Organization of multiprotein complexes at cell-cell junctions

被引:113
作者
Ebnet, Klaus [1 ]
机构
[1] Univ Munster, Ctr Mol Biol & Inflammat ZMBE, Inst Med Biochem, Munster, Germany
关键词
adherens junction; tight junction; cell polarity; cell-cell adhesion; protein complexes; JAM; PAR proteins;
D O I
10.1007/s00418-008-0418-7
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The formation of stable cell-cell contacts is required for the generation of barrier-forming sheets of epithelial and endothelial cells. During various physiological processes like tissue development, wound healing or tumorigenesis, cellular junctions are reorganized to allow the release or the incorporation of individual cells. Cell-cell contact formation is regulated by multiprotein complexes which are localized at specific structures along the lateral cell junctions like the tight junctions and adherens junctions and which are targeted to these site through their association with cell adhesion molecules. Recent evidence indicates that several major protein complexes exist which have distinct functions during junction formation. However, this evidence also indicates that their composition is dynamic and subject to changes depending on the state of junction maturation. Thus, cell-cell contact formation and integrity is regulated by a complex network of protein complexes. Imbalancing this network by oncogenic proteins or pathogens results in barrier breakdown and eventually in cancer. Here, I will review the molecular organization of the major multiprotein complexes at junctions of epithelial cells and discuss their function in cell-cell contact formation and maintenance.
引用
收藏
页码:1 / 20
页数:20
相关论文
共 196 条
[81]   Composition and formation of intercellular junctions in epithelial cells [J].
Knust, E ;
Bossinger, O .
SCIENCE, 2002, 298 (5600) :1955-1959
[82]   Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables [J].
Kobielak, A ;
Pasolli, HA ;
Fuchs, E .
NATURE CELL BIOLOGY, 2004, 6 (01) :21-U2
[83]   E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts [J].
Kovacs, EM ;
Ali, RG ;
McCormack, AJ ;
Yap, AS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (08) :6708-6718
[84]   CRB3 binds directly to Par6 and regulates the morphogenesis of the tight junctions in mammalian epithelial cells [J].
Lemmers, C ;
Michel, D ;
Lane-Guermonprez, L ;
Delgrossi, MH ;
Médina, E ;
Arsanto, JP ;
Le Bivic, A .
MOLECULAR BIOLOGY OF THE CELL, 2004, 15 (03) :1324-1333
[85]   Getting to the site of inflammation: the leukocyte adhesion cascade updated [J].
Ley, Klaus ;
Laudanna, Carlo ;
Cybulsky, Myron I. ;
Nourshargh, Sussan .
NATURE REVIEWS IMMUNOLOGY, 2007, 7 (09) :678-689
[86]   A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity [J].
Lin, D ;
Edwards, AS ;
Fawcett, JP ;
Mbamalu, G ;
Scott, JD ;
Pawson, T .
NATURE CELL BIOLOGY, 2000, 2 (08) :540-547
[87]   The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule [J].
Lopez, M ;
Aoubala, M ;
Jordier, F ;
Isnardon, D ;
Gomez, S ;
Dubreuil, P .
BLOOD, 1998, 92 (12) :4602-4611
[88]   Mammalian Crumbs3 is a small transmembrane protein linked to protein associated with Lin-7 (Pals1) [J].
Makarova, O ;
Roh, MH ;
Liu, CJ ;
Laurinec, S ;
Margolis, B .
GENE, 2003, 302 (1-2) :21-29
[89]   Ponsin/SH3P12: An 1-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions [J].
Mandai, K ;
Nakanishi, H ;
Satoh, A ;
Takahashi, K ;
Satoh, K ;
Nishioka, H ;
Mizoguchi, A ;
Takai, Y .
JOURNAL OF CELL BIOLOGY, 1999, 144 (05) :1001-1017
[90]   Afadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction [J].
Mandai, K ;
Nakanishi, H ;
Satoh, A ;
Obaishi, H ;
Wada, M ;
Nishioka, H ;
Itoh, M ;
Mizoguchi, A ;
Aoki, T ;
Fujimoto, T ;
Matsuda, Y ;
Tsukita, S ;
Takai, Y .
JOURNAL OF CELL BIOLOGY, 1997, 139 (02) :517-528