The Human PTK6 Interacts with a 23-kDa Tyrosine-Phosphorylated Protein and is localized in Cytoplasm in Breast Carcinoma T-47D Cells

Joon Seol Bae, Seung Taek Lee

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The human PTK6 (also known as Brk) polypeptide, which is deduced from its full-length cDNA, represents a nonreceptor protein tyrosine kinase (PTK). It contains SH3, SH2, and tyrosine kinase catalytic domains that are closely related to Src family members. We generated an antihuman PTK6 antibody by immunizing rabbits with a PTK6-specific oligopeptide conjugated to BSA, which corresponds to 11 amino acid residues near the C-terminus. An immunoblot analysis with the antibody detected an expected 52-kDa band in various mammalian transformed cell lines. Immunoprecipitation and immunoblot analyses demonstrated that PTK6 is phosphorylated on the tyrosine residue(s) and interacts with approximately a 23-kDa tyrosine-phosphorylated polypeptide (most likely a substrate of PTK6) in breast carcinoma T-47D cells. An immunofluorescence analysis demonstrated that PTK6 is localized throughout the cytoplasm of T-47D cells. These results support a possible role for PTK6 in the intracellular signal transduction through tyrosine phosphorylation.

Original languageEnglish
Pages (from-to)33-38
Number of pages6
JournalJournal of biochemistry and molecular biology
Volume34
Issue number1
Publication statusPublished - 2001 Jan 31

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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