TAILIEUCHUNG - Báo cáo khoa học: Autolytic activity of human calpain 7 is enhanced by ESCRT-III-related protein IST1 through MIT–MIM interaction

Calpain 7, a mammalian ortholog of yeast Cpl1⁄Rim13 and fungal PalB, is an atypical calpain that lacks a penta-EF-hand domain. Previously, we reported that a region containing a tandem repeat of microtubule-interact-ing and transport (MIT) domains in calpain 7 interacts with a subset of endosomal sorting complex required for transport (ESCRT)-III-related proteins, suggesting involvement of calpain 7 in the ESCRT system. | ễFEBS Journal Autolytic activity of human calpain 7 is enhanced by ESCRT-III-related protein IST1 through MIT-MIM interaction Yohei Osako Yuki Maemoto Ryohei Tanaka Hironori Suzuki Hideki Shibata and Masatoshi Maki Department of Applied Molecular Biosciences Graduate Schoolof BioagriculturalSciences Nagoya University Japan Keywords calpain 7 ESCRT-III IST1 microtubuleinteracting and transport MIT proteolysis Correspondence M. Maki Department of Applied Molecular Biosciences Graduate School of BioagriculturalSciences Nagoya University Furo-cho Chikusa-ku Nagoya 464-8601 Japan Fax 81 52 789 5542 Tel 81 52 789 4088 E-mail mmaki@ Received 10 May 2010 revised 21 July 2010 accepted 20 August 2010 doi Calpain 7 a mammalian ortholog of yeast Cpl1 Rim13 and fungal PalB is an atypical calpain that lacks a penta-EF-hand domain. Previously we reported that a region containing a tandem repeat of microtubule-interacting and transport MIT domains in calpain 7 interacts with a subset of endosomal sorting complex required for transport ESCRT -III-related proteins suggesting involvement of calpain 7 in the ESCRT system. Although yeast and fungal calpains are thought to be involved in alkaline adaptation via limited proteolysis of specific transcription factors proteolytic activity of calpain 7 has not been demonstrated yet. In this study we investigated the interaction between calpain 7 and a newly reported ESC-RT-III family member increased sodium tolerance-1 IST1 which possesses two different types of MIT-interacting motifs MIM1 and MIM2 . We found that glutathione-S-transferase GST -fused tandem MIT domains of calpain 7 calpain 7MIT pulled down FLAG-tagged IST1 expressed in HEK293T cells. Coimmunoprecipitation assays with various deletion or point mutants of epitope-tagged calpain 7 and IST1 revealed that both repetitive MIT domains and MIMs are required for efficient interaction. Direct MIT-MIM binding was confirmed by a .

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