Oncogenic functions of PTK6 are enhanced by its targeting to plasma membrane but abolished by its targeting to nucleus

Han Ie Kim, Seung-Taek Lee

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

PTK6 (also known as Brk) is an intracellular tyrosine kinase whose expression is up-regulated in several tumour types. Because localization of protein tyrosine kinases plays an important role in the development of cancers, we investigated the relationship between subcellular localization of PTK6 and its oncogenic properties. PTK6 was targeted to the plasma membrane or the nucleus of HEK 293 cells using the Src myristoylation signal (Myr) or SV40 T-antigen nuclear localization signal (NLS), respectively. The profile of cellular proteins phosphorylated by Myr-PTK6 was quite different from those phosphorylated by NLS-PTK6. Localization of PTK6 to the plasma membrane enhanced the ability of PTK6 to promote proliferation, cell survival and migration and to permit anchorage-independent colony formation. In contrast, nuclear localization of PTK6 impaired these functions. Our results demonstrate that recruitment of PTK6 to the plasma membrane is required for oncogenic function.

Original languageEnglish
Pages (from-to)133-139
Number of pages7
JournalJournal of Biochemistry
Volume146
Issue number1
DOIs
Publication statusPublished - 2009 Jul 1

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Cell membranes
Nuclear Localization Signals
Cell Membrane
Protein-Tyrosine Kinases
Polyomavirus Transforming Antigens
HEK293 Cells
Cell proliferation
Cell Movement
Tumors
Neoplasms
Cell Survival
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

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abstract = "PTK6 (also known as Brk) is an intracellular tyrosine kinase whose expression is up-regulated in several tumour types. Because localization of protein tyrosine kinases plays an important role in the development of cancers, we investigated the relationship between subcellular localization of PTK6 and its oncogenic properties. PTK6 was targeted to the plasma membrane or the nucleus of HEK 293 cells using the Src myristoylation signal (Myr) or SV40 T-antigen nuclear localization signal (NLS), respectively. The profile of cellular proteins phosphorylated by Myr-PTK6 was quite different from those phosphorylated by NLS-PTK6. Localization of PTK6 to the plasma membrane enhanced the ability of PTK6 to promote proliferation, cell survival and migration and to permit anchorage-independent colony formation. In contrast, nuclear localization of PTK6 impaired these functions. Our results demonstrate that recruitment of PTK6 to the plasma membrane is required for oncogenic function.",
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Oncogenic functions of PTK6 are enhanced by its targeting to plasma membrane but abolished by its targeting to nucleus. / Ie Kim, Han; Lee, Seung-Taek.

In: Journal of Biochemistry, Vol. 146, No. 1, 01.07.2009, p. 133-139.

Research output: Contribution to journalArticle

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