Faculty Opinions recommendation of Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation.

2005 ◽  
Author(s):  
Antonio Rosato
Keyword(s):  
Membrane Protein ◽  
Calcium Pump ◽  
Conformational Switch ◽  
Interaction Surface

The plasma membrane protein Rch1 and the Golgi/ER calcium pump Pmr1 have an additive effect on filamentation in Candida albicans

2018 ◽  
Vol 115 ◽  
pp. 1-8 ◽  
Author(s):  
Linghuo Jiang ◽  
Dayong Xu ◽  
Ahsan Hameed ◽  
Tianshu Fang ◽  
Abu Bakr Ahmad Fazili ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Additive Effect ◽  
Calcium Pump ◽  
Plasma Membrane Protein ◽  
Er Calcium

The Effect of Exogenous Fluoride on the Calcium PUMP, Ciliary Activity, and Shell Formation of the Fingernail Clam, Musculium Transversum

1982 ◽  
Vol 40 ◽  
pp. 58-59
Author(s):  
Anthony Paparo ◽  
Judy A. Murphy ◽  
Robert Dean
Keyword(s):  
Mississippi River ◽  
Calcium Pump ◽  
Bottom Fauna ◽  
Ciliary Activity ◽  
Shell Formation ◽  
Middle Reach ◽  
Shell Matrix ◽  
Fingernail Clams ◽  
Ca Carbonate

In the mid-1950's, fingernail clams virtually disappeared from a 100-mile section of the IL River, a tributary of the Mississippi River, due to unknown causes. A survey of the bottom fauna of the IL River in 1979, revealed that the clams were still absent from the middle reach of the River, where they had been abundant prior to the die-off in the 1950's. Some factor(s) in the River currently prevent the clams from recolonizing areas where they were formerly abundant. Recently, clams exposed to fluoride developed abnormal grooves in the shell matrix. Fluorides are known to be protoplasmic poisons removing essential body calcium by precipitation. Since the shell consists primarily of Ca carbonate, this investigation examines the possible role of fluoride on shell formation and the poisoning of the Ca pump which can directly inhibit lateral ciliary activity on the gill.

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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