نتایج جستجو برای: trapp

تعداد نتایج: 224  

2012
Hichem Mahfouz Antonella Ragnini-Wilson Rossella Venditti Maria Antonietta De Matteis Cathal Wilson

Trs20p is a subunit of the evolutionarily conserved TRAPP (TRAnsport Protein Particle) complex that mediates various aspects of membrane trafficking. Three TRAPP complexes have been identified in yeast with roles in ER-to-Golgi trafficking, post-Golgi and endosomal-to-Golgi transport and in autophagy. The role of Trs20p, which is essential for viability and a component of all three complexes, a...

Journal: :The EMBO journal 2000
J Barrowman M Sacher S Ferro-Novick

Bet3p, a component of a large novel complex called TRAPP, acts upstream of endoplasmic reticulum (ER)-Golgi SNAREs. Unlike the SNAREs, which reside on multiple compartments, Bet3p is localized exclusively to Golgi membranes. While other proteins recycle from the Golgi to the ER, Bet3p and other TRAPP subunits remain associated with this membrane under conditions that block anterograde traffic. ...

2012
Min Zong Ayano Satoh Mei Kuen Yu Ka Yu Siu Wing Yan Ng Hsiao Chang Chan Julian A. Tanner Sidney Yu

BACKGROUND The transport of endoplasmic reticulum (ER)-derived COPII vesicles toward the ER-Golgi intermediate compartment (ERGIC) requires cytoplasmic dynein and is dependent on microtubules. p150(Glued), a subunit of dynactin, has been implicated in the transport of COPII vesicles via its interaction with COPII coat components Sec23 and Sec24. However, whether and how COPII vesicle tether, TR...

2011
Brennon D. Thomas Barry E. Mullins Gilbert L. Peterson Robert F. Mills

Billions of packets traverse computer networks every day. Often, these packets have legitimate destinations such as buying a book at amazon.com or streaming a video. Unfortunately, malicious and suspicious network traffic continues to plague the Internet. One example is abusing the Domain Name System (DNS) protocol to exfiltrate sensitive data, establish backdoor tunnels, or control botnets. To...

Journal: :EMBO reports 2005
Daniel Kümmel Jürgen J Müller Yvette Roske Rolf Misselwitz Konrad Büssow Udo Heinemann

The TRAPP (transport protein particle) complexes are tethering complexes that have an important role at the different steps of vesicle transport. Recently, the crystal structures of the TRAPP subunits SEDL and BET3 have been determined, and we present here the 1.7 Angstroms crystal structure of human TPC6, a third TRAPP subunit. The protein adopts an alpha/beta-plait topology and forms a dimer....

2000
Christopher Olston Jennifer Widom

Strict consistency of replicated data is infeasible or not required by many distributed applications, so current systems often permit stale replication, in which cached copies of data values are allowed to become out of date. Queries over cached data return an answer quickly, but the stale answer may be unboundedly imprecise. Alternatively, queries over remote master data return a precise answe...

2011
Brennon Thomas Barry E. Mullins Gilbert L. Peterson Robert F. Mills

Billions of legitimate packets traverse computer networks every day. Unfortunately, malicious traffic also traverses these same networks. An example is traffic that abuses the Domain Name System (DNS) protocol to exfiltrate sensitive data, establish backdoor tunnels or control botnets. This paper describes the TRAPP-2 system, an extended version of the Tracking and Analysis for Peer-to-Peer (TR...

2015
Miroslav P. Milev Michael Sacher

Intracellular vesicle transport is a mechanism required for the proper targeting and secretion of proteins and lipids. The process comprises sorting, budding, movement, tethering and fusion of the vesicle with the target membrane resulting in delivery of its contents [1]. Transport protein particle (TRAPP) has been demonstrated to contribute to endoplasmic reticulum (ER)-to–Golgi, intra-Golgi a...

Journal: :Cell 2006
Yeon-Gil Kim Stefan Raunser Christine Munger John Wagner Young-Lan Song Miroslaw Cygler Thomas Walz Byung-Ha Oh Michael Sacher

Transport protein particle (TRAPP) I is a multisubunit vesicle tethering factor composed of seven subunits involved in ER-to-Golgi trafficking. The functional mechanism of the complex and how the subunits interact to form a functional unit are unknown. Here, we have used a multidisciplinary approach that includes X-ray crystallography, electron microscopy, biochemistry, and yeast genetics to el...

Journal: :Journal of cell science 2005
Eva Loh Frank Peter V Nathan Subramaniam Wanjin Hong

The TRAPP complex identified in yeast regulates vesicular transport in the early secretory pathway. Although some components of the TRAPP complex are structurally conserved in mammalian cells, the function of the mammalian components has not been examined. We describe our biochemical and functional analysis of mammalian Bet3, the most conserved component of the TRAPP complex. Bet3 mRNA is ubiqu...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید