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

Shin Ae Kang, Seung Taek Lee

Research output: Contribution to journalArticlepeer-review

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

Bibliographical note

Funding Information:
This work was supported by a Grant from the National Research Foundation, Ministry of Education, Science, and Technology, Republic of Korea through the project for Studies on Ubiquitome Functions ( M10533010001-05N3301 ) and the Basic Research Program ( 2012R1A1A2007638 ), and by a Seoul Research and Business Development Grant ( 10527 ). S.-A.K. was a pre-doctoral trainee and a post-doctoral trainee of the Brain Korea 21 program from the Ministry of Education, Science, and Technology, Republic of Korea.

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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