A target for Src in mitosis

Stefano Fumagalli, Nicholas F. Totty, J. Justin Hsuan, Sara Courtneidge

Research output: Contribution to journalArticle

306 Citations (Scopus)

Abstract

The activity of the c-Src protein is increased during cell-cycle stage G1 in fibroblasts stimulated with certain growth factors, and at the G2/M transition, but little is known about Src substrates in ese circumstances. In contrast, cells transformed with activated Src contain many tyrosine-phosphorylated proteins. We compared the phosphotyrosine content of growing and mitotically arrested Src-transformed cells. We report here that although phosphorylation of most proteins was unchanged during mitosis, phosphorylation of one of about 68K was greatly enhanced. The p68 was physically associated with activated c-Src, and it bound to the SH3 domain of c-Src in vitro. Tyrosine-phosphorylated p68 was also present in mitotic extracts of normal cells, suggesting that its phosphorylation was not just a consequence of transformation. Purification and microsequencing of p68 showed that it was related to the previously described GAP-associated protein p62.

Original languageEnglish (US)
Pages (from-to)871-874
Number of pages4
JournalNature
Volume368
Issue number6474
DOIs
StatePublished - Apr 28 1994
Externally publishedYes

Fingerprint

Mitosis
Phosphorylation
Tyrosine
Phosphotyrosine
Proteins
src Homology Domains
Cell Extracts
Intercellular Signaling Peptides and Proteins
Cell Cycle
Fibroblasts

ASJC Scopus subject areas

  • General

Cite this

Fumagalli, S., Totty, N. F., Hsuan, J. J., & Courtneidge, S. (1994). A target for Src in mitosis. Nature, 368(6474), 871-874. https://doi.org/10.1038/368871a0

A target for Src in mitosis. / Fumagalli, Stefano; Totty, Nicholas F.; Hsuan, J. Justin; Courtneidge, Sara.

In: Nature, Vol. 368, No. 6474, 28.04.1994, p. 871-874.

Research output: Contribution to journalArticle

Fumagalli, S, Totty, NF, Hsuan, JJ & Courtneidge, S 1994, 'A target for Src in mitosis', Nature, vol. 368, no. 6474, pp. 871-874. https://doi.org/10.1038/368871a0
Fumagalli S, Totty NF, Hsuan JJ, Courtneidge S. A target for Src in mitosis. Nature. 1994 Apr 28;368(6474):871-874. https://doi.org/10.1038/368871a0
Fumagalli, Stefano ; Totty, Nicholas F. ; Hsuan, J. Justin ; Courtneidge, Sara. / A target for Src in mitosis. In: Nature. 1994 ; Vol. 368, No. 6474. pp. 871-874.
@article{1d8d379d0f3b4223af41f0fe5ee12edf,
title = "A target for Src in mitosis",
abstract = "The activity of the c-Src protein is increased during cell-cycle stage G1 in fibroblasts stimulated with certain growth factors, and at the G2/M transition, but little is known about Src substrates in ese circumstances. In contrast, cells transformed with activated Src contain many tyrosine-phosphorylated proteins. We compared the phosphotyrosine content of growing and mitotically arrested Src-transformed cells. We report here that although phosphorylation of most proteins was unchanged during mitosis, phosphorylation of one of about 68K was greatly enhanced. The p68 was physically associated with activated c-Src, and it bound to the SH3 domain of c-Src in vitro. Tyrosine-phosphorylated p68 was also present in mitotic extracts of normal cells, suggesting that its phosphorylation was not just a consequence of transformation. Purification and microsequencing of p68 showed that it was related to the previously described GAP-associated protein p62.",
author = "Stefano Fumagalli and Totty, {Nicholas F.} and Hsuan, {J. Justin} and Sara Courtneidge",
year = "1994",
month = "4",
day = "28",
doi = "10.1038/368871a0",
language = "English (US)",
volume = "368",
pages = "871--874",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6474",

}

TY - JOUR

T1 - A target for Src in mitosis

AU - Fumagalli, Stefano

AU - Totty, Nicholas F.

AU - Hsuan, J. Justin

AU - Courtneidge, Sara

PY - 1994/4/28

Y1 - 1994/4/28

N2 - The activity of the c-Src protein is increased during cell-cycle stage G1 in fibroblasts stimulated with certain growth factors, and at the G2/M transition, but little is known about Src substrates in ese circumstances. In contrast, cells transformed with activated Src contain many tyrosine-phosphorylated proteins. We compared the phosphotyrosine content of growing and mitotically arrested Src-transformed cells. We report here that although phosphorylation of most proteins was unchanged during mitosis, phosphorylation of one of about 68K was greatly enhanced. The p68 was physically associated with activated c-Src, and it bound to the SH3 domain of c-Src in vitro. Tyrosine-phosphorylated p68 was also present in mitotic extracts of normal cells, suggesting that its phosphorylation was not just a consequence of transformation. Purification and microsequencing of p68 showed that it was related to the previously described GAP-associated protein p62.

AB - The activity of the c-Src protein is increased during cell-cycle stage G1 in fibroblasts stimulated with certain growth factors, and at the G2/M transition, but little is known about Src substrates in ese circumstances. In contrast, cells transformed with activated Src contain many tyrosine-phosphorylated proteins. We compared the phosphotyrosine content of growing and mitotically arrested Src-transformed cells. We report here that although phosphorylation of most proteins was unchanged during mitosis, phosphorylation of one of about 68K was greatly enhanced. The p68 was physically associated with activated c-Src, and it bound to the SH3 domain of c-Src in vitro. Tyrosine-phosphorylated p68 was also present in mitotic extracts of normal cells, suggesting that its phosphorylation was not just a consequence of transformation. Purification and microsequencing of p68 showed that it was related to the previously described GAP-associated protein p62.

UR - http://www.scopus.com/inward/record.url?scp=0028220672&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028220672&partnerID=8YFLogxK

U2 - 10.1038/368871a0

DO - 10.1038/368871a0

M3 - Article

C2 - 7512695

AN - SCOPUS:0028220672

VL - 368

SP - 871

EP - 874

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6474

ER -