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

Wen Jie Lin, Chih Yung Yang, Ying Chih Lin, Meng Chun Tsai, Chu Wen Yang, Chien Yi Tung, Pei Yun Ho, Fu Jen Kao, Chi Hung Lin*


研究成果: Article同行評審

12 引文 斯高帕斯(Scopus)


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-containing lipid associated protein, called Phafin2, is preferentially expressed in the human hepatocellular carcinoma (HCC) and is involved in the biogenesis of endosomes. Over-expression of Phafin2 or its FYVE domain results in the formation of enlarged endosomes that are still functional for endocytosis; the biogenesis of such abnormal organelles is mediated by phosphoinositide 3-kinases (PI3K) and Rab5 signaling. Using fluorescence resonance energy transfer measured by fluorescence lifetime imaging microscopy (FLIM-FRET), we further demonstrate in live cells that Phafin2 can directly activate Rab5. By modulating the receptor internalization/recycling and Rab5 activation, Phafin2 affects the density of membranous insulin receptors, and regulates the transcriptional activity of AP-1 that is downstream of the insulin signaling pathway. These results provide a vivid example that an endosome modulator, such as Phafin2, may control the cells' responses to the extracellular cues.

頁(從 - 到)1043-1048
期刊Biochemical and Biophysical Research Communications
出版狀態Published - 1 1月 2010


深入研究「Phafin2 modulates the structure and function of endosomes by a Rab5-dependent mechanism」主題。共同形成了獨特的指紋。