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Multiple Sgip1 splice variants inhibit cannabinoid receptor 1 internalization
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SYSNO ASEP 0579881 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Multiple Sgip1 splice variants inhibit cannabinoid receptor 1 internalization Author(s) Durydivka, Oleh (UMG-J)
Gazdarica, Matej (UMG-J)
Večerková, Kateřina (UMG-J)
Radenkovic, Silvia (UMG-J)
Blahoš, Jaroslav (UMG-J) RIDNumber of authors 5 Article number 147851 Source Title Gene. - : Elsevier - ISSN 0378-1119
Roč. 892, Jan (2024)Number of pages 16 s. Language eng - English Country NL - Netherlands Keywords amino-acid-composition ; protein-phosphorylation ; platform ; association ; enrichment ; domain ; Alternative splicing ; Cannabinoid receptor ; Clathrin-mediated endocytosis ; Isoform ; Molecular cloning ; RNA OECD category Cell biology R&D Projects GA19-24172S GA ČR - Czech Science Foundation (CSF) GA21-02371S GA ČR - Czech Science Foundation (CSF) LM2023050 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2023036 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) EF18_046/0015861 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support UMG-J - RVO:68378050 UT WOS 001098807000001 EID SCOPUS 85173311361 DOI 10.1016/j.gene.2023.147851 Annotation Alternative splicing can often result in the expression of distinct protein isoforms from a single gene, with specific composition and properties. SH3-containing GRB2-like protein 3-interacting protein 1 (Sgip1) is a brain-enriched protein that regulates clathrin-mediated endocytosis and interferes with the internalization of cannabinoid receptor 1. Several research groups have studied the physiological importance of Sgip1, and four Sgip1 protein isoforms have been described to date, while the NCBI Gene database predicts the expression of 20 splice variants from the Sgip1 gene in mice. In this work, we cloned 15 Sgip1 splice variants from the mouse brain, including 11 novel splice variants. The cloned splice variants differed in exon composition within two Sgip1 regions: the membrane phospholipid-binding domain and the proline-rich region. All the Sgip1 splice isoforms had similar stability and comparable ability to inhibit the internalization of cannabinoid receptor 1. None of the isoforms influenced the internalization of the mu-opioid receptor. We confirm the expression of Sgip1 splice variants described in previous studies or predicted in silico. Our data provide a basis for further studies exploring the significance of Sgip1 splicing, and we suggest a new classification of Sgip1 splice variants to unify their nomenclature. Workplace Institute of Molecular Genetics Contact Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Year of Publishing 2025 Electronic address https://www.sciencedirect.com/science/article/pii/S0378111923006923?via%3Dihub
Number of the records: 1