Secretory Carrier Membrane Proteins (SCAMPs) are transmembrane proteins that function in the plasma membrane, endosomes, and trans-Golgi network. Here we show that SCAMP 3 is a novel regulator of endosomal morphology and composition. Under certain nutrient-starved conditions, SCAMP 3 concentrates in enlarged early endosomes. The enlarged contain ubiquitylated and non-ubiquitylated SCAMP 3 as well as other SCAMPs, EEA1, and the ESCRT-0 protein Hrs. We demonstrate that SCAMP 3 is sufficient to recruit Hrs to the enlarged endosomes. Taken together, our results suggest a novel role for SCAMP 3 in modifying endosome structure through interactions that involve its ubiquitylation and ESCRT proteins.
Keywords: ESCRT; Endosome; SCAMP; Ubiquitin.
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