Rajagopalan et al. 2010 — Glycosylation regulates prestin cellular activity
Full citation: Rajagopalan L, Organ-Darling LE, Liu H, Davidson AL, Raphael RM, Brownell WE, Pereira FA. “Glycosylation regulates prestin cellular activity.” J Assoc Res Otolaryngol. 2010 Mar;11(1):39-51. Epub 2009 Nov 7. PMID 19898896.
Correction note (2026-04-25)
The h11 audit note (STRC h10 h11 Parameter Provenance Audit 2026-04-23.md) cited this work as:
“Zheng et al. 2009 JARO 10:373–383 — ‘Glycosylation regulates prestin cellular activity’”
This is a wrong-author attribution. The actual paper is by Rajagopalan et al., not Zheng. The correct volume and page numbers are JARO 11:39-51, not 10:373-383. The year of publication is formally 2010 (epub November 2009). A “Zheng 2009” prestin glycosylation paper does not appear in PubMed (multiple search attempts 2026-04-25 returned no results).
However: the phantom attribution came via the h11 audit, which replaced the earlier phantom “Song 2021 prestin glycosylation.” The underlying science (prestin glycosylation regulates OHC electromotility) is real and documented in this paper. The citation error is author/year/page, not scientific substance.
Numbers that matter
| Finding | Value | Notes |
|---|---|---|
| N-glycosylation sites in prestin | N163, N166 (also confirmed by Matsuda 2004) | Rajagopalan confirmed both sites regulate activity |
| Effect of N163/N166 removal | Disrupts prestin self-association (oligomerization) | Prestin normally forms homotetramers |
| Prestin membrane trafficking | Impaired when N-glycans removed | Fewer prestin molecules reach PM |
| Link to electromotility | Reduced NLC (nonlinear capacitance) when glycosylation disrupted | Indirect link to OHC somatic electromotility |
Relevance to h11
The STRC Engineered TECTA Chimera hypothesis proposed using prestin N-glycans as an OHC-restricted surface handle to anchor TECTA-EC to OHC stereocilia. The claim: N163/N166 glycans are OHC-specific (prestin is OHC-restricted). This paper confirms glycosylation regulates prestin function but does NOT directly address whether the glycan pattern is accessible/distinguishable from the extracellular side for binding purposes. h11’s Phase 1 AF3 failed on architectural grounds before this specificity question was tested.
Connections
[applies]STRC Engineered TECTA Chimera (h11)[see-also]2004-matsuda-prestin-n-glycosylation (N163/N166 site identification paper)[source]STRC h10 h11 Parameter Provenance Audit 2026-04-23