TY  - JOUR
A1  - Büttner, Cora
A1  - Sadtler, Sven
A1  - Leyendecker, Anne Larissa
A1  - Laube, Bodo
A1  - Griffon, Nathalie
A1  - Betz, Heinrich
A1  - Schmalzing, Günther
T1  - Ubiquitination precedes internalization and proteolytic cleavage of plasma membrane-bound glycine receptors
T2  - The journal of biological chemistry
N2  - The inhibitory glycine receptor (GlyR) in developing spinal neurones is internalized efficiently upon antagonist inhibition. Here we used surface labeling combined with affinity purification to show that homopentameric α1 GlyRs generated inXenopus oocytes are proteolytically nicked into fragments of 35 and 13 kDa upon prolonged incubation. Nicked GlyRs do not exist at the cell surface, indicating that proteolysis occurs exclusively in the endocytotic pathway. Consistent with this interpretation, elevation of the lysosomal pH, but not the proteasome inhibitor lactacystin, prevents GlyR cleavage. Prior to internalization, α1 GlyRs are conjugated extensively with ubiquitin in the plasma membrane. Our results are consistent with ubiquitination regulating the endocytosis and subsequent proteolysis of GlyRs residing in the plasma membrane. Ubiquitin-conjugating enzymes thus may have a crucial role in synaptic plasticity by determining postsynaptic receptor numbers.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/75985
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-759856
SN  - 0021-9258
VL  - 276
IS  - 46
SP  - 42978
EP  - 42985
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -