Literature DB >> 2016771

A myristylated form of the sea oncoprotein can transform chicken embryo fibroblasts.

A J Crowe1, M J Hayman.   

Abstract

The transforming gene product of the S13 avian erythroblastosis virus, v-sea, is a member of the growth factor receptor class of tyrosine kinases. In the virus genome, the sea sequences are fused in frame to the virus env gene, thereby generating an abnormally large envelope protein because of the presence of a cytoplasmic tyrosine kinase domain. To determine what role these envelope sequences play in v-sea transformation, we generated a myristylated form of v-sea which contains no envelope sequences. In this report, we show that this myristylated sea-encoded protein retained the ability to transform chicken embryo fibroblasts, indicating that envelope sequences are not essential for transformation by the v-sea tyrosine kinase.

Entities:  

Mesh:

Substances:

Year:  1991        PMID: 2016771      PMCID: PMC240609     

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  27 in total

1.  Identification of two additional v-sea-encoded proteins in avian erythroblastosis virus, S13-infected fibroblasts.

Authors:  J Knight; D R Smith; M J Hayman
Journal:  Virology       Date:  1990-09       Impact factor: 3.616

2.  Synthesis and processing of avian sarcoma virus glycoproteins.

Authors:  M Hayman
Journal:  Virology       Date:  1978-04       Impact factor: 3.616

3.  The putative transforming protein of S13 avian erythroblastosis virus is a transmembrane glycoprotein with an associated protein kinase activity.

Authors:  M J Hayman; G Kitchener; P K Vogt; H Beug
Journal:  Proc Natl Acad Sci U S A       Date:  1985-12       Impact factor: 11.205

4.  S13, a rapidly oncogenic replication-defective avian retrovirus.

Authors:  H Beug; M J Hayman; T Graf; S H Benedict; A M Wallbank; P K Vogt
Journal:  Virology       Date:  1985-08       Impact factor: 3.616

5.  The absence of myristic acid decreases membrane binding of p60src but does not affect tyrosine protein kinase activity.

Authors:  J E Buss; M P Kamps; K Gould; B M Sefton
Journal:  J Virol       Date:  1986-05       Impact factor: 5.103

6.  Myristic acid, a rare fatty acid, is the lipid attached to the transforming protein of Rous sarcoma virus and its cellular homolog.

Authors:  J E Buss; B M Sefton
Journal:  J Virol       Date:  1985-01       Impact factor: 5.103

7.  A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation.

Authors:  F R Cross; E A Garber; D Pellman; H Hanafusa
Journal:  Mol Cell Biol       Date:  1984-09       Impact factor: 4.272

8.  An N-terminal peptide from p60src can direct myristylation and plasma membrane localization when fused to heterologous proteins.

Authors:  D Pellman; E A Garber; F R Cross; H Hanafusa
Journal:  Nature       Date:  1985 Mar 28-Apr 3       Impact factor: 49.962

9.  Avian retrovirus S13: properties of the genome and of the transformation-specific protein.

Authors:  S H Benedict; Y Maki; P K Vogt
Journal:  Virology       Date:  1985-08       Impact factor: 3.616

10.  Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation.

Authors:  M P Kamps; J E Buss; B M Sefton
Journal:  Proc Natl Acad Sci U S A       Date:  1985-07       Impact factor: 11.205

View more
  1 in total

1.  The amino-terminal 14 amino acids of v-src can functionally replace the extracellular and transmembrane domains of v-erbB.

Authors:  M McMahon; R C Schatzman; J M Bishop
Journal:  Mol Cell Biol       Date:  1991-09       Impact factor: 4.272

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.