Identification of a Targeting Factor for Posttranslational Membrane Protein Insertion into the ER
434
TL;DR: A cytosolic TMD recognition complex (TRC) that targets TA proteins for insertion into the ER membrane, and an ATPase-deficient mutant of TRC40/Asna-1 dominantly inhibited TA protein insertion selectively without influencing other translocation pathways.
read more
About: This article is published in Cell. The article was published on 23 Mar 2007. and is currently open access. The article focuses on the topics: Membrane protein & Integral membrane protein.
read more
Chat with Paper
AI Agents for this Paper
Find similar papers on Google Scholar, PubMed and Arxiv
Write a critical review of this paper
Analyze citations of this paper to find unaddressed research gaps
Citations
Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway
TL;DR: The key players that mediate secretory protein biogenesis and trafficking are discussed, highlighting recent advances that have deepened the understanding of the complexity of this conserved and essential process.
323
Hsp90: Structure and Function.
TL;DR: The focus of this review is the structural and mechanistic studies which have been performed in order to understand how this important chaperone acts on a wide variety of different proteins (its client proteins) and cellular processes.
322
The ER membrane protein complex is a transmembrane domain insertase
TL;DR: It is found that known membrane insertion pathways fail to effectively engage tail-anchored membrane proteins with moderately hydrophobic transmembrane domains, and these proteins are instead shielded in the cytosol by calmodulin.
284
Breaking BAG: The Co-Chaperone BAG3 in Health and Disease.
TL;DR: The discovery of its role in selective autophagy and the description of B AG3-mediated selective macroautophagy as an adaptive mechanism to maintain cellular homeostasis, under stress as well as during aging, make BAG3 a highly interesting target for future pharmacological interventions.
244
A nuclear-envelope bridge positions nuclei and moves chromosomes
TL;DR: The bridge of SUN and KASH across the nuclear envelope functions to transfer forces that are generated in the cytoplasm into the nucleoplasm during nuclear migration, nuclear anchorage, centrosome attachment, intermediate-filament association and telomere clustering.
217
References
Hsp70 chaperones: cellular functions and molecular mechanism.
Matthias P. Mayer,Bernd Bukau +1 more
TL;DR: This work has shown that for specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100, and this ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target H Sp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the HSp70-substrate complex.
X-ray structure of a protein-conducting channel
Bert van den Berg,William M. Clemons,Ian Collinson,Yorgo Modis,Enno Hartmann,Stephen C. Harrison,Tom A. Rapoport +6 more
TL;DR: 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.
1.3K
Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
Dirk Görlich,Tom A. Rapoport +1 more
TL;DR: It is suggested that the Sec61p complex binds the ribosome during translocation and forms the postulated protein-conducting channel, indicating a surprising simplicity of the basic translocation machinery.
694
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
TL;DR: The folding of polypeptides emerging from ribosomes was analysed in a mammalian translation system using firefly luciferase as a model protein and found that the ordered assembly of these components on the nascent chain forms a high molecular mass complex.
684
Preparation of microsomal membranes for cotranslational protein translocation
Peter Walter,Günter Blobel +1 more
TL;DR: This chapter describes a rapid isolation procedure that reproducibly yields highly active microsomal membranes, and presents method for refining the crude rough microsomes (RM) fraction by column washing, EDTA stripping, or nuclease treatment.
651
Related Papers (5)
[...]