Polytopic proteins: preventing aggregation in the membrane.

J Michael Lord; Stephen High

doi:10.1016/j.cub.2005.02.043

Home/Archive/PubMed

PubMed · 15753028

Polytopic proteins: preventing aggregation in the membrane.

J Michael Lord·Stephen High

View original source ↗Export metadata ↓

Abstract

It has been proposed that the aggregation of nascent transmembrane segments of polytopic proteins is prevented by chaperones present in the endoplasmic reticulum membrane; now the first experimental support for this proposal has been reported.

Explore related subjects

Carrier Proteins Endoplasmic Reticulum Membrane Proteins Models, Biological Molecular Chaperones Protein Folding Protein Structure, Tertiary SEC Translocation Channels Journal Article Review

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

J Michael Lord, Stephen High. 2005-03-08. Polytopic proteins: preventing aggregation in the membrane.. https://doi.org/10.1016/j.cub.2005.02.043

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Electrochemical screening of recombinant protein solubility in Escherichia coli using scanning electrochemical microscopy (SECM).

A microbial array chip with collagen gel spots entrapping living Escherichia coli (E. coli) DH5alpha was applied for the screening of recombinant protein solubilities. The alpha-fragment of beta-galactosidase (betaGal) was fused to the target protein, namely, maltose-binding protein (MBP), to monitor the solubility of MBP. Scanning electrochemical microscopy (SECM) was used to detect the release of p-aminophenol from E. coli cells catalyzed by intracellular betaGal. Comparison of the SECM-based method with the Western blotting-based method indicated that the current response obtained using SECM increased with an increase in the betaGal activity and therefore, with the soluble fraction of MBP in the host cells.

Carrier Proteins↗

PubMed2007

AMG 531 for chronic ITP.

Explore the source record for details and available documents.

Carrier Proteins↗

PubMed2007

Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity.

Although cullin-1 neddylation is crucial for the activation of SCF ubiquitin E3 ligases, the underlying mechanisms for NEDD8-mediated activation of SCF remain unclear. Here we demonstrate by NMR and mutational studies that NEDD8 binds the ubiquitin E2 (UBC4), but not NEDD8 E2 (UBC12). Our data imply that NEDD8 forms an active platform on the SCF complex for selective recruitment of ubiquitin-charged E2s in collaboration with RBX1, and thereby upregulates the E3 activity.

Carrier Proteins↗