Molecular characterization of SH3P2 in Autophagy and Endocytosis
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AbstractAutophagy is a fundamental catabolic process for cargo degradation under stress conditions via a double-membrane structure named as autophagosome. Recently, report also suggests that autophagy plays a role in the unconventional secretion of cargo proteins. Our previous study has identified a novel regulator, SH3P2 (SH3 domain-containing protein2), which contains an N-terminus BAR (Bin/Amphiphysin/Rvs) and C-terminus SH3 (Src Homology 3) domain, plays an essential role in plant autophagosome formation. SH3P2 interacts with ATG8, as well as a plant unique ESCRT (Endosomal sorting complex required for transport) component, FREE1 (FYVE domain protein required for endosomal sorting 1), to regulate the fusion between autophagosome and vacuole. In addition, it has been shown that SH3P2 functions with other endocytic components to involve in the clathrin-mediated endocytosis and cell plate formation. However, the molecular mechanism underlying SH3P2 activity for its switch between autophagy and endocytosis remains largely unknown. Here, we aim to use a combination of cellular, molecular, biochemical and genetic approaches to identify the SH3P2 protein complex and to investigate how they are coordinated during autophagy or endocytosis in plant cells. Supported by grants from the Research Grants Council of Hong Kong (C4011-14R, C4012-16E, C4002-17G and AoE/M- 05/12).Reference
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Acceptance Date12/11/2018
All Author(s) ListLanlan Feng, Liwen Jiang, Xiaohong Zhuang
Name of Conference2018 CSHA Meeting on “Biology of Extracellular Vesicles”
Start Date of Conference12/11/2018
End Date of Conference16/11/2018
Place of ConferenceSuzhou, China
Country/Region of ConferenceChina
LanguagesEnglish-United States

Last updated on 2019-04-07 at 10:42