Plakins: a family of versatile cytolinker proteins

被引:245
作者
Leung, CL
Green, KJ
Liem, RKH
机构
[1] Columbia Univ Coll Phys & Surg, Dept Pathol, New York, NY 10032 USA
[2] Columbia Univ Coll Phys & Surg, Dept Anat & Cell Biol, New York, NY 10032 USA
[3] Northwestern Univ, Sch Med, RH Lurie Canc Ctr, Chicago, IL 60611 USA
[4] Northwestern Univ, Sch Med, Dept Pathol, Chicago, IL 60611 USA
[5] Northwestern Univ, Sch Med, Dept Dermatol, Chicago, IL 60611 USA
关键词
D O I
10.1016/S0962-8924(01)02180-8
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
By connecting cytoskeletal elements to each other and to junctional complexes, the plakin family of cytolinkers plays a crucial role in orchestrating cellular development and maintaining tissue integrity. Plakins are built from combinations of interacting domains that bind to microfilaments, microtubules, intermediate filaments, cell-adhesion molecules and members of the armadillo family. Plakins are involved in both inherited and autoimmune diseases that affect the skin, neuronal tissue, and cardiac and skeletal muscle. Here, we describe the members of the plakin family and their interaction partners, and give examples of the cellular defects that result from their dysfunction.
引用
收藏
页码:37 / 45
页数:9
相关论文
共 84 条
[1]   Antibodies against desmoglein 3 (Pemphigus vulgaris antigen) are present in sera from patients with paraneoplastic pemphigus and cause acantholysis in vivo in neonatal mice [J].
Amagai, M ;
Nishikawa, T ;
Nousari, HC ;
Anhalt, GJ ;
Hashimoto, T .
JOURNAL OF CLINICAL INVESTIGATION, 1998, 102 (04) :775-782
[2]   Not just scaffolding:: plectin regulates actin dynamics in cultured cells [J].
Andrä, K ;
Nikolic, B ;
Stöcher, M ;
Drenckhahn, D ;
Wiche, G .
GENES & DEVELOPMENT, 1998, 12 (21) :3442-3451
[3]   Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture [J].
Andra, K ;
Lassmann, H ;
Bittner, R ;
Shorny, S ;
Fassler, R ;
Propst, F ;
Wiche, G .
GENES & DEVELOPMENT, 1997, 11 (23) :3143-3156
[4]  
ANGST BD, 1990, J CELL SCI, V97, P247
[5]   MIDGESTATIONAL LETHALITY IN MICE LACKING KERATIN-8 [J].
BARIBAULT, H ;
PRICE, J ;
MIYAI, K ;
OSHIMA, RG .
GENES & DEVELOPMENT, 1993, 7 (7A) :1191-1202
[6]   Cloning and characterization of mouse ACF7, a novel member of the dystonin subfamily of actin binding proteins [J].
Bernier, G ;
Mathieu, M ;
DeRepentigny, Y ;
Vidal, SM ;
Kothary, R .
GENOMICS, 1996, 38 (01) :19-29
[7]  
Bornslaeger EA, 2001, J CELL SCI, V114, P727
[8]   Breaking the connection: Displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly [J].
Bornslaeger, EA ;
Corcoran, CM ;
Stappenbeck, TS ;
Green, KJ .
JOURNAL OF CELL BIOLOGY, 1996, 134 (04) :985-1001
[9]   MICROFILAMENT REORGANIZATION DURING APOPTOSIS - THE ROLE OF GAS2, A POSSIBLE SUBSTRATE FOR ICE-LIKE PROTEASES [J].
BRANCOLINI, C ;
BENEDETTI, M ;
SCHNEIDER, C .
EMBO JOURNAL, 1995, 14 (21) :5179-5190
[10]   THE MOUSE DYSTONIA MUSCULORUM GENE IS A NEURAL ISOFORM OF BULLOUS PEMPHIGOID ANTIGEN-1 [J].
BROWN, A ;
BERNIER, G ;
MATHIEU, M ;
ROSSANT, J ;
KOTHARY, R .
NATURE GENETICS, 1995, 10 (03) :301-306