|
KMID : 0613820070170091303
|
|
Journal of Life Science
2007 Volume.17 No. 9 p.1303 ~ p.1307
|
|
|
Interaction of FERM Domain of Tumor Suppressor, Merlin to its C-terminal Domain
|
|
Kang Beom-Sik
Oh Jeong-Il
|
|
|
Abstract
|
|
|
|
A tumor suppressor, merlin is a member of ERM family proteins. It consists of N-terminal FERM domain, α- 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.
|
|
|
KEYWORD
|
|
|
Merlin, ERM, tumor suppressor, isothermal titration calorimetry
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
|
|