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Coupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3.

Abstract：

:Activation of the protein tyrosine kinase receptors requires the coupling of ligand binding to a change in both the proximity and orientation of the single transmembrane (TM) helices of receptor monomers to allow transphosphorylation of the receptor kinase domain. We make use of peptides corresponding to the TM and juxtamembrane (JM) regions of the fibroblast growth factor receptor 3 to assess how mutations in the TM region (G380R and A391E), which lead to receptor activation, influence the orientation of the TM domain and interactions of the intracellular JM sequence with the membrane surface. On the basis of fluorescence and Fourier transform infrared spectroscopy, we find that both activating mutations change the TM helix tilt angle relative to the membrane normal and release the JM region from the membrane. These results suggest a general mechanism regarding how the TM-JM region functionally bridges the extracellular and intracellular regions for these receptors.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Tamagaki H,Furukawa Y,Yamaguchi R,Hojo H,Aimoto S,Smith SO,Sato T

doi

10.1021/bi500327q

subject

Has Abstract

pub_date

2014-08-05 00:00:00

pages

5000-7

issue

30

eissn

0006-2960

issn

1520-4995

journal_volume

53

pub_type

杂志文章

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