Elucidating Structural Dynamics of Integral Membrane Proteins on Native Cell Surface by Hydroxyl Radical Footprinting and Nano LC-MS/MS

2011 ◽  
pp. 287-303 ◽  
Author(s):  
Yi Zhu ◽  
Tiannan Guo ◽  
Siu Kwan Sze
Keyword(s):  
Membrane Proteins ◽  
Cell Surface ◽  
Hydroxyl Radical ◽  
Structural Dynamics ◽  
Integral Membrane Proteins ◽  
Native Cell ◽  
Hydroxyl Radical Footprinting

scholarly journals The ART-Rsp5 ubiquitin ligase network comprises a plasma membrane quality control system that protects yeast cells from proteotoxic stress

eLife ◽  
2013 ◽  
Vol 2 ◽  
Author(s):  
Yingying Zhao ◽  
Jason A MacGurn ◽  
Max Liu ◽  
Scott Emr
Keyword(s):  
Quality Control ◽  
Plasma Membrane ◽  
Control System ◽  
Membrane Proteins ◽  
Cell Surface ◽  
Ubiquitin Ligase ◽  
Integral Membrane Proteins ◽  
Quality Control System ◽  
Er Quality Control ◽  
Proteotoxic Stress

Secretory cargo that cannot fold properly in the ER are selectively targeted for removal by a well-studied ER-associated degradation pathway, or ERAD. In contrast, very little is known about post-ER quality control mechanisms for damaged or misfolded integral membrane proteins. Here we describe a quality control function of the Rsp5-ART ubiquitin ligase adaptor network that functions to protect plasma membrane (PM) integrity. Failure to mediate this protective response during heat stress leads to toxic accumulation of misfolded integral membrane proteins at the cell surface, which causes loss of PM integrity and cell death. Thus, the Rsp5-ART network comprises a PM quality control system that works together with sequential quality control pathways in the ER and Golgi to (i) target the degradation of proteins that have exceeded their functional lifetime due to damage and/or misfolding and (ii) limit the toxic accumulation of specific proteins at the cell surface during proteotoxic stress.

Image Analysis of Intramembrane Particles in Freeze-Fractured Biomembranes Using Computer Simulation Techniques

1975 ◽  
Vol 33 ◽  
pp. 214-215
Author(s):  
D.J. Benefiel ◽  
R.S. Weinstein
Keyword(s):  
Membrane Proteins ◽  
Freeze Fracture ◽  
Integral Membrane Proteins ◽  
Systematic Evaluation ◽  
Intramembrane Particles ◽  
Modeling Methods ◽  
Simulation Techniques ◽  
Freeze Fracture Electron Microscopy ◽  
Fracture Electron ◽  
Computer Simulation Techniques

Intramembrane particles (IMP or MAP) are components of most biomembranes. They are visualized by freeze-fracture electron microscopy, and they probably represent replicas of integral membrane proteins. The presence of MAP in biomembranes has been extensively investigated but their detailed ultrastructure has been largely ignored. In this study, we have attempted to lay groundwork for a systematic evaluation of MAP ultrastructure. Using mathematical modeling methods, we have simulated the electron optical appearances of idealized globular proteins as they might be expected to appear in replicas under defined conditions. By comparing these images with the apearances of MAPs in replicas, we have attempted to evaluate dimensional and shape distortions that may be introduced by the freeze-fracture technique and further to deduce the actual shapes of integral membrane proteins from their freezefracture images.

How Do Lipids Affect the Structure and Function of Integral Membrane Proteins

2012 ◽  
Vol 28 (11) ◽  
pp. 866
Author(s):  
Jie HENG ◽  
Yan WU ◽  
Xianping WANG ◽  
Kai ZHANG
Keyword(s):  
Membrane Proteins ◽  
Structure And Function ◽  
Integral Membrane Proteins ◽  
And Function

3D Crystallization and Structural Studies of Integral Membrane Proteins in Lipidic Cubic phases

2000 ◽  
Vol 56 (s1) ◽  
pp. s83-s83
Author(s):  
P. Nollert ◽  
M. L. Chiu ◽  
M. C. Loewen ◽  
A. Royant ◽  
H. Behrhali ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Integral Membrane Proteins ◽  
Structural Studies ◽  
Cubic Phases
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