scholarly journals Independent membrane protein clustering

2007 ◽  
Vol 178 (7) ◽  
pp. 1096-1096
Author(s):  
Nicole LeBrasseur
Keyword(s):  
Membrane Protein ◽  
Protein Clustering ◽  
Membrane Protein Clustering

scholarly journals Stability Analysis of a Bulk–Surface Reaction Model for Membrane Protein Clustering

2020 ◽  
Vol 82 (2) ◽  
Author(s):  
Lucas M. Stolerman ◽  
Michael Getz ◽  
Stefan G. Llewellyn Smith ◽  
Michael Holst ◽  
Padmini Rangamani
Keyword(s):  
Stability Analysis ◽  
Membrane Protein ◽  
Surface Reaction ◽  
Reaction Model ◽  
Protein Clustering ◽  
Bulk Surface ◽  
Membrane Protein Clustering ◽  
Surface Reaction Model

scholarly journals Lipid Composition Modulates Membrane Protein Clustering

2016 ◽  
Vol 110 (3) ◽  
pp. 81a
Author(s):  
Anna L. Duncan ◽  
Heidi Koldsø ◽  
Tyler Reddy ◽  
Jean Helie ◽  
Mark S.P. Sansom
Keyword(s):  
Membrane Protein ◽  
Lipid Composition ◽  
Protein Clustering ◽  
Membrane Protein Clustering

scholarly journals The packing density of a supramolecular membrane protein cluster is controlled by cytoplasmic interactions

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Elisa Merklinger ◽  
Jan-Gero Schloetel ◽  
Pascal Weber ◽  
Helena Batoulis ◽  
Sarah Holz ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Membrane Protein ◽  
Protein Interactions ◽  
Cluster Size ◽  
Protein Domain ◽  
Self Organization ◽  
Cytoplasmic Protein ◽  
Transmembrane Segment ◽  
Protein Clustering ◽  
Membrane Protein Clustering

Molecule clustering is an important mechanism underlying cellular self-organization. In the cell membrane, a variety of fundamentally different mechanisms drive membrane protein clustering into nanometre-sized assemblies. To date, it is unknown whether this clustering process can be dissected into steps differentially regulated by independent mechanisms. Using clustered syntaxin molecules as an example, we study the influence of a cytoplasmic protein domain on the clustering behaviour. Analysing protein mobility, cluster size and accessibility to myc-epitopes we show that forces acting on the transmembrane segment produce loose clusters, while cytoplasmic protein interactions mediate a tightly packed state. We conclude that the data identify a hierarchy in membrane protein clustering likely being a paradigm for many cellular self-organization processes.

scholarly journals Mathematical Simulation of Membrane Protein Clustering for Efficient Signal Transduction

2012 ◽  
Vol 40 (11) ◽  
pp. 2307-2318 ◽  
Author(s):  
Krishnan Radhakrishnan ◽  
Ádám Halász ◽  
Meghan M. McCabe ◽  
Jeremy S. Edwards ◽  
Bridget S. Wilson
Keyword(s):  
Signal Transduction ◽  
Membrane Protein ◽  
Mathematical Simulation ◽  
Protein Clustering ◽  
Membrane Protein Clustering

Modulated red blood cell survival by membrane protein clustering

1995 ◽  
Vol 144 (1) ◽  
pp. 53-59 ◽  
Author(s):  
Laura Chiarantini ◽  
Luigia Rossi ◽  
Alessandra Fraternale ◽  
Mauro Magnani
Keyword(s):  
Membrane Protein ◽  
Blood Cell ◽  
Cell Survival ◽  
Red Blood Cell ◽  
Protein Clustering ◽  
Membrane Protein Clustering

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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