Stoichiometric Analysis of Oligomerization of Membrane Proteins on Living Cells Using Coiled-Coil Labeling and Spectral Imaging

2013 ◽  
Vol 85 (6) ◽  
pp. 3454-3461 ◽  
Author(s):  
Kenichi Kawano ◽  
Yoshiaki Yano ◽  
Kaoru Omae ◽  
Sayaka Matsuzaki ◽  
Katsumi Matsuzaki
Keyword(s):  
Membrane Proteins ◽  
Coiled Coil ◽  
Spectral Imaging ◽  
Living Cells ◽  
Stoichiometric Analysis

scholarly journals A Visualization Tool for Oligomerization and Internalization of Membrane Proteins in Living Cells: Coiled-Coil Labeling Method

2014 ◽  
Vol 134 (4) ◽  
pp. 501-506 ◽  
Author(s):  
Yoshiaki Yano ◽  
Kenichi Kawano ◽  
Kaoru Omae ◽  
Yuki Takeda ◽  
Sayaka Matsuzaki ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Coiled Coil ◽  
Living Cells ◽  
Visualization Tool ◽  
Labeling Method

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.

scholarly journals Divisome under Construction: Distinct Domains of the Small Membrane Protein FtsB Are Necessary for Interaction with Multiple Cell Division Proteins

2009 ◽  
Vol 191 (8) ◽  
pp. 2815-2825 ◽  
Author(s):  
Mark D. Gonzalez ◽  
Jon Beckwith
Keyword(s):  
Cell Division ◽  
Membrane Proteins ◽  
Protein Interactions ◽  
Cell Envelope ◽  
Coiled Coil ◽  
Main Function ◽  
Protein Protein Interactions ◽  
Molecular Scaffold ◽  
C Terminus ◽  
Under Construction

ABSTRACT Cell division in bacteria requires the coordinated action of a set of proteins, the divisome, for proper constriction of the cell envelope. Multiple protein-protein interactions are required for assembly of a stable divisome. Within the Escherichia coli divisome is a conserved subcomplex of inner membrane proteins, the FtsB/FtsL/FtsQ complex, which is necessary for linking the upstream division proteins, which are predominantly cytoplasmic, with the downstream division proteins, which are predominantly periplasmic. FtsB and FtsL are small bitopic membrane proteins with predicted coiled-coil motifs, which themselves form a stable subcomplex that can recruit downstream division proteins independently of FtsQ; however, the details of how FtsB and FtsL interact together and with other proteins remain to be characterized. Despite the small size of FtsB, we identified separate interaction domains of FtsB that are required for interaction with FtsL and FtsQ. The N-terminal half of FtsB is necessary for interaction with FtsL and sufficient, when in complex with FtsL, for recruitment of downstream division proteins, while a portion of the FtsB C terminus is necessary for interaction with FtsQ. These properties of FtsB support the proposal that its main function is as part of a molecular scaffold to allow for proper formation of the divisome.

scholarly journals Trapped in Cristae: Localization and Tracking of Mitochondrial Membrane-Proteins in Living Cells

2011 ◽  
Vol 100 (3) ◽  
pp. 226a
Author(s):  
Karin B. Busch ◽  
Verena Wilkens ◽  
Timo Appelhans ◽  
Christian Richter ◽  
Wladislaw Kohl ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Mitochondrial Membrane ◽  
Living Cells ◽  
Localization And Tracking

Stoichiometric analysis of oligomeric states of three class-A GPCRs, chemokine-CXCR4, dopamine-D2, and prostaglandin-EP1 receptors, on living cells

2017 ◽  
Vol 23 (7-8) ◽  
pp. 650-658 ◽  
Author(s):  
Kenichi Kawano ◽  
Tetsuya Yagi ◽  
Nozomu Fukada ◽  
Yoshiaki Yano ◽  
Katsumi Matsuzaki
Keyword(s):  
Living Cells ◽  
Stoichiometric Analysis ◽  
Class A ◽  
Dopamine D2

scholarly journals A Tissue-Like Printed Material

Science ◽  
2013 ◽  
Vol 340 (6128) ◽  
pp. 48-52 ◽  
Author(s):  
Gabriel Villar ◽  
Alexander D. Graham ◽  
Hagan Bayley
Keyword(s):  
Tissue Engineering ◽  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Collective Behavior ◽  
Three Dimensional ◽  
Living Cells ◽  
Emergent Properties ◽  
Living Tissue ◽  
Cohesive Material

Living cells communicate and cooperate to produce the emergent properties of tissues. Synthetic mimics of cells, such as liposomes, are typically incapable of cooperation and therefore cannot readily display sophisticated collective behavior. We printed tens of thousands of picoliter aqueous droplets that become joined by single lipid bilayers to form a cohesive material with cooperating compartments. Three-dimensional structures can be built with heterologous droplets in software-defined arrangements. The droplet networks can be functionalized with membrane proteins; for example, to allow rapid electrical communication along a specific path. The networks can also be programmed by osmolarity gradients to fold into otherwise unattainable designed structures. Printed droplet networks might be interfaced with tissues, used as tissue engineering substrates, or developed as mimics of living tissue.

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