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Interaction of FERM Domain of Tumor Suppressor, Merlin to its C-terminal Domain.

종양 억제 인자, Merlin의 FERM 도메인과 C-말단 도메인간의 결합

  • Oh, Jeong-Il (School of Life Science and Biotechnology, Kyungpook National University) ;
  • Kang, Beom-Sik (Department of Microbiology, Pusan National University)
  • 강범식 (경북대학교 자연과학대학 생명공학부) ;
  • 오정일 (부산대학교 자연과학대학 미생물학과)
  • Published : 2007.09.30

Abstract

A tumor suppressor, merlin is a member of ERM family proteins. It consists of N-terminal FERM domain, ${\alpha}-helical$ region, and C-terminal domain. Alternative splicing of merlin's mRNA generates two isotypes of merlin. Isotype I, which has exon17 at the C-terminus instead of exon16 in isotype II, is known to have tumor suppressor activity. Like other ERM proteins, the C-terminal domain of merlin isotype I interacts to its FERM domain. That of isotype II, however, was reported not to bind FERM domain despite the large common part of C-terminal domain, which possibly binds FERM domain. Here, we show the binding of FERM domain to both C-terminal domains of merlin's two isotypes by isothermal titration calorimetry. These results support that merlin isotype II also can form a closed conformation or a multimer by intramolecular or intermolecular interactions using their FERM domain and C-terminal domain.

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