A potential molecular switch in an α-helical coiled coil

2007 ◽  
Vol 70 (1) ◽  
pp. 25-30 ◽  
Author(s):  
Charles A. Laughton ◽  
Ben F. Luisi ◽  
J. Venkatesh Pratap ◽  
Chris R. Calladine
Keyword(s):  
Coiled Coil ◽  
Molecular Switch

Polymer Coiled-Coil Conjugates: Potential for Development as a New Class of Therapeutic “Molecular Switch”

2011 ◽  
Vol 12 (1) ◽  
pp. 19-27 ◽  
Author(s):  
Samuel P. E. Deacon ◽  
Bojana Apostolovic ◽  
Rodrigo J. Carbajo ◽  
Anne-Kathrin Schott ◽  
Konrad Beck ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Molecular Switch ◽  
New Class

scholarly journals A potential molecular switch in an α-helical coiled coil

2008 ◽  
Vol 75 (1) ◽  
pp. 272-272
Author(s):  
Charles A. Laughton ◽  
Ben F. Luisi ◽  
J. Venkatesh Pratap ◽  
Chris R. Calladine
Keyword(s):  
Coiled Coil ◽  
Molecular Switch

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.

ALMS1 acts as a critical molecular switch that controls Insulin-stimulated glucose transport in adipocytes

2016 ◽  
Author(s):  
Cynthia Licona ◽  
Cathy Obringer ◽  
Harinda Rajapaksha ◽  
Helene Dollfus ◽  
Nikolai Petrovsky ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Molecular Switch
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