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Æü»þ: 2013-04-19 10:00 - 11:30
¾ì½ê: 4¹æ´Û2³¬Îعּ¼1
²ñµÄ̾: ʪ¹½¸¦ÃÌÏòñ¡Ê13-04¡ËThe regulation of endosomal protein trafficking and autophagy by N-terminalatypical LIR of TBC1D5
Ï¢ÍíÀè: ÀîºêÀ¯¿Í4347
¹Ö±é¼Ô: °¤µ×ÄÅÀ¿¿Í¡¡»á  (Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt)
¥¢¥Ö¥¹¥È¥é¥¯¥È: Autophagy is important for cytosolic quality control. The LC3 is known as a marker protein of autophagosomal membranes. Autophagy adaptor proteins bring ubiquitinated substrates to autophagosomes by binding to LC3 through its LC3 interacting region (LIR), thereby regulating selective autophagy. We recently reported TBC1D5 as a potential autophagy adaptor protein. TBC1D5 contains two LIRs. The N-terminal LIR of TBC1D5 (which interacts with LC3) can also bind to VPS29, another component of the Retromer complex (VPS29, VPS26 and VPS35) that regulates the recycling of receptor proteins from the endosome to the trans-Golgi network. Therefore, this atypical N-terminal LIR, together with the C-terminal LIR of TBC1D5 could bridge the trafficking events between the endosome and autophagosome. We studied the structures of this N-terminal atypical LIR of TBC1D5 and its recognition mechanisms to VPS29 and LC3. In this seminar, I would like to talk about the molecular basis for this unique binding of TBC1D5 to Retromer complex.

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