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Protein quality control at the plasma membrane

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TLDR
Accumulating evidences indicate that membrane proteins exported from the endoplasmic reticulum are subjected to peripheral quality control (QC) along the late secretory and endocytic pathways, as well as at the plasma membrane (PM).
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This article is published in Current Opinion in Cell Biology.The article was published on 2011-08-01 and is currently open access. It has received 70 citations till now. The article focuses on the topics: Proteostasis & Peripheral membrane protein.

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Citations
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Targeting the Intracellular Environment in Cystic Fibrosis: Restoring Autophagy as a Novel Strategy to Circumvent the CFTR Defect.

TL;DR: Recent pre-clinical evidence indicating that targeting the intracellular environment surrounding the misfolded mutant CFTR instead of protein itself could constitute an attractive therapeutic option to sensitize patients carrying the F508del-CFTR mutation to the beneficial action of CFTR potentiators on lung inflammation is reviewed.
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CFTR: folding, misfolding and correcting the ΔF508 conformational defect

TL;DR: Recent basic research aimed at elucidating the structural and trafficking defects of ΔF508 CFTR, a prerequisite for the rational design of CF therapy to correct the loss-of-function phenotype are discussed.
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Protein quality control in the secretory pathway

TL;DR: The machinery that maintains protein fidelity and how its actions are coordinated is described in the secretory pathway of eukaryotic proteomes.
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Identification of Downstream Components of Ubiquitin-Conjugating Enzyme PHOSPHATE2 by Quantitative Membrane Proteomics in Arabidopsis Roots

TL;DR: A mechanism by which PHO2 modulates Pi acquisition by regulating the abundance of PHT1s in the secretory pathway destined for plasma membranes is uncovers and a database of the membrane proteome is provided that will be widely applicable in root biology research.
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Ubiquitin-Dependent Sorting in Endocytosis

TL;DR: An overview of how membrane proteins are selected for ubiquitination and deubiquitination within the endocytic pathway and how that ubiquitin signal is interpreted byendocytic sorting machineries is provided.
References
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Journal ArticleDOI

Quality control in the endoplasmic reticulum

TL;DR: Recent progress is discussed in understanding the conformation-specific sorting of proteins at the level of ER retention and export, which is important for the fidelity of cellular functions.
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HSP90 at the hub of protein homeostasis: emerging mechanistic insights

TL;DR: Comprehensive understanding of how HSP90 functions promises not only to provide new avenues for therapeutic intervention, but to shed light on fundamental biological questions.
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Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome

TL;DR: The proteasome contains deubiquitinating enzymes (DUBs) that can remove ubiquitin before substrate degradation initiates, thus allowing some substrates to dissociate from the proteasomes and escape degradation.
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Targeting the dynamic HSP90 complex in cancer

TL;DR: The molecular chaperone heat shock protein 90 (HSP90) has been used by cancer cells to facilitate the function of numerous oncoproteins, and it can be argued that cancer cells are 'addicted' to HSP90.
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The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins

TL;DR: The endosomal sorting complex required for transport (ESCRT) machinery sorts cargo labelled with ubiquitin into invaginations of endosome membranes and mediates the breaking off of the cargo-containing intraluminal vesicles from the perimeter membrane.
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