The C-terminal ¦Á-helix of SPAS-1, a Caenorhabditis elegans spastin homologue, is crucial for microtubule severing

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• 作者：Akinobu Onitake ; Yuka Matsushita-Ishiodori ; Ai Johjima ; Masatoshi Esaki ; Teru Ogura ; Kunitoshi Yamanaka
• 关键词：AAA ATPase ; Caenorhabditis elegans ; Chaperone ; Hereditary spastic paraplegia ; Microtubule ; Spastin
• 刊名：Journal of Structural Biology
• 出版年：2012
• 出版时间：August, 2012
• 年：2012
• 卷：179
• 期：2
• 页码：138-142
• 全文大小：632 K

文摘

Spastin belongs to the meiotic subfamily, together with Vps4/SKD1, fidgetin and katanin, of AAA (ATPases associated with diverse cellular activities) proteins, and functions in microtubule severing. Interestingly, all members of this subgroup specifically contain an additional ¦Á-helix at the very C-terminal end. To understand the function of the C-terminal ¦Á-helix, we characterised its deletion mutants of SPAS-1, a Caenorhabditis elegans spastin homologue, in vitro and in vivo. We found that the C-terminal ¦Á-helix plays essential roles in ATP binding, ATP hydrolysing and microtubule severing activities. It is likely that the C-terminal ¦Á-helix is required for cellular functions of members of meiotic subgroup of AAA proteins, since the C-terminal ¦Á-helix of Vps4 is also important for assembly, ATPase activity and in vivo function mediated by ESCRT-III complexes.