AMINOACID EXCHANGE R25W AFFECTS PROPER CELLULAR LOCALISATION OF Best1 PROTEIN IN MDCKII CELLS

被引：0

作者：

Moskova-Doumanova, Veselina ^{[1
]}

Mladenova, Kirilka ^{[1
]}

Petrova, Svetla ^{[1
]}

Topouzova-Hristova, Tanya ^{[1
]}

Chakarova, Christina ^{[2
]}

Lalchev, Zdravko ^{[1
]}

Doumanov, Jordan ^{[1
]}

机构：

[1] St Kl Ohridski Univ Sofia, Fac Biol, Sofia 1164, Bulgaria

[2] UCL, Inst Ophthalmol, Dept Mol Genet, London EC1V 9EV, England

来源：

COMPTES RENDUS DE L ACADEMIE BULGARE DES SCIENCES | 2014年 / 67卷 / 02期

关键词：

Best1; MDCK II cells; BVMD; protein sorting; VITELLIFORM MACULAR DYSTROPHY; VMD2; GENE; MUTATIONS; BESTROPHIN-1; DISEASE; SIGNAL;

D O I：

暂无

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Bestrophinopathies are rare diseases, linked to the mutations in BEST1 gene, coding Best1 protein. This is a channel protein, predominantly expressed on the basolateral membrane of the retinal pigment epithelial cells in the eye. It was recently shown that some mutations alter proper cellular localisation of the protein. In a recent study we investigated localisation of Best1 protein, carrying R25W disease causing mutation, in polarised MDCK II cells. Our observations revealed a growing of apical localisation of the protein but not a complete reverse of polarity. Arginine (R) at position 25 is very conservative and lies between two potential sorting motives. It influences proper localisation of the protein, even though it is not a potential sorting motif itself.

引用

页码：231 / 236

页数：8