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The N‐terminal acidic residue of the cytosolic helix 8 of an odorant receptor is responsible for different response dynamics via G‐protein
Author(s) -
Kawasaki Takashi,
Saka Takahiro,
Mine Shouhei,
Mizohata Eiichi,
Inoue Tsuyoshi,
Matsumura Hiroyoshi,
Sato Takaaki
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.03.025
Subject(s) - cytosol , helix (gastropod) , residue (chemistry) , chemistry , biochemistry , receptor , point mutation , stereochemistry , biophysics , mutation , biology , enzyme , gene , ecology , snail
We previously observed highly rapid and robust response of murine olfactory receptor S6 (mOR‐S6) with chimeric Gα 15_olf , compared to Gα 15 . To identify residues responsible for this difference in response, mutations of the cytosolic helix 8 were analyzed in a heterologous functional expression system. The N‐terminal hydrophobic core between helix 8 and TM1–2 of mOR‐S6 is important for activation of both Gα 15_olf and Gα 15 . Point mutation of a helix 8 N‐terminal acidic residue eliminated the differences in response dynamics via Gα. This result suggests that an N‐terminal acidic residue of helix 8 is responsible for rapid response via Gα 15_olf .