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• W2023183933 abstract "GTPases of Immunity-Associated Proteins (GIMAPs) are a family of guanine nucleotide binding (G) proteins which are implicated in the regulation of apoptosis in lymphocytes. GIMAPs are composed of an amino-terminal G domain and carboxy-terminal extensions of varying size. Our recent biochemical and structural analysis of a representative GIMAP family member, GIMAP2, revealed the molecular basis of GTP-dependent oligomerization which involves two interfaces in the G domain. Whereas the amphipathic helix α7 in the C-terminal extension closely folds against the G domain in the GDP-bound state, it might be released in the GTP-bound state to assemble interaction partners. We also showed that the GIMAP2 oligomer functions at the surface of lipid droplets in a Jurkat T cell line. Here, we review our recent work and discuss the GIMAP2 oligomer as a GTP-dependent protein scaffold at the surface of lipid droplets controlling apoptosis." @default.
• W2023183933 created "2016-06-24" @default.
• W2023183933 creator A5059679748 @default.
• W2023183933 creator A5061323368 @default.
• W2023183933 date "2011-01-01" @default.
• W2023183933 modified "2023-09-27" @default.
• W2023183933 title "GTP-dependent scaffold formation in the GTPase of Immunity-Associated Protein family" @default.
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• W2023183933 doi "https://doi.org/10.4161/sgtp.2.1.14938" @default.
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