HER-2/c-erbB2 is phosphorylated by calmodulin-dependent protein kinase II on a single site in the cytoplasmic tail at threonine-1172

Oncogene

Volumn 12, Issue 12, 1996, Pages 2725-2730

  Feinmesser, Rachel L ^a   Gray, Kirsty ^a   Means, Anthony R ^b   Chantry, Andrew ^a  

^a IMPERIAL COLLEGE SCHOOL OF MEDICINE   (United Kingdom)

^b DUKE UNIVERSITY   (United States)

Author keywords

Calmodulin dependent protein kinase; Desensitisation; HER 2 c erbB2; Tyrosine kinases

Indexed keywords

COMPLEMENTARY DNA; EPIDERMAL GROWTH FACTOR RECEPTOR; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MEMBRANE PROTEIN; PHOSPHOAMINO ACID; PHOSPHORUS 32; PROTEIN KINASE (CALCIUM,CALMODULIN); PROTEIN TYROSINE KINASE; THREONINE;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; AUTOPHOSPHORYLATION; CONTROLLED STUDY; DNA TRANSFECTION; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; ISOTOPE LABELING; NONHUMAN; ONCOGENE C ERB; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTO ONCOGENE; RAT; RECEPTOR BINDING; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CYTOPLASM; EPIDERMAL GROWTH FACTOR; FIBROBLASTS; HUMANS; MOLECULAR SEQUENCE DATA; PHOSPHOPEPTIDES; PHOSPHORYLATION; RATS; RECEPTOR, EPIDERMAL GROWTH FACTOR; RECEPTOR, ERBB-2; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; THREONINE;

CATHARANTHUS ROSEUS; CHIMAERA; FUNGI;

EID: 0029938094     PISSN: 09509232     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (24)

1. Akiyama T, Saito T, Ogawara H, Toyoshima K and Yamamoto T. (1988). Mol. Cell. Biol., 8, 1019-1026.
2. Boyle WJ, van der Geer P and Hunter T. (1991). Meth. Enzymol., 201, 110-149.
3. Chantry A. (1995). J. Biol. Chem., 270, 3068-3073.
4. Chen C and Okayama H. (1987). Mol. Cell. Biol., 7, 2745-2752.
5. Countaway JL, McQuilkin P, Girones N and Davis RJ. (1990). J. Biol. Chem., 265, 3407-3416.
6. Countaway JL, Nairn AC and Davis RJ (1992). J. Biol. Chem., 267, 1129-1140.
7. Coussens L, Yang-Feng TL, Liao YC, Chen E, Gray A, McGrath J, Seeburg PH, Libermann TA, Schlessinger J, Francke U, Levinson A and Ullrich A. (1985). Science 230, 1132-1139.
8. Cruzalegui FH, Kapiloff MS, Morfin JP, Kemp BE, Rosenfeld MG and Means AR. (1992). Proc. Natl. Acad. Sci. USA. 89, 12127-12131.
9. Davis RJ. (1988). J. Biol. Chem., 263, 9462-9469.
10. Di Fiore PP, Pierce JH, Fleming TP, Hazan R, Ullrich A, King CR, Schlessinger J and Aaronson S. (1987). Cell, 51, 1063-1070.
11. Di Fiore PP, Heiln K, Kraus MH, Pierce JH, Artrip J, Segatto O and Bottaro DP (1992). EMBO J. 11, 3927-3933.
12. Dobashi K, Weiner DB and Greene MI. (1989). DNA, 8, 723-732.
13. Gorman CM, Gies D, McCray G and Huang M. (1988). Virology, 171, 377-385.
14. Heisermann GJ and Gill GN. (1988). J. Biol. Chem., 263, 13152-13158.
15. Heldin K-H. (1995). Cell, 80, 213-223.
16. Kuppuswamy D, Dalton M and Pike LJ. (1993). J. Biol. Chem., 268, 19134-19142.
17. Lee J, Dull TJ, Lax I, Schlessinger J and Ullrich A. (1989). EMBO J., 8, 167-173.
18. Lemmon MA and Schlessinger J. (1994). TIBS, 19, 459-463.
19. Morrison P, Takishima K and Rosner MR. (1993). J. Biol. Chem., 268, 15536-15543.
20. Pawson T. (1995). Nature, 373, 573-580.
21. Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A and McGuire WL. (1987). Science, 235, 177-182.
22. Theroux SJ, Taglienti-Sian C, Nair N, Countaway JL, Robinson HL and Davis RJ. (1992). J. Biol. Chem., 267, 7967-7970.
23. Ullrich A and Schlessinger J. (1990). Cell, 61, 203-212.
24. Ullrich A, Coussens L, Hayflick JS, Dull TJ, Gray A, Tam AW, Lee J, Yarden Y, Libermann TA, Sehlessinger J, Downward J, Mayes ELV, Whittle N, Waterfield MD and Seeburg PH. (1984). Nature, 309, 418-425.