Ca2+-dependent cell aggregation of halophilic archaeon, Halobacterium salinarum

2005 ◽  
Vol 100 (6) ◽  
pp. 681-684 ◽  
Author(s):  
Yoshitaka Kawakami ◽  
Takeori Ito ◽  
Masahiro Kamekura ◽  
Masashi Nakayama
2021 ◽  
Vol 134 (22) ◽  
Author(s):  
Takashi Nagata ◽  
Keiichi Inoue

ABSTRACT Rhodopsins are photoreceptive membrane proteins consisting of a common heptahelical transmembrane architecture that contains a retinal chromophore. Rhodopsin was first discovered in the animal retina in 1876, but a different type of rhodopsin, bacteriorhodopsin, was reported to be present in the cell membrane of an extreme halophilic archaeon, Halobacterium salinarum, 95 years later. Although these findings were made by physiological observation of pigmented tissue and cell bodies, recent progress in genomic and metagenomic analyses has revealed that there are more than 10,000 microbial rhodopsins and 9000 animal rhodopsins with large diversity and tremendous new functionality. In this Cell Science at a Glance article and accompanying poster, we provide an overview of the diversity of functions, structures, color discrimination mechanisms and optogenetic applications of these two rhodopsin families, and will also highlight the third distinctive rhodopsin family, heliorhodopsin.


1998 ◽  
Vol 244 (2) ◽  
pp. 505-513 ◽  
Author(s):  
Akira Nagasaki ◽  
Keiko Sutoh ◽  
Hiroyuki Adachi ◽  
Kazuo Sutoh

Extremophiles ◽  
2013 ◽  
Vol 17 (3) ◽  
pp. 485-497 ◽  
Author(s):  
Kimberly M. Webb ◽  
Jerry Yu ◽  
Courtney K. Robinson ◽  
Tomiya Noboru ◽  
Yuan C. Lee ◽  
...  

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
P. Vauclare ◽  
F. Natali ◽  
J. P. Kleman ◽  
G. Zaccai ◽  
B. Franzetti

2020 ◽  
Author(s):  
Anna Yui ◽  
Jose M. M. Caaveiro ◽  
Daisuke Kuroda ◽  
Makoto Nakakido ◽  
Satoru Nagatoishi ◽  
...  

AbstractLI-cadherin is a member of cadherin superfamily which is a Ca2+-dependent cell adhesion protein. Its expression is observed on various types of cells in the human body such as normal small intestine and colon cells, and gastric cancer cells. Because its expression is not observed on normal gastric cells, LI-cadherin is a promising target for gastric cancer imaging. However, since the cell adhesion mechanism of LI-cadherin has remained unknown, rational design of therapeutic molecules targeting this cadherin has been complicated. Here, we have studied the homodimerization mechanism of LI-cadherin. We report the crystal structure of the LI-cadherin EC1-4 homodimer. The EC1-4 homodimer exhibited a unique architecture different from that of other cadherins reported so far. The crystal structure also revealed that LI-cadherin possesses a noncanonical calcium ion-free linker between EC2 and EC3. Various biochemical techniques and molecular dynamics (MD) simulations were employed to elucidate the mechanism of homodimerization. We also showed that the formation of the homodimer observed by the crystal structure is necessary for LI-cadherin-dependent cell adhesion by performing cell aggregation assay.


PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0129215 ◽  
Author(s):  
Rafael Silva-Rocha ◽  
Marjorie Cornejo Pontelli ◽  
Gilvan Pessoa Furtado ◽  
Livia Soares Zaramela ◽  
Tie Koide

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