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Autophagy: molecular mechanisms and disease outcomes# o# K# E" R, g! h6 g" Z
Daniel J. Klionsky and Vojo Deretic& l: z$ v4 U. h0 }" s
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Article bodyDuring autophagy, double-membrane structures called autophagosomes engulf cytosol or organelles and deliver them to lysosomes (in mammalian cells) or the vacuole (in yeast) to be degraded and recycled. Our molecular understanding of this process has greatly advanced in the past decade, in terms of both the signalling pathways that drive it and the membrane trafficking events that participate in the formation of the autophagosome. Furthermore, the finding that autophagy is implicated in human pathophysiologies, including tumorigenesis and neurodegeneration, has highlighted its role as a dynamic and selective cellular process.
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7 _# o% O" i" A7 X3 d! [9 C' YThis Poster by Daniel J. Klionsky and Vojo Deretic provides an overview of the subcellular control of autophagy in yeast and mammals, and emphasizes the recent links between autophagy and human disease.
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Fluorescent proteins illuminate cell biology/ \) O1 B8 _, j% B/ |
Michael Z. Lin, Atsushi Miyawaki and Roger Y. Tsien ~/ l7 i, U! @, z% l% X
( l1 k H M" J7 L3 Y0 x4 e- BArticle bodyThe discovery that green fluorescent protein (GFP) from the jellyfish Aequorea victoria could be used to label proteins in cells led to a revolution in our ability to track proteins in live cells and whole organisms. A bewildering range of fluorescent proteins and sensors are now available that span the fluorescent spectrum, and together these provide the opportunity to dissect cell biological processes with exquisite spatiotemporal resolution.
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This poster by Michael Z. Lin, Atsushi Miyawaki and Roger Y. Tsien provides a user's guide to the range of fluorescent proteins and sensors available, their key properties and the cell biological questions to which they can be best applied.
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Ubiquitin signalling by ubiquitin-binding domains/ X5 `5 _8 f. N! p0 ]& |9 \
Nicola Crosetto, David Komander and Ivan Dikic: j f2 Y2 Y& _/ W: t1 g v+ m. Z
+ H! A, j7 Q5 p" fArticle bodyUbiquitylation is a highly regulated process that tags proteins to specify distinct functional outcomes. Ubiquitin signals are 'read' non-covalently by ubiquitin-binding domains (UBDs) embedded on various proteins, which show preference for ubiquitin chains of different lengths and linkages. More than 20 types of UBDs have been recognized, which have been classified into 5 families on the basis of their three-dimensional structure. Studies have revealed the importance of ubiquitin–UBD interactions in several cellular processes, including proteolysis, endocytosis and DNA repair.
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This Poster by Nicola Crosetto, David Komander and Ivan Dikic provides structural information on ubiquitin signals and UBDs, and schematically presents the molecular outputs of ubiquitin–UBD interactions and the cellular processes they are involved in.
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v! d4 K" U' W, e# Y( D I' {7 F( ZCellular regulation by deubiquitinating enzymes& n: m# U! ?! H! V
Eric J. Bennett, Mathew E. Sowa and J. Wade Harper
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0 u# v) ^8 R0 k* mArticle bodyUbiquitination is a reversible post-translational modification with key roles in protein stability, as well as in various signal transduction cascades, membrane trafficking and mitosis. Much progress has been made in the characterization of a superfamily of isopeptidases that remove ubiquitin from substrates — the deubiquitinating enzymes (DUBs). Far from merely processing ubiquitin precursors and scavenging ubiquitin from substrates that are targeted for degradation, DUBs are dynamic enzymes that assemble into distinct protein complexes to process the numerous different monoubiquitin and polyubiquitin marks on substrates.# ?+ w1 s8 G. z7 i- k6 Y/ t
) o( A* c% K. q0 _3 I WThis Poster by Eric J. Bennett, Mathew E. Sowa and J. Wade Harper provides a schematic overview of the different DUB families and highlights the cellular pathways in which some DUB-associated complexes act.3 ?( t1 V5 x# m# X( e" E
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发表于 2010-12-12 21:44
发表于 2010-12-13 09:17
