[Todos] Fwd: [Todos FBMC] SEMINARIO CONJUNTO QB/IFIBYNE - Viernes 24 de octubre 15:30 h - Anton Khmelinskii

[Paula Felman]

>
>
>
>SEMINARIO CONJUNTO QU�MICA BIOLÓGICA / IFIBYNE
>
>VIERNES de octubre a las 15:30 h, Aula Cardini del Departamento de Química
>Biológica, 4to piso.
>----------------------------------------------------------------------------
>
>Expositor: Anton Khmelinskii
>Center for Molecular Biology of the University of Heidelberg (ZMBH),
>DKFZ-ZMBH Alliance, Heidelberg, Germany.
>
>"Functional profiling of the ubiquitin-proteasome system of protein
>degradation".
>
>Selective protein degradation contributes to cellular homeostasis through
>removal of unnecessary or damaged proteins. The ubiquitin-proteasome
>system (UPS) plays a key role in selective protein degradation, whereby a
>cascade of E1 ubiquitin-activating, E2 ubiquitin-conjugating and E3
>ubiquitin-protein ligase enzymes marks proteins with polyubiquitin chains
>for degradation by the proteasome. Deubiquitinating enzymes (DUBs), which
>remove ubiquitin marks from target proteins and replenish the pool of free
>ubiquitin, are involved at various stages of the targeting and degradation
>processes. Despite the central role of the UPS in protein degradation,
>many UPS components are poorly characterized, various E3 ligases have no
>known substrates and the functions of DUBs are not well understood. To
>help bridge these gaps, we generated a genome-wide library tailored for in
>vivo analysis of proteome dynamics in the budding yeast Saccharomyces
>cerevisiae. This library consists of ~ 4000 strains each expressing a
>different protein endogenously tagged with a tandem fluorescent protein
>timer (tFT). The tFT is composed of two fluorescent proteins with distinct
>kinetics of fluorophore maturation and reports on the abundance and
>degradation kinetics of the tagged proteins.
>We applied this resource to systematically analyze the role of different
>UPS components in proteome turnover. Using synthetic genetic array
>technology followed by high-throughput whole colony fluorescence imaging,
>the abundance and stability of each fusion in the tFT library were
>measured in strains carrying mutations in key UPS components. Our
>experiments provide evidence for the existence of a novel protein quality
>control pathway at the inner nuclear membrane and it's interplay with
>endoplasmic reticulum-associated protein degradation.
>----------------------------------------------------------------------------
>
>Los esperamos!
>_______________________________________________
>Todos mailing list
><mailto:Todos en cerebro.fbmc.fcen.uba.ar>Todos en cerebro.fbmc.fcen.uba.ar
>http://cerebro.fbmc.fcen.uba.ar/mailman/listinfo/todos
>
>
>
>--
>Alejandro Colman-Lerner
------------ próxima parte ------------
Se ha borrado un adjunto en formato HTML...
URL: http://mail.df.uba.ar/pipermail/todos/attachments/20141023/612460db/attachment.html