Matsuda et al. 2004 — N-linked glycosylation sites of prestin
Full citation: Matsuda K, Zheng J, Du GG, Klöcker N, Madison LD, Dallos P. “N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.” J Neurochem. 2004 May;89(4):928-38. PMID 15140192.
Numbers that matter
| Finding | Value | Notes |
|---|---|---|
| N-glycosylation sites | N163 and N166 | Confirmed by site-directed mutagenesis N→Q |
| N166 vs N163 glycosylation extent | N166 greater glycosylation | Differential programs for synthesis and trimming |
| Effect of N163/N166 removal | Affects membrane targeting | Reduced prestin at plasma membrane |
| Electrophysiological impact | Reduced NLC (nonlinear capacitance) | Prestin’s voltage-dependent motor function impaired |
Usage in STRC vault
- Cited in STRC Engineered TECTA Chimera (h11) as a primary source for “prestin glycans OHC-restricted.” This paper confirms N163/N166 as the glycosylation sites. ✅
- Note: PMID 15140192 confirmed real (PubMed lookup 2026-04-25). ✅
- The companion paper for glycan functional significance is 2010-rajagopalan-prestin-glycosylation-jaro.
Connections
[applies]STRC Engineered TECTA Chimera (h11)[see-also]2010-rajagopalan-prestin-glycosylation-jaro[source]STRC h10 h11 Parameter Provenance Audit 2026-04-23