Bayesian semiparametric multivariate stochastic volatility with application

In this article, we establish a Cholesky-type multivariate stochastic volatility estimation framework, in which we let the innovation vector follow a Dirichlet process mixture (DPM), thus enabling us to model highly flexible return distributions. The Cholesky decomposition allows parallel univariate process modeling and creates potential for estimating high-dimensional specifications. We use Markov chain Monte Carlo methods for posterior simulation and predictive density computation. We apply our framework to a five-dimensional stock-return data set and analyze international stockmarket co-movements among the largest stock markets. The empirical results show that our DPM modeling of the innovation vector yields substantial gains in out-of-sample density forecast accuracy when compared with the prevalent benchmark models

Bayesian semiparametric multivariate stochastic volatility with application

In this article, we establish a Cholesky-type multivariate stochastic volatility estimation framework, in which we let the innovation vector follow a Dirichlet process mixture (DPM), thus enabling us to model highly flexible return distributions. The Cholesky decomposition allows parallel univariate process modeling and creates potential for estimating high-dimensional specifications. We use Markov chain Monte Carlo methods for posterior simulation and predictive density computation. We apply our framework to a five-dimensional stock-return data set and analyze international stock-market co-movements among the largest stock markets. The empirical results show that our DPM modeling of the innovation vector yields substantial gains in out-of-sample density forecast accuracy when compared with the prevalent benchmark models

A Selective Autophagy Pathway for Phase-Separated Endocytic Protein Deposits

Autophagy eliminates cytoplasmic content selected by autophagy receptors, which link cargo to the membrane-bound autophagosomal ubiquitin-like protein Atg8/LC3. Here, we report a selective autophagy pathway for protein condensates formed by endocytic proteins in yeast. In this pathway, the endocytic protein Ede1 functions as a selective autophagy receptor. Distinct domains within Ede1 bind Atg8 and mediate phase separation into condensates. Both properties are necessary for an Ede1-dependent autophagy pathway for endocytic proteins, which differs from regular endocytosis and does not involve other known selective autophagy receptors but requires the core autophagy machinery. Cryo-electron tomography of Ede1-containing condensates, at the plasma membrane and in autophagic bodies, shows a phase-separated compartment at the beginning and end of the Ede1-mediated selective autophagy route. Our data suggest a model for autophagic degradation of macromolecular protein complexes by the action of intrinsic autophagy receptors

Selective autophagy degrades nuclear pore complexes

Nuclear pore complexes (NPCs) are very large proteinaceous assemblies that consist of more than 500 individual proteins1,2. NPCs are essential for nucleocytoplasmic transport of different cellular components, and disruption of the integrity of NPCs has been linked to aging, cancer and neurodegenerative diseases3-7. However, the mechanism by which membrane-embedded NPCs are turned over is currently unknown. Here we show that, after nitrogen starvation or genetic interference with the architecture of NPCs, nucleoporins are rapidly degraded in the budding yeast Saccharomyces cerevisiae. We demonstrate that NPC turnover involves vacuolar proteases and the core autophagy machinery. Autophagic degradation is mediated by the cytoplasmically exposed Nup159, which serves as intrinsic cargo receptor and directly binds to the autophagy marker protein Atg8. Autophagic degradation of NPCs is therefore inducible, enabling the removal of individual NPCs from the nuclear envelope

COPI buds 60-nm lipid droplets from reconstituted water-phospholipid-triacylglyceride interfaces, suggesting a tension clamp function

Intracellular trafficking between organelles is achieved by coat protein complexes, coat protomers, that bud vesicles from bilayer membranes. Lipid droplets are protected by a monolayer and thus seem unsuitable targets for coatomers. Unexpectedly, coat protein complex I (COPI) is required for lipid droplet targeting of some proteins, suggesting a possible direct interaction between COPI and lipid droplets. Here, we find that COPI coat components can bud 60-nm triacylglycerol nanodroplets from artificial lipid droplet (LD) interfaces. This budding decreases phospholipid packing of the monolayer decorating the mother LD. As a result, hydrophobic triacylglycerol molecules become more exposed to the aqueous environment, increasing LD surface tension. In vivo, this surface tension increase may prime lipid droplets for reactions with neighboring proteins or membranes. It provides a mechanism fundamentally different from transport vesicle formation by COPI, likely responsible for the diverse lipid droplet phenotypes associated with depletion of COPI subunits