Phafin2 modulates the structure and function of endosomes by a Rab5-dependent mechanism

By regulating the amount of protein receptors on the cell membrane and the metabolisms of receptor-bound ligands, endocytosis represents one of the fundamental biological activities that regulate how cells respond to the environment. We report here that a Fab1–YotB–Vac1p–EEA1 (FYVE) domain-containin...

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Veröffentlicht in:	Biochemical and biophysical research communications 2010-01, Vol.391 (1), p.1043-1048
Hauptverfasser:	Lin, Wen-Jie, Yang, Chih-Yung, Lin, Ying-Chih, Tsai, Meng-Chun, Yang, Chu-Wen, Tung, Chien-Yi, Ho, Pei-Yun, Kao, Fu-Jen, Lin, Chi-Hung
Format:	Artikel
Sprache:	eng
Schlagworte:	Cell Line, Tumor Endocytosis Endosome Endosomes - metabolism Endosomes - ultrastructure FLIM FYVE domain Humans Phafin2 Phosphatidylinositol 3-Kinases - metabolism Rab5 rab5 GTP-Binding Proteins - genetics rab5 GTP-Binding Proteins - metabolism Receptor, Insulin - metabolism Signal Transduction Transcription Factor AP-1 - metabolism Vesicular Transport Proteins - genetics Vesicular Transport Proteins - metabolism
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