Peptide antibodies to the human c-fyn gene product demonstrate pp59c-fyn is capable of complex formation with the middle-T antigen of polyomavirus.

S. H. Cheng, R. Harvey, P. C. Espino, Kentaro Senba, T. Yamamoto, K. Toyoshima, A. E. Smith

Research output: Contribution to journalArticle

69 Citations (Scopus)

Abstract

The c-fyn proto-oncogene is a member of a family of closely related genes of which c-src is the prototype. Using peptide antibodies which had been raised against sequences predicted to be specific for the human c-fyn gene product, the c-fyn protein was identified. It is a tyrosine kinase with apparent mol. wt of 59 kd that is also phosphorylated and myristylated. Like pp60c-src and pp62c-yes, pp59c-fyn is able to form a stable complex with middle-T antigen, the transforming protein of polyomavirus. The transformation-defective middle-T mutant NG59, which is unable to associate stably with pp60c-src does not associate with pp59c-fyn. In contrast to pp60c-src, complex formation with middle-T antigen does not lead to a significant increase in the tyrosine kinase activity of pp59c-fyn. These findings lead us to suggest that middle-T mediated transformation may be a consequence of the deregulation of several members of the src-family of protein tyrosine kinases.

Original languageEnglish
Pages (from-to)3845-3855
Number of pages11
JournalEMBO Journal
Volume7
Issue number12
Publication statusPublished - 1988 Dec 1
Externally publishedYes

Fingerprint

Polyomavirus Transforming Antigens
src-Family Kinases
Viral Tumor Antigens
Protein-Tyrosine Kinases
Proto-Oncogene Proteins c-fyn
Genes
src Genes
Polyomavirus
Peptides
Proto-Oncogenes
Antibodies
Deregulation
Proteins

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Immunology and Microbiology(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Cheng, S. H., Harvey, R., Espino, P. C., Senba, K., Yamamoto, T., Toyoshima, K., & Smith, A. E. (1988). Peptide antibodies to the human c-fyn gene product demonstrate pp59c-fyn is capable of complex formation with the middle-T antigen of polyomavirus. EMBO Journal, 7(12), 3845-3855.

Peptide antibodies to the human c-fyn gene product demonstrate pp59c-fyn is capable of complex formation with the middle-T antigen of polyomavirus. / Cheng, S. H.; Harvey, R.; Espino, P. C.; Senba, Kentaro; Yamamoto, T.; Toyoshima, K.; Smith, A. E.

In: EMBO Journal, Vol. 7, No. 12, 01.12.1988, p. 3845-3855.

Research output: Contribution to journalArticle

Cheng, SH, Harvey, R, Espino, PC, Senba, K, Yamamoto, T, Toyoshima, K & Smith, AE 1988, 'Peptide antibodies to the human c-fyn gene product demonstrate pp59c-fyn is capable of complex formation with the middle-T antigen of polyomavirus.', EMBO Journal, vol. 7, no. 12, pp. 3845-3855.
Cheng, S. H. ; Harvey, R. ; Espino, P. C. ; Senba, Kentaro ; Yamamoto, T. ; Toyoshima, K. ; Smith, A. E. / Peptide antibodies to the human c-fyn gene product demonstrate pp59c-fyn is capable of complex formation with the middle-T antigen of polyomavirus. In: EMBO Journal. 1988 ; Vol. 7, No. 12. pp. 3845-3855.
@article{fba6a77d3a704a16b79ef707b014fdcd,
title = "Peptide antibodies to the human c-fyn gene product demonstrate pp59c-fyn is capable of complex formation with the middle-T antigen of polyomavirus.",
abstract = "The c-fyn proto-oncogene is a member of a family of closely related genes of which c-src is the prototype. Using peptide antibodies which had been raised against sequences predicted to be specific for the human c-fyn gene product, the c-fyn protein was identified. It is a tyrosine kinase with apparent mol. wt of 59 kd that is also phosphorylated and myristylated. Like pp60c-src and pp62c-yes, pp59c-fyn is able to form a stable complex with middle-T antigen, the transforming protein of polyomavirus. The transformation-defective middle-T mutant NG59, which is unable to associate stably with pp60c-src does not associate with pp59c-fyn. In contrast to pp60c-src, complex formation with middle-T antigen does not lead to a significant increase in the tyrosine kinase activity of pp59c-fyn. These findings lead us to suggest that middle-T mediated transformation may be a consequence of the deregulation of several members of the src-family of protein tyrosine kinases.",
author = "Cheng, {S. H.} and R. Harvey and Espino, {P. C.} and Kentaro Senba and T. Yamamoto and K. Toyoshima and Smith, {A. E.}",
year = "1988",
month = "12",
day = "1",
language = "English",
volume = "7",
pages = "3845--3855",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Nature Publishing Group",
number = "12",

}

TY - JOUR

T1 - Peptide antibodies to the human c-fyn gene product demonstrate pp59c-fyn is capable of complex formation with the middle-T antigen of polyomavirus.

AU - Cheng, S. H.

AU - Harvey, R.

AU - Espino, P. C.

AU - Senba, Kentaro

AU - Yamamoto, T.

AU - Toyoshima, K.

AU - Smith, A. E.

PY - 1988/12/1

Y1 - 1988/12/1

N2 - The c-fyn proto-oncogene is a member of a family of closely related genes of which c-src is the prototype. Using peptide antibodies which had been raised against sequences predicted to be specific for the human c-fyn gene product, the c-fyn protein was identified. It is a tyrosine kinase with apparent mol. wt of 59 kd that is also phosphorylated and myristylated. Like pp60c-src and pp62c-yes, pp59c-fyn is able to form a stable complex with middle-T antigen, the transforming protein of polyomavirus. The transformation-defective middle-T mutant NG59, which is unable to associate stably with pp60c-src does not associate with pp59c-fyn. In contrast to pp60c-src, complex formation with middle-T antigen does not lead to a significant increase in the tyrosine kinase activity of pp59c-fyn. These findings lead us to suggest that middle-T mediated transformation may be a consequence of the deregulation of several members of the src-family of protein tyrosine kinases.

AB - The c-fyn proto-oncogene is a member of a family of closely related genes of which c-src is the prototype. Using peptide antibodies which had been raised against sequences predicted to be specific for the human c-fyn gene product, the c-fyn protein was identified. It is a tyrosine kinase with apparent mol. wt of 59 kd that is also phosphorylated and myristylated. Like pp60c-src and pp62c-yes, pp59c-fyn is able to form a stable complex with middle-T antigen, the transforming protein of polyomavirus. The transformation-defective middle-T mutant NG59, which is unable to associate stably with pp60c-src does not associate with pp59c-fyn. In contrast to pp60c-src, complex formation with middle-T antigen does not lead to a significant increase in the tyrosine kinase activity of pp59c-fyn. These findings lead us to suggest that middle-T mediated transformation may be a consequence of the deregulation of several members of the src-family of protein tyrosine kinases.

UR - http://www.scopus.com/inward/record.url?scp=0024232372&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024232372&partnerID=8YFLogxK

M3 - Article

VL - 7

SP - 3845

EP - 3855

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 12

ER -