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Pawson, Tony >

Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/9437

Title: Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using anti-phosphotyrosine antibody
Authors: Letwin, K
Yee, SP
Pawson, Tony
Keywords: Fusion Proteins, gag-onc
Nerve Tissue Proteins
Protein-Tyrosine Kinase
Receptor Protein-Tyrosine Kinases
Issue Date: Dec-1988
Publisher: Nature Publishing Gro
Citation: Oncogene. 1988 Dec;3(6):621-7
Abstract: 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.
URI: http://www.nature.com
ISSN: 0950-9232
Appears in Collections:Pawson, Tony
Pawson, Tony

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