{'fraction_non_alphanumeric': 0.02564102564102564, 'fraction_numerical': 0.01237842617152962, 'mean_word_length': 6.1645569620253164, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Distinct Clathrin‐Coated Pits Sort Different G Protein‐Coupled Receptor Cargo

Upon activation, many G protein‐coupled receptors (GPCRs) internalize by clathrin‐mediated endocytosis and are subsequently sorted to undergo recycling or lysosomal degradation. Here we observe that sorting can take place much earlier than previously thought, by entry of different GPCRs into distinct populations of clathrin‐coated pit (CCP). These distinct populations were revealed by analysis of two purinergic GPCRs, P2Y1 and P2Y12, which enter two populations of CCPs in a mutually exclusive manner. The mechanisms underlying early GPCR sorting involve differential kinase‐dependent processes because internalization of P2Y12 is mediated by GPCR kinases (GRKs) and arrestin, whereas P2Y1 internalization is GRK‐ and arrestin‐independent but requires protein kinase C. Importantly, the β2 adrenoceptor which also internalizes in a GRK‐dependent manner also traffics exclusively to P2Y12‐containing CCPs. Our data therefore reveal distinct populations of CCPs that sort GPCR cargo at the plasma membrane using different kinase‐dependent mechanisms.