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PMID: 2747647 Published · ppublish English Journal Article

The myristylation signal of p60v-src functionally complements the N-terminal fps-specific region of P130gag-fps.

Molecular and cellular biology ·Vol. 9 ·No. 5 ·1989-05-00 ·Pages 2214-9

Brooks-Wilson AR, Ball E, Pawson T

Abstract

The P130gag-fps protein-tyrosine kinase of Fujinami sarcoma virus contains an N-terminal fps-specific domain (Nfps) that is important for oncogenicity. The N-terminal 14 amino acids of p60v-src, which direct myristylation and membrane association, can replace the gag-Nfps sequences of P130gag-fps (residues 1 to 635), producing a highly transforming src-fps polypeptide. Conversely, gag-Nfps can restore modest transforming activity to a nonmyristylated v-src polypeptide. These results emphasize the modular construction of protein-tyrosine kinases and indicate that Nfps, possibly in conjunction with gag, functions in the subcellular localization of P130gag-fps.

MeSH Terms
Amino Acid Sequence Base Sequence Cell Line, Transformed DNA/genetics Genetic Complementation Test Molecular Sequence Data Myristic Acids/metabolism Oncogene Proteins, Viral/genetics Protein-Tyrosine Kinases/genetics Recombinant Proteins/genetics,metabolism Subcellular Fractions/metabolism
Chemicals
Myristic Acids Oncogene Proteins, Viral Recombinant Proteins DNA Protein-Tyrosine Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Brooks-Wilson A R
Division of Molecular and Developmental Biology, Mount Sinai Hospital Research Institute, Toronto, Ontario, Canada.
Ball E
Pawson T
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41 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1989-05-00
Pages
2214-9
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC363016
Subset
IM
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