c-Cbl is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages

Yun Wang, Yee Gruide Yeung, Wallace Y. Langdon, E. Richard Stanley

Research output: Contribution to journalArticle

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Abstract

Early colony stimulating factor-1 (CSF-1)-induced changes in the behavior of p120c-cbl in mouse BAC1.2F5 macrophages were investigated. p120c-cbl is associated with Grfo2 in the cytoplasm of unstimulated cells. Following a 1-min stimulation with CSF-1, p120c-cbl becomes tyrosine-phosphorylated and associates with tyrosine-phosphorylated Shc and an unknown phosphotyrosyl protein (pp80). Simultaneously, it is ubiquitinated and translocated to the membrane. By 10 min of stimulation, this c-Cbl exhibits substantially decreased tyrosine phosphorylation and is de-ubiquitinated and relocated in the cytosol. However, the association of p120c-cbl with Shc persists for at least 60 min. These data indicate that signaling via the CSF-1R involves the transient modification of p120c-cbl and its recruitment as a complex to membrane.

Original languageEnglish (US)
Pages (from-to)17-20
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number1
StatePublished - Jan 5 1996

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Macrophage Colony-Stimulating Factor
Macrophages
Tyrosine
Membranes
Phosphorylation
Cytosol
Cytoplasm
Association reactions
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

c-Cbl is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages. / Wang, Yun; Yeung, Yee Gruide; Langdon, Wallace Y.; Stanley, E. Richard.

In: Journal of Biological Chemistry, Vol. 271, No. 1, 05.01.1996, p. 17-20.

Research output: Contribution to journalArticle

Wang, Yun ; Yeung, Yee Gruide ; Langdon, Wallace Y. ; Stanley, E. Richard. / c-Cbl is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages. In: Journal of Biological Chemistry. 1996 ; Vol. 271, No. 1. pp. 17-20.
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