Cloning of a novel phosphoprotein regulated by colony-stimulating factor 1 shares a domain with the Drosophila disabled gene product

Xiangxi Xu, W. Yang, S. Jackowski, C. O. Rock

Research output: Contribution to journalArticle

121 Citations (Scopus)

Abstract

A unique protein with an apparent molecular mass of 96 kilodaltons (p96) was detected in the routine macrophage cell line, BAC1.2F5. The murine cDNA encoding p96 was cloned and sequenced, along with cDNAs representing two alternatively spliced forms of the protein. All three proteins possessed identical amino-terminal domains with significant similarity to the amino- terminal domain of the Drosophila disabled gene product and carboxyl-terminal domains containing proline-rich sequences characteristic of src homology region (domain 3) binding regions. BAC1.2F5 cells predominately expressed the p96 protein, although mRNA and protein corresponding to the p67 splice variant were also detected. Electrophoretic gel retardation of p96 in response to stimulation of the cells with colony-stimulating factor 1 was noticeable within 5 min after growth factor addition and reached a maximum at 60 min. Metabolic labeling experiments showed that the gel retardation of p96 was associated with increased phosphorylation of the protein exclusively on serine residues. These data identify a novel protein that is phosphorylated in response to mitogenic growth factor stimulation.

Original languageEnglish
Pages (from-to)14184-14191
Number of pages8
JournalJournal of Biological Chemistry
Volume270
Issue number23
DOIs
StatePublished - Jan 1 1995
Externally publishedYes

Fingerprint

Macrophage Colony-Stimulating Factor
Cloning
Phosphoproteins
Drosophila
Organism Cloning
Genes
Proteins
Intercellular Signaling Peptides and Proteins
Complementary DNA
Gels
Phosphorylation
src Homology Domains
Macrophages
Molecular mass
Proline
Labeling
Serine
Cells
Cell Line
Messenger RNA

ASJC Scopus subject areas

  • Biochemistry

Cite this

Cloning of a novel phosphoprotein regulated by colony-stimulating factor 1 shares a domain with the Drosophila disabled gene product. / Xu, Xiangxi; Yang, W.; Jackowski, S.; Rock, C. O.

In: Journal of Biological Chemistry, Vol. 270, No. 23, 01.01.1995, p. 14184-14191.

Research output: Contribution to journalArticle

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