N-linked glycosylation of the mGlu7 receptor regulates the forward trafficking and transsynaptic interaction with Elfn1
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F20%3A00535045" target="_blank" >RIV/67985823:_____/20:00535045 - isvavai.cz</a>
Alternative codes found
RIV/68378041:_____/20:00538742
Result on the web
<a href="https://doi.org/10.1096/fj.202001544R" target="_blank" >https://doi.org/10.1096/fj.202001544R</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1096/fj.202001544R" target="_blank" >10.1096/fj.202001544R</a>
Alternative languages
Result language
angličtina
Original language name
N-linked glycosylation of the mGlu7 receptor regulates the forward trafficking and transsynaptic interaction with Elfn1
Original language description
Metabotropic glutamate receptor 7 (mGlu7) regulates neurotransmitter release at the presynaptic active zone in the mammalian brain. The regulation of mGlu7 trafficking into and out of the plasma membrane by binding proteins within the C-terminal region of mGlu7 governs the bidirectional synaptic plasticity. However, the functional importance of the extracellular domain of mGlu7 has not yet been characterized. N-glycosylation is an abundant posttranslational modification that plays crucial roles in protein folding and forward trafficking, but the role of N-glycosylation in mGlu7 function remains unknown. In this study, we find that mGlu7 is N-glycosylated at four asparagine residues in heterologous cells and rat cultured neurons. We demonstrate that N-glycosylation is essential for forward transport and surface expression of mGlu7. Deglycosylated mGlu7 is retained in the ER, obstructing expression on the cell surface, and is degraded through the autophagolysosomal degradation pathway. In addition, we identify the binding domain of mGlu7 to Elfn1, a transsynaptic adhesion protein. We find that N-glycosylation of mGlu7 promotes its interaction with Elfn1, thereby enabling proper localization and stable surface expression of mGlu7 at the presynaptic active zone. These findings provide evidence that N-glycans act to modulate the surface expression, stability, and function of mGlu7.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30103 - Neurosciences (including psychophysiology)
Result continuities
Project
<a href="/en/project/GA18-04329S" target="_blank" >GA18-04329S: Regulation of trafficking and function of the GluN3A-containing NMDA receptors in the mammalian neurons</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FASEB Journal
ISSN
0892-6638
e-ISSN
—
Volume of the periodical
34
Issue of the periodical within the volume
11
Country of publishing house
US - UNITED STATES
Number of pages
20
Pages from-to
14977-14996
UT code for WoS article
000570777800001
EID of the result in the Scopus database
2-s2.0-85090983760