The protein content of an adaptor protein, STAP-2 is controlled by E3 ubiquitin ligase Cbl

Yuichi Sekine, Chikako Yamamoto, Osamu Ikeda, Ryuta Muromoto, Asuka Nanbo, Kenji Oritani, Akihiko Yoshimura, Tadashi Matsuda

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


Signal transducing adaptor protein-2 (STAP-2) is a recently identified adaptor protein that contains pleckstrin and Src homology 2 (SH2)-like domains as well as a YXXQ motif in its C-terminal region. Our previous study in T cells demonstrated that STAP-2 influences FAK protein levels through recruitment of E3 ubiquitin ligase, Cbl, to FAK. In the present study, we found that Cbl directly controls the protein levels and activity of STAP-2. STAP-2 physically interacted with Cbl through its PH and SH2-like domains. Small-interfering RNA-mediated reduction of endogenous Cbl restored STAP-2 protein levels. In contrast, over-expression of Cbl induced STAP-2 degradation. Importantly, Cbl-mediated regulation of STAP-2 protein levels affected Brk/STAP-2-induced STAT3 activation. These results indicate that Cbl regulates STAP-2 protein levels and Brk/STAP-2-mediated STAT3 activation.

Original languageEnglish
Pages (from-to)187-192
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 2009 Jun 26


  • Cbl
  • Protein degradation
  • STAP-2

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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