Membrane Protein Solubilization and Quality Control: An Example of a Primary Active Transporter

2020 ◽  
pp. 93-103
Author(s):  
Charlott Stock ◽  
Inga Hänelt
Keyword(s):  
Quality Control ◽  
Membrane Protein ◽  
Protein Solubilization ◽  
Primary Active Transporter

The lysosomal membrane protein Sidt2 is a vital regulator of mitochondrial quality control in skeletal muscle

2021 ◽  
Vol 35 (4) ◽  
Author(s):  
Lizhuo Wang ◽  
Cui Yu ◽  
Wenjun Pei ◽  
Mengya Geng ◽  
Yao Zhang ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Quality Control ◽  
Membrane Protein ◽  
Lysosomal Membrane ◽  
Mitochondrial Quality Control ◽  
Lysosomal Membrane Protein

scholarly journals Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease

2020 ◽  
Vol 39 (10) ◽  
Author(s):  
Jakub Began ◽  
Baptiste Cordier ◽  
Jana Březinová ◽  
Jordan Delisle ◽  
Rozálie Hexnerová ◽  
...  
Keyword(s):  
Quality Control ◽  
Membrane Protein ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Bacterial Membrane

scholarly journals Proteasome-dependent protein quality control of the peroxisomal membrane protein Pxa1p

2020 ◽  
Vol 1862 (9) ◽  
pp. 183342
Author(s):  
S. Devarajan ◽  
M. Meurer ◽  
C.W.T. van Roermund ◽  
X. Chen ◽  
E.H. Hettema ◽  
...  
Keyword(s):  
Quality Control ◽  
Membrane Protein ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Peroxisomal Membrane ◽  
Peroxisomal Membrane Protein ◽  
Dependent Protein

scholarly journals Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase

2012 ◽  
Vol 197 (6) ◽  
pp. 761-773 ◽  
Author(s):  
Eric M. Rubenstein ◽  
Stefan G. Kreft ◽  
Wesley Greenblatt ◽  
Robert Swanson ◽  
Mark Hochstrasser
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Membrane Protein ◽  
Ubiquitin Ligase ◽  
Apolipoprotein B ◽  
Secretory Pathway ◽  
Protein A ◽  
Proteasomal Degradation ◽  
Membrane Localization ◽  
General Role

Little is known about quality control of proteins that aberrantly or persistently engage the endoplasmic reticulum (ER)-localized translocon en route to membrane localization or the secretory pathway. Hrd1 and Doa10, the primary ubiquitin ligases that function in ER-associated degradation (ERAD) in yeast, target distinct subsets of misfolded or otherwise abnormal proteins based primarily on degradation signal (degron) location. We report the surprising observation that fusing Deg1, a cytoplasmic degron normally recognized by Doa10, to the Sec62 membrane protein rendered the protein a Hrd1 substrate. Hrd1-dependent degradation occurred when Deg1-Sec62 aberrantly engaged the Sec61 translocon channel and underwent topological rearrangement. Mutations that prevent translocon engagement caused a reversion to Doa10-dependent degradation. Similarly, a variant of apolipoprotein B, a protein known to be cotranslocationally targeted for proteasomal degradation, was also a Hrd1 substrate. Hrd1 therefore likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the translocon.

New ganglio-tripod amphiphiles (TPAs) for membrane protein solubilization and stabilization: implications for detergent structure–property relationships

2014 ◽  
Vol 12 (42) ◽  
pp. 8480-8487 ◽  
Author(s):  
Pil Seok Chae ◽  
Hyoung Eun Bae ◽  
Muhammad Ehsan ◽  
Hazrat Hussain ◽  
Jin Woong Kim
Keyword(s):  
Membrane Protein ◽  
Structure Property ◽  
Protein Solubilization ◽  
Structure Property Relationships

This study introduces new ganglio-TPAs with enhanced efficacy for membrane protein solubilization and stabilization compared to conventional detergents.

scholarly journals Membrane protein folding and quality control

2021 ◽  
Vol 69 ◽  
pp. 50-54
Author(s):  
Ben P. Phillips ◽  
Elizabeth A. Miller
Keyword(s):  
Quality Control ◽  
Protein Folding ◽  
Membrane Protein ◽  
Membrane Protein Folding
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