Alternative Membrane Protein Conformations in Alcohols†

Biochemistry ◽  
2007 ◽  
Vol 46 (14) ◽  
pp. 4348-4359 ◽  
Author(s):  
D. E. Otzen ◽  
P. Sehgal ◽  
L. W. Nesgaard
Keyword(s):  
Membrane Protein ◽  
Protein Conformations

Detergent Release Prolongs the Lifetime of Native-like Membrane Protein Conformations in the Gas-Phase

2013 ◽  
Vol 135 (16) ◽  
pp. 6078-6083 ◽  
Author(s):  
Antoni J. Borysik ◽  
Dominic J. Hewitt ◽  
Carol V. Robinson
Keyword(s):  
Membrane Protein ◽  
Gas Phase ◽  
Protein Conformations

Probing Membrane Protein Conformations with an Extrinsic Fluorophore

1995 ◽  
pp. 409-410
Author(s):  
E. Lewitzki ◽  
E. Schick ◽  
K. Brand ◽  
R. Hutterer ◽  
F. W. Schneider ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Conformations

scholarly journals Helical membrane protein conformations and their environment

2013 ◽  
Vol 42 (10) ◽  
pp. 731-755 ◽  
Author(s):  
Timothy A. Cross ◽  
Dylan T. Murray ◽  
Anthony Watts
Keyword(s):  
Membrane Protein ◽  
Protein Conformations

Membrane Protein Clusters at Nanoscale Resolution: More Than Pretty Pictures

Physiology ◽  
2010 ◽  
Vol 25 (2) ◽  
pp. 116-124 ◽  
Author(s):  
Thorsten Lang ◽  
Silvio O. Rizzoli
Keyword(s):  
Membrane Protein ◽  
Fluorescence Microscopy ◽  
Molecular Machines ◽  
Protein Conformations ◽  
Superresolution Microscopy ◽  
Protein Clusters ◽  
Microscopy Techniques

Fluorescence microscopy is powerful for analyzing the composition and dynamics of cellular elements, but studying precise molecule patterns is precluded due to diffraction limited resolution. This barrier has been lifted now through several superresolution microscopy techniques. They revealed that proteins assemble in defined groups (clusters). A new challenge thus appears for the biologist: to find out whether clusters are molecular machines, stabilizers of defined protein conformations, or simply protein reservoirs.

TMCC3 localizes at the three-way junctions for the proper tubular network of the endoplasmic reticulum

2019 ◽  
Vol 476 (21) ◽  
pp. 3241-3260
Author(s):  
Sindhu Wisesa ◽  
Yasunori Yamamoto ◽  
Toshiaki Sakisaka
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Mammalian Cells ◽  
Coiled Coil ◽  
Transmembrane Domains ◽  
Domain Family ◽  
Coiled Coil Domain ◽  
U2os Cells ◽  
Er Membrane

The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.

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