The 300-kDa intermediate filament-associated protein (IFAP300) is a hamster plectin ortholog

被引:15
作者
Clubb, BH
Chou, YH
Herrmann, H
Svitkina, TM
Borisy, GG
Goldman, RD
机构
[1] Northwestern Univ, Sch Med, Dept Cell & Mol Biol, Chicago, IL 60657 USA
[2] German Canc Res Ctr, Div Cell Biol, D-6900 Heidelberg, Germany
[3] Univ Wisconsin, Mol Biol Lab, Madison, WI 53706 USA
关键词
cytoskeleton; plectin; intermediate filament-associated protein;
D O I
10.1006/bbrc.2000.2916
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
Plectin is a high-molecular-weight cytoskeleton-associated protein that was initially identified in intermediate filament (IF) enriched fractions of rat C6 glioma cells, At the cellular level, plectin has been found to associate with IF networks and IF-associated structures that are involved in cell-cell and cell-substrate adhesions, IFAP300 is an IF-associated protein that was initially identified in hamster cells by a monoclonal antibody directed against a high molecular weight protein present in IF-enriched cytoskeletal preparations. Plectin and IFAP300 display similar distribution patterns within cells as determined by immunofluorescence. Based upon this and the finding that their biochemical properties are similar, it has been suggested that they may actually be orthologous proteins. In this paper we demonstrate that this is the case. Cloning and sequencing of most of the hamster plectin cDNA demonstrates that plectin is found in hamster cells and that its sequence is highly conserved between species. Using immunological crossreactivity, epitope mapping, and immunoelectron microscopy, we show that IFAP300 is actually the hamster ortholog of plectin. (C) 2000 Academic Press.
引用
收藏
页码:183 / 187
页数:5
相关论文
共 23 条
[1]
SPECIES-SPECIFIC RECOGNITION PATTERNS OF MONOCLONAL-ANTIBODIES DIRECTED AGAINST VIMENTIN [J].
BOHN, W ;
WIEGERS, W ;
BEUTTENMULLER, M ;
TRAUB, P .
EXPERIMENTAL CELL RESEARCH, 1992, 201 (01) :1-7
[2]
Defective expression of plectin/HD1 in epidermolysis bullosa simplex with muscular dystrophy [J].
Gache, Y ;
Chavanas, S ;
Lacour, JP ;
Wiche, G ;
Owaribe, K ;
Meneguzzi, G ;
Ortonne, JP .
JOURNAL OF CLINICAL INVESTIGATION, 1996, 97 (10) :2289-2298
[3]
Binding of integrin α6β4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding [J].
Geerts, D ;
Fontao, L ;
Nievers, MG ;
Schaapveld, RQJ ;
Purkis, PE ;
Wheeler, GN ;
Lane, EB ;
Leigh, IM ;
Sonnenberg, A .
JOURNAL OF CELL BIOLOGY, 1999, 147 (02) :417-434
[4]
Herrmann H, 1996, J CELL SCI, V109, P569
[5]
HERRMANN H, 1987, J BIOL CHEM, V262, P1320
[6]
MOLECULAR CHARACTERIZATION OF MAMMALIAN CYLICIN, A BASIC-PROTEIN OF THE SPERM HEAD CYTOSKELETON [J].
HESS, H ;
HEID, H ;
FRANKE, WW .
JOURNAL OF CELL BIOLOGY, 1993, 122 (05) :1043-1052
[7]
Plectin abnormality in epidermolysis bullosa simplex Ogna: Non-responsiveness of basal keratinocytes to some anti-rat plectin antibodies [J].
KossHarnes, D ;
Jahnsen, FL ;
Wiche, G ;
Soyland, E ;
Brandtzaeg, P ;
GeddeDahl, T .
EXPERIMENTAL DERMATOLOGY, 1997, 6 (01) :41-48
[8]
PURIFICATION OF THE 300K INTERMEDIATE FILAMENT ASSOCIATED PROTEIN AND ITS INVITRO RECOMBINATION WITH INTERMEDIATE FILAMENTS [J].
LIESKA, N ;
YANG, HY ;
GOLDMAN, RD .
JOURNAL OF CELL BIOLOGY, 1985, 101 (03) :802-813
[9]
Human plectin: Organization of the gene, sequence analysis, and chromosome localization (8q24) [J].
Liu, CG ;
Maercker, C ;
Castanon, MJ ;
Hauptmann, R ;
Wiche, G .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (09) :4278-4283
[10]
Loss of plectin causes epidermolysis bullosa with muscular dystrophy: cDNA cloning and genomic organization [J].
McLean, WHI ;
Pulkkinen, L ;
Smith, FJD ;
Rugg, EL ;
Lane, EB ;
Bullrich, F ;
Burgeson, RE ;
Amano, S ;
Hudson, DL ;
Owaribe, K ;
McGrath, JA ;
McMillan, JR ;
Eady, RAJ ;
Leigh, IM ;
Christiano, AM ;
Uitto, J .
GENES & DEVELOPMENT, 1996, 10 (14) :1724-1735