Specific types of prosomes distribute differentially between intermediate and actin filaments in epithelial, fibroblastic and muscle cells

被引:18
作者
Arcangeletti, C
De Conto, F
Sütterlin, R
Pinardi, F
Missorini, S
Géraud, G
Aebi, U
Chezzi, C
Scherrer, K
机构
[1] Inst Jacques Monod, CNRS, F-75251 Paris 05, France
[2] Univ Paris 07, Paris, France
[3] Univ Parma, Dipartimento Patol & Med Lab, Sez Microbiol, I-43100 Parma, Italy
[4] Univ Basel, Biozentrum, ME Muller Inst, Basel, Switzerland
关键词
prosomes; proteasomes; mRNP; intermediate filaments; microfilament-stress fibers; actin;
D O I
10.1078/0171-9335-00059
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
First observed as components of non-translated mRNP complexes, prosomes harbour RNase and several proteinase activities; they are also the central constituent of the "Multicatalytic Proteinase (MCP) complexes" or "26S-proteasomes". In two recent publications (Arcangeletti et al,, 1997b; De Conto et al,, 1997) we have shown, by applying a new fixation technique, that these particles distribute differentially between the cytoskeletal networks of intermediate filament (IF) and actin types; previously they had been observed exclusively on the intermediate filaments. Here we further investigate the distribution of prosomes of several types, distinct by their subunit composition, between the IF of vimentin type and the actin network, as well as in the 3D space of the cell. It is shown that subtypes of prosomes occupy specific networks of the cytoskeleton, and that this pattern is specific for a given cell type. Confocal microscopy shows that prosome cytodistribution is not homogeneous in the 3D space: in the perinuclear area they colocalize most strongly with the IF, and more peripherally with the microfilament/stress fiber system; connections may exist between the two networks. Furthermore, new data indicate that the prosome-actin interaction may participate in the molecular structure of the stress fibers.
引用
收藏
页码:423 / 437
页数:15
相关论文
共 65 条
[1]   Visualization of prosomes (MCP-proteasomes), intermediate filament and actin networks by ''instantaneous fixation'' preserving the cytoskeleton [J].
Arcangeletti, C ;
Sutterlin, R ;
Aebi, U ;
DeConto, F ;
Missorini, S ;
Chezzi, C ;
Scherrer, K .
JOURNAL OF STRUCTURAL BIOLOGY, 1997, 119 (01) :35-58
[2]  
ARCANGELETTI C, 1992, EUR J CELL BIOL, V59, P464
[3]   Modification of cytoskeleton and prosome networks in relation to protein synthesis in influenza A virus-infected LLC-MK2 cells [J].
Arcangeletti, MC ;
Pinardi, F ;
Missorini, S ;
DeConto, F ;
Conti, G ;
Portincasa, P ;
Scherrer, K ;
Chezzi, C .
VIRUS RESEARCH, 1997, 51 (01) :19-34
[4]   IDENTITY OF THE 19S PROSOME PARTICLE WITH THE LARGE MULTIFUNCTIONAL PROTEASE COMPLEX OF MAMMALIAN-CELLS (THE PROTEASOME) [J].
ARRIGO, AP ;
TANAKA, K ;
GOLDBERG, AL ;
WELCH, WJ .
NATURE, 1988, 331 (6152) :192-194
[5]   Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells [J].
Avalos, RT ;
Yu, Z ;
Nayak, DP .
JOURNAL OF VIROLOGY, 1997, 71 (04) :2947-2958
[6]  
Barois N, 1998, J CELL SCI, V111, P1791
[7]   SINGLE MESSENGER-RNAS VISUALIZED BY ULTRASTRUCTURAL IN-SITU HYBRIDIZATION ARE PRINCIPALLY LOCALIZED AT ACTIN FILAMENT INTERSECTIONS IN FIBROBLASTS [J].
BASSELL, GJ ;
POWERS, CM ;
TANEJA, KL ;
SINGER, RH .
JOURNAL OF CELL BIOLOGY, 1994, 126 (04) :863-876
[8]   The proteasome:: Paradigm of a self-compartmentalizing protease [J].
Baumeister, W ;
Walz, J ;
Zühl, F ;
Seemuller, E .
CELL, 1998, 92 (03) :367-380
[9]   ELECTRON-MICROSCOPY AND IMAGE-ANALYSIS OF THE MULTICATALYTIC PROTEINASE [J].
BAUMEISTER, W ;
DAHLMANN, B ;
HEGERL, R ;
KOPP, F ;
KUEHN, L ;
PFEIFER, G .
FEBS LETTERS, 1988, 241 (1-2) :239-245
[10]  
Bhui AJ, 1996, INT J ONCOL, V9, P669