proc. Natl. Acad. Sci. U.S.A.

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Myosins play countless critical roles in the cell, each requiring it to be activated at a specific location and time. To control myosin VI with this specificity, we created an optogenetic tool for activating myosin VI by fusing the light-sensitive Avena sativa phototropin1 LOV2 domain to a peptide from Dab2 (LOVDab), a myosin VI cargo protein. Our approach harnesses the native targeting and activation mechanism of myosin VI, allowing direct inferences on myosin VI function. LOVDab robustly recruits human full-length myosin VI to various organelles in vivo and hinders peroxisome motion in a lightcontrollable manner. LOVDab also activates myosin VI in an in vitro gliding filament assay. Our data suggest that protein and lipid cargoes cooperate to activate myosin VI, allowing myosin VI to integrate Ca 2+, lipid, and protein cargo signals in the cell to deploy in a site-specific manner.otor proteins play countless roles in biology, each requiring the motor to be recruited and activated at a particular time and place inside the cell. To dissect these multiple roles, we must develop tools that allow us to control the recruitment and activation process. One promising technique for achieving this goal is through optogenetics (1). Optogenetics involves the engineering and application of optically controlled, genetically encoded proteins and is transforming the fields of neuro-and cell biology (2, 3). A major benefit of optogenetics is that proteins are activated using light, which allows for high temporal and spatial control over a protein of interest.Myosin VI is a motor protein whose study could particularly benefit from optogenetic control. It is the only myosin known to walk toward the pointed end of actin filaments (4, 5). This property enables it to perform a diverse array of cellular functions, including cell division, endosome trafficking, autophagy, and Golgi and plasma membrane anchoring (6-9). Myosin VI is also autoinhibited, a property that is commonly found in other myosins (10). When myosin VI binds to cargo through specialized adaptor proteins, this autoinhibition is relieved through a poorly understood mechanism likely involving the disruption of an interaction between its cargo binding domain (CBD) and the myosin head (11,12). Dissociation of the CBD from the head both frees the head to bind tightly to actin and exposes dimerization sites throughout the tail domain of myosin VI, allowing it to become a processive dimer (13-15). In some cases, myosin VI could conceivably function as a monomer, for example when fulfilling its role as a membrane tether during spermatid individualization (16). If this is the case, more work is needed to elucidate the cellular signals that determine its oligomeric state at each site of action.Myosin VI has two classes of cargo proteins that bind to distinct, conserved motifs on the myosin VI C terminus (17). Disabled2, or Dab2, belongs to the class of cargo proteins that bind to a conserved WWY site on myosin (18). Optineurin (OPTN) is a member of the second class that binds ...

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“…Namely, vesicles are formed by the budding machinery, which comprises COPI (coat protein complex I) and the Arf GTPase, and are targeted to a particular cisterna by the fusion machinery, which involves tethers, Rab GTPases, NSF (N-ethylmaleimide-sensitive factor), SNAP (soluble NSF-attachment protein) and SNAREs (SNAP receptors). Indeed, the cisternal maturation in yeast is strictly controlled by COPI, again supporting the main frame of the model (Ishii et al, 2016;Papanikou et al, 2015). It should also be noticed, however, that tubular extensions and interconnections can also play roles in intra-Golgi transport (Glick and Luini, 2011;Glick and Nakano, 2009).…”

Section: Introductionmentioning

confidence: 97%

A Missense Mutation in the <i>NSF</i> Gene Causes Abnormal Golgi Morphology in <i>Arabidopsis thaliana</i>

Tanabashi

Shoda

Saito

et al. 2018

Cell Struct. Funct.

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The Golgi apparatus is a key station of glycosylation and membrane traffic. It consists of stacked cisternae in most eukaryotes. However, the mechanisms how the Golgi stacks are formed and maintained are still obscure. The model plant Arabidopsis thaliana provides a nice system to observe Golgi structures by light microscopy, because the Golgi in A. thaliana is in the form of mini-stacks that are distributed throughout the cytoplasm. To obtain a clue to understand the molecular basis of Golgi morphology, we took a forward-genetic approach to isolate A. thaliana mutants that show abnormal structures of the Golgi under a confocal microscope. In the present report, we describe characterization of one of such mutants, named #46-3. The #46-3 mutant showed pleiotropic Golgi phenotypes. The Golgi size was in majority smaller than the wild type, but varied from very small ones, sometimes without clear association of cis and trans cisternae, to abnormally large ones under a confocal microscope.At the ultrastructual level by electron microscopy, queer-shaped large Golgi stacks were occasionally observed. By positional mapping, genome sequencing, and complementation and allelism tests, we linked the mutant phenotype to the missense mutation D374N in the NSF gene, encoding the N-ethylmaleimide-sensitive factor (NSF), a key component of membrane fusion. This residue is near the ATP-binding site of NSF, which is very well conserved in eukaryotes, suggesting that the biochemical function of NSF is important for maintaining the normal morphology of the Golgi.3

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COPI selectively drives maturation of the early Golgi

Cited by 76 publications

References 150 publications

Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast

Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast

Investigations of human myosin VI targeting using optogenetically controlled cargo loading

A Missense Mutation in the <i>NSF</i> Gene Causes Abnormal Golgi Morphology in <i>Arabidopsis thaliana</i>

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