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Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER Proteins
Three distinct ubiquitin-ligase complexes that define different ERAD pathways are identified in S. cerevisiae, leading to a unifying concept for ERAD that may also apply to mammalian cells. Expand
The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
This work proposes that the Cdc48/p97–Ufd1–Npl4 complex extracts proteins from the ER membrane for cytosolic degradation, and demonstrates that it requires the interacting partners Ufd1 and Npl4. Expand
A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
A p97-interacting membrane protein complex in the mammalian ER that links elimination of misfolded proteins from the endoplasmic reticulum by retro-translocation and its subsequent movement through the membrane by the cytosolic p97 ATPase is identified. Expand
A Class of Membrane Proteins Shaping the Tubular Endoplasmic Reticulum
How is the characteristic shape of a membrane bound organelle achieved? We have used an in vitro system to address the mechanism by which the tubular network of the endoplasmic reticulum (ER) isExpand
Cargo of Kinesin Identified as Jip Scaffolding Proteins and Associated Signaling Molecules
Results demonstrate a direct interaction between conventional kinesin and a cargo, indicate that motor proteins are linked to their membranous cargo via scaffolding proteins, and support a role for motor proteins in spatial regulation of signal transduction pathways. Expand
Structure of a complex of the ATPase SecA and the protein-translocation channel
The crystal structure of SecA bound to the SecY complex, with a maximum resolution of 4.5 ångström (Å), obtained for components from Thermotoga maritima, shows that one copy ofSecA in an intermediate state of ATP hydrolysis is bound to one molecule of theSecY complex. Expand
Sec6l-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
The human cytomegalovirus genome encodes proteins that trigger destruction of newly synthesized major histocompatibility complex (MHC) class I molecules, which involves the Sec6l complex, in what appears to be a reversal of the reaction by which it translocates nascent chains into the endoplasmic reticulum. Expand
X-ray structure of a protein-conducting channel
The crystal structure of the Sec61 or SecY complex from Methanococcus jannaschii suggests mechanisms for signal-sequence recognition and for the lateral exit of transmembrane segments of nascent membrane proteins into lipid, and indicates binding sites for partners that provide the driving force for translocation. Expand
A Class of Dynamin-like GTPases Involved in the Generation of the Tubular ER Network
It is shown that mammalian atlastins, which are dynamin-like, integral membrane GTPases, interact with the tubule-shaping proteins and form an interconnected network in the endoplasmic reticulum. Expand
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
Structural, genetic and biochemical data show how the channel opens across the membrane, releases hydrophobic segments of membrane proteins laterally into lipid, and maintains the membrane barrier for small molecules. Expand