ArticleJournal of the Association for Research in Otolaryngology : JARO2010
Glycosylation regulates prestin cellular activity.
Article in Journal of the Association for Research in Otolaryngology : JARO, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- The Challenges to Advancing Induced Pluripotent Stem Cell-Dependent Cell Replacement Therapy.Medical research archives · 2023Article
- A novel theoretical framework reveals more than one voltage-sensing pathway in the lateral membrane of outer hair cells.The Journal of general physiology · 2020Article
- Prestin kinetics and corresponding frequency dependence augment during early development of the outer hair cell within the mouse organ of Corti.Scientific reports · 2019Article
- The susceptibility of cochlear outer hair cells to cyclodextrin is not related to their electromotile activity.Acta neuropathologica communications · 2018Article
- The role of post-translational modifications in hearing and deafness.Cellular and molecular life sciences : CMLS · 2016Review
- Membrane prestin expression correlates with the magnitude of prestin-associated charge movement.Hearing research · 2016Article
- Susceptibility of outer hair cells to cholesterol chelator 2-hydroxypropyl-β-cyclodextrine is prestin-dependent.Scientific reports · 2016Article
- Localization and proteomic characterization of cholesterol-rich membrane microdomains in the inner ear.Journal of proteomics · 2014Article
- Effects of cholesterol alterations are mediated via G-protein-related pathways in outer hair cells.Pflugers Archiv : European journal of physiology · 2013Article
- Prestin regulation and function in residual outer hair cells after noise-induced hearing loss.PloS one · 2013Article
- Membrane cholesterol strongly influences confined diffusion of prestin.Biophysical journal · 2012Article
- A motif of eleven amino acids is a structural adaptation that facilitates motor capability of eutherian prestin.Journal of cell science · 2012Article
- KCNE1 and KCNE2 inhibit forward trafficking of homomeric N-type voltage-gated potassium channels.Biophysical journal · 2011Article
- Selective cell-surface labeling of the molecular motor protein prestin.Biochemical and biophysical research communications · 2011Article
- Membrane cholesterol modulates cochlear electromechanics.Pflugers Archiv : European journal of physiology · 2011Article
- Plasticity in membrane cholesterol contributes toward electrical maturation of hearing.The Journal of biological chemistry · 2011Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling. The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction. Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells. 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. In addition, unlike WT prestin that readily forms oligomers, prestin(NN163/166AA) is enriched as monomers and more mobile in the plasma membrane, suggesting that oligomerization of prestin is dependent on glycosylation but is not essential for the generation of NLC in HEK 293 cells. However, in the presence of increased membrane cholesterol, unlike the hyperpolarizing shift in NLC seen with WT prestin, cells expressing prestin(NN163/166AA) exhibit a linear capacitance function. In an attempt to explain this finding, we discovered that both WT prestin and prestin(NN163/166AA) participate in cholesterol-dependent cellular trafficking. 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. Based on our observations, we conclude that glycosylation regulates self-association and cellular trafficking of prestin(NN163/166AA). These observations are the first to implicate a regulatory role for cellular trafficking and sorting in prestin function. We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms.
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Registered trials
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