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- W1587799008 abstract "Publisher Summary This chapter discusses the biological significance of a particular type of prenylation that has been pursued by in vitro and in vivo analyses. Protein prenylation is a type of posttranslational lipid modification by either 15-carbon farnesyl or 20-carbon geranylgeranyl, which are found in signaling proteins such as G proteins. Farnesylation has a smaller and specific repertoire of modified proteins, when compared with geranylgeranylation. Farnesylation of transducin is interchangeable with geranylgeranylation as for transducin activity in vitro, while geranylgeranylated Gtγ augmented interaction of Gtβγ with Gtα and enhanced the rate of guanosine-5′-triphosphate (GTP)-binding reaction to Gtα. The farnesyl-to-geranylgeranyl replacement in transducin provides unequivocally a new role of lipid modification in proteins. The selective farnesylation of Gtγ provides Gtβγ with a proper (sufficient but not excessive) membrane affinity, allowing Gtβγ to (1) stay with Gtα in the outer segment in the dark and (2) translocate to the inner region during light adaptation for modulation of light sensitivity. Membrane anchoring of the prenylated proteins is important for effective signal transduction by accumulating relevant proteins at the membrane surface. Geranylgeranylation is more advantageous because of its higher membrane affinity compared with farnesylation. As a consequence of such evolutionary advantage, most of the G proteins may adopt geranylgeranylation for their membrane localization." @default.
- W1587799008 created "2016-06-24" @default.
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- W1587799008 date "2011-01-01" @default.
- W1587799008 modified "2023-10-13" @default.
- W1587799008 title "Farnesylation Versus Geranylgeranylation in G-Protein-Mediated Light Signaling" @default.
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- W1587799008 doi "https://doi.org/10.1016/b978-0-12-381339-8.00007-x" @default.
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