The 'ins' and 'outs' of intermediate filament organization

被引:136
作者
Coulombe, PA [1 ]
Bousquet, O
Ma, LL
Yamada, S
Wirtz, D
机构
[1] Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA
[2] Johns Hopkins Univ, Sch Engn, Dept Chem Engn, Baltimore, MD 21205 USA
关键词
D O I
10.1016/S0962-8924(00)01828-6
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
A major function shared by several types of cytoplasmic intermediate filaments (IFs) is to stabilize cellular architecture against the mechanical forces it is subjected to. As for other fibrous cytoskeletal arrays, a crucial determinant of this function is the spatial organization of IFs in the cytoplasm. However, very few crossbridging proteins are specific for IFs - most IF-associated proteins known to exert a structural role act to tether Ifs to other major cytoskeletal elements, such as F-actin, microtubules or adhesion complexes. in addition, IFs are endowed with the ability tit participate in their own organization. This intriguing property is probably connected to the unusual degree of sequence diversity and sequence-specific regulation that characterize IF genes and their proteins. This dependence upon a combination of extrinsic and intrinsic determinants contributes to distinguish IFs from other fibrous cytoskeletal polymers and is key to their function.
引用
收藏
页码:420 / 428
页数:9
相关论文
共 69 条
[1]   THE EXPRESSION OF MUTANT EPIDERMAL KERATIN CDNAS TRANSFECTED IN SIMPLE EPITHELIAL AND SQUAMOUS-CELL CARCINOMA LINES [J].
ALBERS, K ;
FUCHS, E .
JOURNAL OF CELL BIOLOGY, 1987, 105 (02) :791-806
[2]  
Alberts B., 1994, MOL BIOL CELL
[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]   Molecular characteristics and interactions of the intermediate filament protein synemin -: Interactions with α-actinin may anchor synemin-containing heterofilaments [J].
Bellin, RM ;
Sernett, SW ;
Becker, B ;
Ip, W ;
Huiatt, TW ;
Robson, RM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (41) :29493-29499
[5]  
CARY RB, 1995, DEVELOPMENT, V121, P1041
[6]   Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis [J].
Caulin, C ;
Ware, CF ;
Magin, TM ;
Oshima, RG .
JOURNAL OF CELL BIOLOGY, 2000, 149 (01) :17-22
[7]   MICE LACKING VIMENTIN DEVELOP AND REPRODUCE WITHOUT AN OBVIOUS PHENOTYPE [J].
COLUCCIGUYON, E ;
PORTIER, MM ;
DUNIA, I ;
PAULIN, D ;
POURNIN, S ;
BABINET, C .
CELL, 1994, 79 (04) :679-694
[8]   Integrating the actin and vimentin cytoskeletons: Adhesion-dependent formation of fimbrin-vimentin complexes in macrophages [J].
Correia, I ;
Chu, D ;
Chou, YH ;
Goldman, RD ;
Matsudaira, P .
JOURNAL OF CELL BIOLOGY, 1999, 146 (04) :831-842
[9]   DELETIONS IN EPIDERMAL KERATINS LEADING TO ALTERATIONS IN FILAMENT ORGANIZATION INVIVO AND IN INTERMEDIATE FILAMENT ASSEMBLY INVITRO [J].
COULOMBE, PA ;
CHAN, YM ;
ALBERS, K ;
FUCHS, E .
JOURNAL OF CELL BIOLOGY, 1990, 111 (06) :3049-3064
[10]   FOUNDATIONS OF A MISUNDERSTANDING OF THE ULTRASTRUCTURAL BASIS OF MYOCARDIAL FAILURE - A RECIPROCATION NETWORK OF OVERSIMPLIFICATIONS [J].
COULSON, RL ;
FELTOVICH, PJ ;
SPIRO, RJ .
JOURNAL OF MEDICINE AND PHILOSOPHY, 1989, 14 (02) :109-146