Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein

Science

Volumn 272, Issue 5264, 1996, Pages 1020-1023

  Matsumine, Akihiko ^a   Ogai, Akiko ^a   Senda, Takao ^b   Okumura, Nobuaki ^c   Satoh, Kiyotoshi ^a   Baeg, Gyeong Hun ^a   Kawahara, Takeo ^b   Kobayashi, Shigeru ^b   Okada, Masato ^c   Toyoshima, Kumao ^d   Akiyama, Tetsu ^a  

^a OSAKA UNIVERSITY   (Japan)

^b NAGOYA UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d CENTER FOR ADULT DISEASES   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BETA CATENIN;

ARTICLE; CANCER INHIBITION; COLON POLYPOSIS; DROSOPHILA; GENE EXPRESSION REGULATION; GENE LOCATION; GENE MUTATION; GENE SEQUENCE; HUMAN; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; TUMOR SUPPRESSOR GENE;

EID: 9344271549     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.272.5264.1020     Document Type: Article

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33. 35S]methionine-labeled truncated DLGs, containing the indicated regions, were synthesized by in vitro transcription-translation (Promega) with the use of templates obtained by linearizing the dlg cDNA constructs with restriction enzymes or by polymerase chain reaction. We generated GST fusion proteins by subcloning the cDNAs into pGEX5X-1 (Pharmacia), expressing the fusion proteins in Escherichia coli, and isolating them by absorption to glutathione-Sepharose [D. B. Smith and K. S. Johnson, Gene 67, 31 (1988)]. GST fusion proteins immobilized to glutathione-Sepharose were mixed with in vitro-translated proteins in buffer A [50 mM tris-HCl (pH 7.5), 140 mM NaCl, 2 mM EGTA, 1 mM phenylmethylsulfonyl fluoride, leupeptin (5 μg/ml), and aprotinin (5 μg/ml)] containing 0.1% Triton X-100 for 1 hour at 4°C and then were washed extensively with buffer A containing 0.5% NP-40.
34. 2-terminus and the DHR region of DLG were prepared by immunization of rabbits with peptides containing amino acids 6 to 205 and 203 to 518 of DLG, respectively. Antibody to β-catenin was obtained from Transduction Laboratories. Embryonic mouse brain (embryonic day 18) was lysed with a dounce homogenizer in buffer A (19) containing 1% Triton X-100, and the lysates were incubated with indicated antibodies for 1 hour at 4°C. The immunocomplexes were adsorbed to protein A-Sepharose 4B and washed extensively with buffer A containing 0.1% Triton X-100. Samples were resolved by 5% SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and subjected to immunoblotting.
35. Cell cultures were prepared from the hippocampus of 18-day-old fetal rats [T. L. Fletcher, P. Cameron, P. De Camilli, G. Banker. J. Neurosci. 11, 1617 (1991)]. Staining patterns obtained with anti-APC and anti-DLG were visualized with fluorescein isothiocyanate (FITC)-labeled secondary antibodies to rabbit immunoglobulin G (IgG) (Cappel); those obtained with anti-synaptotagmin (Wako) were visualized with Texas Red-labeled secondary antibodies to mouse IgG (Amersham).
36. 2 and then with FITC-conjugated goat antibody to rabbit IgG (Seikagaku Kogyo) (5).
37. 2 and then with 5-nm colloidal gold-conjugated goat antibody to rabbit IgG (Amersham). After blocking with a goat antibody to rabbit IgG, the sections were stained with anti-APC-COOH and then with 10-nm colloidal gold-conjugated goat antibody to rabbit IgG (Amersham) (5) [H. J. Geuze, J. W. Slot, P. A. van der Ley, R. C. Scheffer, J. Cell Biol. 89, 653 (1981)].
38. T. Senda et al., unpublished data.
39. We thank K. Nagai for encouragement and M. Lamphier for reading the manuscript. Supported by grants-in-aid for Scientific Research on Priority Areas.