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Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using anti-phosphotyrosine antibody.

Authors: Letwin, K  Yee, SP  Pawson, T 
Citation: Letwin K, etal., Oncogene 1988 Dec;3(6):621-7.
Pubmed: (View Article at PubMed) PMID:2485255

A rat brain lambda gt11 cDNA expression library was screened with anti-phosphotyrosine antibody to identify recombinant clones that encode enzymatically active protein-tyrosine kinases. The inserts of two bacteriophage that gave positive signals were sequenced. Both translation products possess sequence motifs characteristic of protein-tyrosine kinases. However, each polypeptide is distinct from previously described members of the tyrosine kinase family. The predicted product of the lambda B1 clone contains a catalytic domain and C-terminal tail most closely related to the eph gene product, a presumed transmembrane receptor-like protein-tyrosine kinase. The clone lambda B2 encodes a partial SH2 domain and a kinase domain similar in organization and sequence to the fps/fes cytoplasmic protein-tyrosine kinase. These new protein-tyrosine kinases (elk and flk) are apparently members of subfamilies for which eph and fps/fes are prototypes. elk is predominantly expressed in brain, while flk RNA is widely distributed and most abundant in testes. The preferential isolation of cDNAs for previously uncharacterized protein-tyrosine kinases in a screen based on catalytic activity suggests that additional members of the protein-tyrosine kinase family remain to be identified.

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CRRD Object Information
CRRD ID: 632706
Created: 2003-08-29
Species: All species
Last Modified: 2004-05-25
Status: ACTIVE



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