PTK6 promotes degradation of c-Cbl through PTK6-mediated phosphorylation

Shin Ae Kang, Seung-Taek Lee

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

PTK6 (also known as Brk) is an intracellular tyrosine kinase which induces proliferation, anti-apoptosis, migration, and anchorage-independent growth. Herein we report that PTK6 phosphorylates and down-regulates E3 ubiquitin ligase c-Cbl. Tyr700, Tyr731, and Tyr774 residues in the C-terminal domain of c-Cbl are major phosphorylation sites targeted by PTK6. The phosphorylated c-Cbl is subjected to auto-ubiquitination and degraded through the ubiquitin-proteasome pathway. These results provide evidence for a novel mechanism demonstrating the oncogenic potential of PTK6 through degradation of c-Cbl, which is an E3 ligase important in down-regulation of oncoproteins.

Original languageEnglish
Pages (from-to)734-739
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume431
Issue number4
DOIs
Publication statusPublished - 2013 Feb 11

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Phosphorylation
Ubiquitin-Protein Ligases
Down-Regulation
Degradation
Ubiquitination
Oncogene Proteins
Proteasome Endopeptidase Complex
Ubiquitin
Protein-Tyrosine Kinases
Apoptosis
Growth

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

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abstract = "PTK6 (also known as Brk) is an intracellular tyrosine kinase which induces proliferation, anti-apoptosis, migration, and anchorage-independent growth. Herein we report that PTK6 phosphorylates and down-regulates E3 ubiquitin ligase c-Cbl. Tyr700, Tyr731, and Tyr774 residues in the C-terminal domain of c-Cbl are major phosphorylation sites targeted by PTK6. The phosphorylated c-Cbl is subjected to auto-ubiquitination and degraded through the ubiquitin-proteasome pathway. These results provide evidence for a novel mechanism demonstrating the oncogenic potential of PTK6 through degradation of c-Cbl, which is an E3 ligase important in down-regulation of oncoproteins.",
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PTK6 promotes degradation of c-Cbl through PTK6-mediated phosphorylation. / Kang, Shin Ae; Lee, Seung-Taek.

In: Biochemical and Biophysical Research Communications, Vol. 431, No. 4, 11.02.2013, p. 734-739.

Research output: Contribution to journalArticle

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AB - PTK6 (also known as Brk) is an intracellular tyrosine kinase which induces proliferation, anti-apoptosis, migration, and anchorage-independent growth. Herein we report that PTK6 phosphorylates and down-regulates E3 ubiquitin ligase c-Cbl. Tyr700, Tyr731, and Tyr774 residues in the C-terminal domain of c-Cbl are major phosphorylation sites targeted by PTK6. The phosphorylated c-Cbl is subjected to auto-ubiquitination and degraded through the ubiquitin-proteasome pathway. These results provide evidence for a novel mechanism demonstrating the oncogenic potential of PTK6 through degradation of c-Cbl, which is an E3 ligase important in down-regulation of oncoproteins.

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