scholarly journals Varying label density allows artifact-free analysis of membrane-protein nanoclusters

2016 ◽  
Vol 13 (8) ◽  
pp. 661-664 ◽  
Author(s):  
Florian Baumgart ◽  
Andreas M Arnold ◽  
Konrad Leskovar ◽  
Kaj Staszek ◽  
Martin Fölser ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Label Density

scholarly journals Varying Label Density to Probe Membrane Protein Nanoclusters in STORM/PALM

2017 ◽  
Vol 112 (3) ◽  
pp. 20a
Author(s):  
Florian Baumgart ◽  
Andreas Arnold ◽  
Konrad Leskovar ◽  
Kaj Staszek ◽  
Martin Foelser ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Label Density

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.

Identification of Epithelial Membrane Protein 2 (EMP2) as a Molecular Marker and Correlate for Angiogenesis in Meningioma

2020 ◽  
Author(s):  
Kunal S. Patel ◽  
Sameer Kejirwal ◽  
Samasuk Thammachantha ◽  
Courtney Duong ◽  
Ann Chan ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Molecular Marker ◽  
Epithelial Membrane Protein 2
Sign in / Sign up

Export Citation Format

Share Document