Author: Salaun, Christine; Greaves, Jennifer; Chamberlain, Luke H.
Title: The intracellular dynamic of protein palmitoylation Document date: 2010_12_27
ID: svn4e6w6_34
Snippet: Despite Apt1 being identified many years ago, the physiological importance of this protein as a thioesterase is not clear. However, a recent study reported an important function for Apt1 in controlling dendritic spine volume, possibly by regulating palmitoylation and membrane localization of Gî¡ 13 (Siegel et al., 2009 ). The recent description of a novel Apt1 inhibitor (palmostatin B) should provide an important tool to more finely dissect the .....
Document: Despite Apt1 being identified many years ago, the physiological importance of this protein as a thioesterase is not clear. However, a recent study reported an important function for Apt1 in controlling dendritic spine volume, possibly by regulating palmitoylation and membrane localization of Gî¡ 13 (Siegel et al., 2009 ). The recent description of a novel Apt1 inhibitor (palmostatin B) should provide an important tool to more finely dissect the function of this protein in cellular palmitoylation dynamics (Dekker et al., 2010) . Initial analysis with palmostatin B suggests that it promotes a moderate increase in Ras palmitoylation and disrupts the intracellular localization of this protein.
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