Farnesylation of the SNARE Protein Ykt6 Increases Its Stability and Helical Folding

Mechanisms of Membrane Binding of Small GTPase K-Ras4B Farnesylated Hypervariable Region

“…Prenylation is a relatively common modification affecting as many as 0.5% of all cellular proteins (57), including central players in signal transduction (58), cellular trafficking (59), cytoskeletal function (60), regulation of cell growth and polarity (61), viral replication (62), and protein folding (63). Farnesylated proteins are frequently involved in pathogenesis of common human diseases.…”

The Type I Hsp40 Ydj1 Utilizes a Farnesyl Moiety and Zinc Finger-like Region to Suppress Prion Toxicity

“…The simplest mechanism for farnesyl action in Hsp40 chaperone function is interaction between the farnesyl chain and hydrophobic surfaces of protein folding intermediates. However, the farnesyl moiety of Ydj1 could also influence the conformation of Ydj1 and thereby regulate its substrate specificity (52).…”

Structure and function of longin SNAREs

“…Farnesylation is irreversible and occurs after Ykt6 translation. Surprisingly, this addition does not anchor Ykt6 into membranes, and X-ray crystallography experiments have demonstrated that, following farnesylation, Ykt6 switches from a semi-closed to a predominantly closed and fusion-inactive conformation (Pylypenko et al, 2008;Wen et al, 2010). This traps the lipid molecule inside a hydrophobic pocket that is formed by the interface between the longin domain and the coiled-coil domain, and thus inhibits membrane insertion of Ykt6.…”