Biochemical characterization of the protein tyrosine kinase homology domain of the ErbBB (HER3) receptor protein

被引:132
作者
Sierke, SL [1 ]
Cheng, KR [1 ]
Kim, HH [1 ]
Koland, JG [1 ]
机构
[1] UNIV IOWA, COLL MED, DEPT PHARMACOL, IOWA CITY, IA 52242 USA
关键词
EPIDERMAL GROWTH-FACTOR; BACULOVIRUS EXPRESSION SYSTEM; HIGH-AFFINITY RECEPTOR; INSULIN-RECEPTOR; PHOSPHATIDYLINOSITOL; 3-KINASE; CYTOPLASMIC DOMAIN; GENE-PRODUCT; ACTIVATION; HEREGULIN; FAMILY;
D O I
10.1042/bj3220757
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The putative protein tyrosine kinase domain (TKD) of the ErbB3 (HER3) receptor protein was generated as a histidine-tagged recombinant protein (hisTKD-B3) and characterized enzymologically. CD spectroscopy indicated that the hisTKD-B3 protein assumed a native conformation with a secondary structure similar to that of the epidermal growth factor (EGF) receptor TKD. However, when compared with the EGF receptor-derived protein, hisTKD-B3 exhibited negligible intrinsic protein tyrosine kinase activity. Immune complex kinase assays of full-length ErbB3 proteins also yielded no evidence of catalytic activity. A fluorescence assay previously used to characterize the nucleotide-binding properties of the EGF receptor indicated that the ErbB3 protein was unable to bind nucleotide. The hisTKD-B3 protein was subsequently found to be an excellent substrate for the EGF receptor protein tyrosine kinase, which suggested that in able phosphorylation of ErbB3 in response to EGF could be attributed to a direct cross-phosphorylation by the EGF receptor protein tyrosine kinase.
引用
收藏
页码:757 / 763
页数:7
相关论文
共 46 条
[1]  
BEERLI RR, 1995, MOL CELL BIOL, V15, P6496
[2]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[3]  
CARRAWAY KL, 1994, J BIOL CHEM, V269, P14303
[4]   A NEU ACQUAINTANCE FOR ERBB3 AND ERBB4 - A ROLE FOR RECEPTOR HETERODIMERIZATION IN GROWTH SIGNALING [J].
CARRAWAY, KL ;
CANTLEY, LC .
CELL, 1994, 78 (01) :5-8
[5]   Nucleotide binding by the epidermal growth factor receptor protein-tyrosine kinase - Trinitrophenyl-ATP as a spectroscopic probe [J].
Cheng, KR ;
Koland, JG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (01) :311-318
[6]   SYNTHESIS OF EPIDERMAL GROWTH-FACTOR (EGF) RECEPTOR INVITRO USING SP6-RNA POLYMERASE-TRANSCRIBED TEMPLATE MESSENGER-RNA [J].
CLARK, AJL ;
BEGUINOT, L ;
ISHII, S ;
MA, DP ;
ROE, BA ;
MERLINO, GT ;
PASTAN, I .
BIOCHIMICA ET BIOPHYSICA ACTA, 1986, 867 (04) :244-251
[7]  
COBB MH, 1989, J BIOL CHEM, V264, P18701
[8]   A KINASE-NEGATIVE EPIDERMAL GROWTH-FACTOR RECEPTOR THAT RETAINS THE CAPACITY TO STIMULATE DNA-SYNTHESIS [J].
COKER, KJ ;
STAROS, JV ;
GUYER, CA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (15) :6967-6971
[9]   SIGNALING BY RECEPTOR TYROSINE KINASES [J].
FANTL, WJ ;
JOHNSON, DE ;
WILLIAMS, LT .
ANNUAL REVIEW OF BIOCHEMISTRY, 1993, 62 :453-481
[10]   DETECTION AND PURIFICATION OF A RECOMBINANT HUMAN B-LYMPHOTROPIC VIRUS (HHV-6) IN THE BACULOVIRUS EXPRESSION SYSTEM BY LIMITING DILUTION AND DNA DOT-BLOT HYBRIDIZATION [J].
FUNG, MC ;
CHIU, KYM ;
WEBER, T ;
CHANG, TW ;
CHANG, NT .
JOURNAL OF VIROLOGICAL METHODS, 1988, 19 (01) :33-42