Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization

被引：11

作者：

Schuetz, Anja ^{[1
]}

Radusheva, Veselina ^{[1
]}

Krug, Susanne M. ^{[2
]}

Heinemann, Udo ^{[1
,3
,4
]}

机构：

[1] Max Delbruck Ctr Mol Med, Helmholtz Prot Sample Prod Facil, Berlin, Germany

[2] Charite, Inst Clin Physiol, Campus Benjamin Franklin, Berlin, Germany

[3] Max Delbruck Ctr Mol Med, Macromol Struct & Interact, Robert Rossle Str 10, D-13125 Berlin, Germany

[4] Free Univ Berlin, Chem & Biochem Inst, Berlin, Germany

来源：

ANNALS OF THE NEW YORK ACADEMY OF SCIENCES | 2017年 / 1405卷 / 01期

关键词：

tight junction; tricellulin; crystal structure; CC domain; dimerization; TIGHT-JUNCTION; SECONDARY-STRUCTURE; PROTEIN; OCCLUDIN; PERMEABILITY; CONTACTS; BARRIER; IDENTIFICATION; MARVELD3; CLAUDINS;

D O I：

10.1111/nyas.13408

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：

Tricellulin is a tight junction protein localized to tricellular contacts in many epithelial tissues, where it is required for full barrier control. Here, we present crystal structures of the tricellulin C-terminal coiled-coil domain, revealing a potential dimeric arrangement. By combining structural, biochemical, functional, and mutation analyses, we gain insight into the mode of tricellulin oligomerization and suggest a model where dimerization of its cytoplasmic C-terminus may play an auxiliary role in stabilizing homophilic and potentially also heterophilic cis-interactions within tight junctions.

引用

页码：147 / 159

页数：13

共 52 条

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