Literature DB >> 8112607

Alternative splicing generates two distinct transcripts for the Drosophila melanogaster fibroblast growth factor receptor homolog.

M Ito1, T Matsui, T Taniguchi, K Chihara.   

Abstract

We screened Drosophila melanogaster genomic and cDNA libraries by low-stringency hybridization with a probe representing the protein tyrosine kinase (TyK) domain encoded by a human alpha-platelet-derived growth factor receptor-encoding cDNA. The complete sequences of the open reading frames and 3'-untranslated regions (UTR) of some cross-hybridizing clones were identical to the recently published sequence of DFR1, encoding the novel D. melanogaster fibroblast growth factor receptor homology. However, two species of DFR1 cDNAs were isolated that differed with respect to their 5'-UTR. Analysis of the genomic organization revealed that DFR1 is composed of three exons. The entire coding region is contained within the third exon. S1 mapping and RNase-protection assays demonstrated that two distinct DFR1 transcripts possessing either the first or the second exon in combination with the third exon are generated by alternative splicing. This suggests that the transcriptional, as well as posttranscriptional, regulation of fibroblast growth factor receptor (FGFR)-encoding genes during D. melanogaster development is likely to be complex.

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Year:  1994        PMID: 8112607     DOI: 10.1016/0378-1119(94)90758-7

Source DB:  PubMed          Journal:  Gene        ISSN: 0378-1119            Impact factor:   3.688


  2 in total

1.  ACK family tyrosine kinase activity is a component of Dcdc42 signaling during dorsal closure in Drosophila melanogaster.

Authors:  Kai Ping Sem; Baharak Zahedi; Ivan Tan; Maria Deak; Louis Lim; Nicholas Harden
Journal:  Mol Cell Biol       Date:  2002-06       Impact factor: 4.272

Review 2.  Receptor tyrosine kinases in Drosophila development.

Authors:  Richelle Sopko; Norbert Perrimon
Journal:  Cold Spring Harb Perspect Biol       Date:  2013-06-01       Impact factor: 10.005

  2 in total

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