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Myristoylation and its role in conformational changes associated with Galphai subunit activation
Author(s) -
Preininger Anita M.,
Meier Scott M,
Funk Michael A,
Busenlehner Laura S,
Armstrong Richard N,
Iverson Tina M.,
Hamm Heidi E
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.879.9
Subject(s) - heterotrimeric g protein , myristoylation , g protein , protein subunit , g protein coupled receptor , chemistry , g alpha subunit , context (archaeology) , microbiology and biotechnology , gi alpha subunit , transmembrane domain , biophysics , biochemistry , biology , signal transduction , receptor , membrane , paleontology , gene
G‐protein signaling from 7‐transmembrane GPCRs controls a vast array of physiological responses from external stimulii. While much is known about the structure and function of individual Galpha and Gbeta‐gamma subunits, as well as heterotrimeric G proteins, the majority of the structural information collected to date on Galpha subunits has been obtained using unmyristoylated Galpha proteins. Since the alpha subunits of Gi family members are irreversibly myristoylated in vivo at the amino terminus, and since myristoylation of Galphai subunits is not sufficient to tether activated subunits to cell membranes in vitro , new insights may be gained by studying the structure and function of these subunits in the context of the myristoylated form of the protein. Using a combination of structural and biochemical approaches, we probe the effects of myristoylation on the conformation of Galpha subunits to reveal new insights into processes associated with G‐protein activation. This work supported by: TMI, NARSAD; HEH, NIH Grant EY06062.