Title : Glycosylation regulates prestin cellular activity.

Pub. Date : 2010 Mar

PMID : 19898896






5 Functional Relationships(s)
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1 Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model. Cholesterol solute carrier family 26 member 5 Homo sapiens
2 In an attempt to explain this finding, we discovered that both WT prestin and prestin(NN163/166AA) participate in cholesterol-dependent cellular trafficking. Cholesterol solute carrier family 26 member 5 Homo sapiens
3 In an attempt to explain this finding, we discovered that both WT prestin and prestin(NN163/166AA) participate in cholesterol-dependent cellular trafficking. Cholesterol solute carrier family 26 member 5 Homo sapiens
4 In contrast to WT prestin, prestin(NN163/166AA) shows a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function. Cholesterol solute carrier family 26 member 5 Homo sapiens
5 We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms. Cholesterol solute carrier family 26 member 5 Homo sapiens