Research

Hormonal

GLP-1 receptor internalization is arrestin-independent and relies on a dual mechanism involving Gs/Gi/o protein activation, GRK phosphorylation, and both clathrin- and caveolae-mediated endocytosis.

This research clarifies that GLP-1 drugs work by engaging specific cellular recycling pathways (clathrin and caveolae) rather than the arrestin pathway. This mechanistic insight aids in designing drugs with optimized duration and fewer side effects, though it does not change immediate patient behavior.

GoodSupportsHIGH confidence
Our findings indicate that the receptor internalizes independently of arrestin and is dependent on Gs and Gi/o activation and G protein–coupled receptor kinase phosphorylation. Mechanistically, we observed that clathrin- and caveolae-mediated internalization in HEK293 cells.
Ee Von Moo et al. · FEBS Journal · 2025

Why this rating

High-quality in vitro mechanistic study using CRISPR/Cas9 knockout lines and TR-FRET assays, though limited to HEK293 cells.

Source

Arrestin‐independent internalization of the <scp>GLP</scp> ‐1 receptor is facilitated by a <scp>GRK</scp> , clathrin, and caveolae‐dependent mechanism

Ee Von Moo et al. · FEBS Journal · 2025

DOI 10.1111/febs.17338

mechanism_onlyCited 14×
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DOI resolved against Crossref · corpus check 2026-06-10

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