Transient Transfection and Expression of Eukaryotic Membrane Proteins in Expi293F Cells and Their Screening on a Small Scale: Application for Structural Studies

Author(s):  
Ganna O. Krasnoselska ◽  
Maud Dumoux ◽  
Nadisha Gamage ◽  
Harish Cheruvara ◽  
James Birch ◽  
...  
2016 ◽  
Vol 38 ◽  
pp. 137-144 ◽  
Author(s):  
Joseph A Lyons ◽  
Azadeh Shahsavar ◽  
Peter Aasted Paulsen ◽  
Bjørn Panyella Pedersen ◽  
Poul Nissen

2000 ◽  
Vol 56 (s1) ◽  
pp. s83-s83
Author(s):  
P. Nollert ◽  
M. L. Chiu ◽  
M. C. Loewen ◽  
A. Royant ◽  
H. Behrhali ◽  
...  

2020 ◽  
Vol 56 (48) ◽  
pp. 6511-6514 ◽  
Author(s):  
Bankala Krishnarjuna ◽  
Thirupathi Ravula ◽  
Ayyalusamy Ramamoorthy

Directly extracted membrane proteins are stable and suitable for functional and high-resolution structural studies; however, the efficacy is modulated by the net charge of the target protein and the polymer used at a given pH.


2019 ◽  
Vol 116 (3) ◽  
pp. 56a
Author(s):  
Gary A. Lorigan ◽  
Indra D. Sahu ◽  
Daniel L. Drew ◽  
Gunjan Dixit ◽  
Tanbir Ahammad

2014 ◽  
Vol 106 (2) ◽  
pp. 192a-193a ◽  
Author(s):  
Yongae Kim ◽  
Ji-Ho Jeong ◽  
Ji-Sun Kim

2011 ◽  
Vol 300 (5) ◽  
pp. F1062-F1073 ◽  
Author(s):  
Hanne B. Moeller ◽  
Emma T. B. Olesen ◽  
Robert A. Fenton

The cellular functions of many eukaryotic membrane proteins, including the vasopressin-regulated water channel aquaporin-2 (AQP2), are regulated by posttranslational modifications. In this article, we discuss the experimental discoveries that have advanced our understanding of how posttranslational modifications affect AQP2 function, especially as they relate to the role of AQP2 in the kidney. We review the most recent data demonstrating that glycosylation and, in particular, phosphorylation and ubiquitination are mechanisms that regulate AQP2 activity, subcellular sorting and distribution, degradation, and protein interactions. From a clinical perspective, posttranslational modification resulting in protein misrouting or degradation may explain certain forms of nephrogenic diabetes insipidus. In addition to providing major insight into the function and dynamics of renal AQP2 regulation, the analysis of AQP2 posttranslational modification may provide general clues as to the role of posttranslational modification for regulation of other membrane proteins.


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