Molecular evolution of integrins: Genes encoding integrin beta subunits from a coral and a sponge

被引:118
作者
Brower, DL [1 ]
Brower, SM [1 ]
Hayward, DC [1 ]
Ball, EE [1 ]
机构
[1] UNIV ARIZONA, DEPT MOL & CELLULAR BIOL, TUCSON, AZ 85721 USA
关键词
D O I
10.1073/pnas.94.17.9182
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The integrin family of cell surface receptors is strongly conserved in higher animals, but the evolutionary history of integrins is obscure, We have identified and sequenced cDNAs encoding integrin beta subunits from a coral (phylum Cnidaria) and a sponge (Porifera), indicating that these proteins existed in the earliest stages of metazoan evolution, The coral beta(Cn1) and, especially, the sponge beta(Po1) sequences are the most divergent of the ''beta(1)-class'' integrins and share a number of features not found in any other vertebrate or invertebrate integrins, Perhaps the greatest difference from other beta subunits is found in the third and fourth repeats of the cysteine-rich stalk, where the generally conserved spacings between cysteines are highly variable, but not similar, in beta(Cn1) and beta(Po1). Alternatively spliced cDNAs, containing a stop codon about midway through the full-length translated sequence, were isolated from the sponge library, These cDNAs appear to define a boundary between functional domains, as they would encode a protein that includes the globular ligand-binding head but would be missing the stalk transmembrane, and cytoplasmic domains. These and other sequence comparisons with vertebrate integrins are discussed with respect to models of integrin structure and function.
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页码:9182 / 9187
页数:6
相关论文
共 66 条
[1]   EVIDENCE FOR CELL-SURFACE EXTRACELLULAR-MATRIX BINDING-PROTEINS IN HYDRA-VULGARIS [J].
AGBAS, A ;
SARRAS, MP .
CELL ADHESION AND COMMUNICATION, 1994, 2 (01) :59-73
[2]   AMINO-ACID-SEQUENCE OF THE HUMAN FIBRONECTIN RECEPTOR [J].
ARGRAVES, WS ;
SUZUKI, S ;
ARAI, H ;
THOMPSON, K ;
PIERSCHBACHER, MD ;
RUOSLAHTI, E .
JOURNAL OF CELL BIOLOGY, 1987, 105 (03) :1183-1190
[3]   BETA(2) (CD18) MUTATIONS ABOLISH LIGAND RECOGNITION BY I-DOMAIN INTEGRINS LFA-1 (ALPHA(L)BETA(2), CD11A/CD18) AND MAC-1 (ALPHA(M)BETA(2), CD11B/CD18) [J].
BAJT, ML ;
GOODMAN, T ;
MCGUIRE, SL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (01) :94-98
[4]  
BAJT ML, 1992, J BIOL CHEM, V267, P3789
[5]  
BAJT ML, 1994, J BIOL CHEM, V269, P20913
[6]   A genetic analysis of integrin function: Glanzmann thrombasthenia in vitro [J].
Baker, EK ;
Tozer, EC ;
Pfaff, M ;
Shattil, SJ ;
Loftus, JC ;
Ginsberg, MH .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (05) :1973-1978
[7]   MONOCLONAL-ANTIBODY 9EG7 DEFINES A NOVEL BETA(1) INTEGRIN EPITOPE INDUCED BY SOLUBLE LIGAND AND MANGANESE, BUT INHIBITED BY CALCIUM [J].
BAZZONI, G ;
SHIH, DT ;
BUCK, CA ;
HEMLER, ME .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (43) :25570-25577
[8]   Nucleotide sequence of ub52 from the cnidarian Acropora millepora reveals high evolutionary conservation [J].
Berghammer, H ;
Hayward, D ;
Harrison, P ;
Miller, DJ .
GENE, 1996, 178 (1-2) :195-197
[9]   INTEGRINS HOLD DROSOPHILA TOGETHER [J].
BROWN, NH .
BIOESSAYS, 1993, 15 (06) :383-390
[10]   SINGLE-STEP METHOD OF RNA ISOLATION BY ACID GUANIDINIUM THIOCYANATE PHENOL CHLOROFORM EXTRACTION [J].
CHOMCZYNSKI, P ;
SACCHI, N .
ANALYTICAL BIOCHEMISTRY, 1987, 162 (01) :156-159