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The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

SCAMP5 plays a critical role in axonal trafficking and synaptic localization of NHE6 to adjust quantal size at glutamatergic synapses

Lee, Unghwi, Choi, Chunghon, Ryu, Seung Hyun, Park, Daehun, Lee, Sang-Eun, Kim, Kitae, Kim, Yujin, Chang, Sunghoe·2021·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.2011371118
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Abstract

Significance: As a vesicular Na + (K + )/H + exchanger, NHE6 promotes glutamate filling into synaptic vesicles (SVs). Thus, proper localization of NHE6 is critical for determining synaptic strength at glutamatergic synapses, but the underlying mechanism remains unknown. We found that an SV-enriched protein, SCAMP5, is a key determinant for axonal trafficking and synaptic localization of NHE6. By perturbing their interaction, NHE6 fails to be localized at synaptic sites, resulting in hyperacidification of the SV lumen and a significant reduction in the quantal size of glutamate released. Since both are autism candidate genes, our results suggest that impaired interaction between two proteins could relate to the synaptic dysfunction observed in autism.

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  • NHE6 is ubiquitously expressed in all cells of the body, but in the CNS it is highly expressed in neurons and to a lesser extent in glial cells.

    “NHE6 is ubiquitously expressed in all cells of the body, however, in the CNS it is highly expressed in neurons where abundant synaptic vesicles and neurotransmitter receptors recycle in synapses (Lee et al., 2020; Lee et al., 2021) and to a lesser extent in glial cells (Zhang et al., 2014).”

    From NHE6 depletion corrects ApoE4-mediated synaptic impairments and reduces amyloid plaque load (2021) · cites this paper as Lee et al., 2020

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Metadata

Authors
Lee, U., Choi, C., Ryu, S. H., Park, D., Lee, S.-E., Kim, K., Kim, Y., & Chang, S.
Affiliations
Department of Physiology and Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, South Korea;
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2020-12-28
Volume
118
Issue
2
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.2011371118
Cited by
18
References
5
Language
en
Licence
www.pnas.org/site/aboutpnas/licenses.xhtml (vor, 182 d)
Funders
National Research Foundation of Korea (2019R1A2C2089182, 2017M3C7A1044958)

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