TY  - GEN
T1  - Atg27p co-fractionates with clathrin-coated vesicles in budding yeast
AU  - Segarra, Verónica A.
AU  - Sharma, Anupam
AU  - Lemmon, Sandra K.
DO  - 10.17912/micropub.biology.000380
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000380/
AB  - Atg27p is a single-pass transmembrane protein that functions in the process of cellular self-eating or autophagy (Yen et al. 2007, Segarra et al. 2015). Atg27p localizes to a variety of cellular compartments including the pre-autophagosomal structure (PAS), late Golgi, vacuolar membrane, as well as early and late endosomes (Segarra et al. 2015). In fact, its short cytoplasmic C-terminus has been found to contain a tyrosine sorting motif that allows for its anterograde transport to the vacuolar membrane and an additional 15-residue sequence that allows for its retrieval or retrograde transport from the vacuolar membrane to the endosome (Segarra et al. 2015, Suzuki and Emr 2018). Since clathrin is well known to mediate vesicular transport in the endomembrane system, the trafficking itinerary of Atg27p and its tyrosine sorting motif suggested that it might be trafficked inside clathrin-coated vesicles (CCVs).
PY  - 2021
JO  - microPublication Biology
ER  -