Biochemical and Biophysical Research Communications
Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin☆
Section snippets
Materials
Human Axl cDNA was provided by Dr. ET Liu, NIH, Bethesda, MD, USA. This contained the sequence for Axl transcript variant 1 (GenBank Accession No. NM_021913), which possesses nine amino acids more than variant 2, although their cytoplasmic sequences are identical. The cDNA clone for original KIAA1075 (Accession No. AB028998) was a gift of Kazusa DNA Research Institute, Chiba, Japan. The sequence was an ORF of 4962 bp [15] housed in pBluescript II SK+ cloning vector (Stratagene). All
Yeast two-hybrid interactions with Axl-IC
We screened a human heart cDNA library in yeast to identify proteins that interact with the cytoplasmic domain of human Axl. The result of a large-scale mating yielded 64 colonies, which still exhibited activation of all reporter genes (HIS3, ADE2, lacZ, and MEL1) after three re-streaks. We PCR-amplified and sequenced the partner DNA sequences from 33 colonies, which were then identified by BLAST search (Table 1). Expression of the actual partner fusion proteins was verified by Western blotting
Acknowledgements
S.H. was supported by a Marie Curie Fellowship of the European Community Human Potential programme under Contract No. HPMF-CT-1999-000123 and by the Swedish Royal Science Academy (Per-Erik Lindahl stipend). This work was further supported by the Swedish Cancer Society project Grant No. 4413-B01-02XBB, Alfred Österlund Trust, Malmö University Hospital Trust, Malmö University Hospital Cancer Trust, Greta and Johan Kock Trust, and Crafoord Trust. The cDNA sequences for C1-TEN/KIAA1075 splice
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Abbreviations: C1-TEN, C1 domain-containing phosphatase and TENsin homologue; RTK, receptor tyrosine kinase; Axl-IC, Axl intracellular domain; Gas6, growth arrest-specific gene 6 product; SH2, Src homology 2; PTB, phosphotyrosine-binding; PI3K, phosphatidylinositol 3-kinase; RACE, real amplification of cDNA ends.