5LB7

Complex structure between p60N/p80C katanin and a peptide derived from ASPM

5LB7 の概要

• エントリーDOI: 10.2210/pdb5lb7/pdb
• 分子名称: Katanin p80 WD40 repeat-containing subunit B1, Katanin p60 ATPase-containing subunit A1, Abnormal spindle-like microcephaly-associated protein homolog, ... (4 entities in total)
• 機能のキーワード: katanin, aspm, severing enzyme, hydrolase
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 33893.12

構造登録者

Rezabkova, L.,Capitani, G.,Kammerer, R.A.,Steinmetz, M.O. (登録日: 2016-06-15, 公開日: 2017-04-26, 最終更新日: 2024-05-08)

主引用文献

Jiang, K.,Rezabkova, L.,Hua, S.,Liu, Q.,Capitani, G.,Maarten Altelaar, A.F.,Heck, A.J.R.,Kammerer, R.A.,Steinmetz, M.O.,Akhmanova, A.
Microtubule minus-end regulation at spindle poles by an ASPM-katanin complex.
Nat. Cell Biol., 19:480-492, 2017

PubMed Abstract: ASPM (known as Asp in fly and ASPM-1 in worm) is a microcephaly-associated protein family that regulates spindle architecture, but the underlying mechanism is poorly understood. Here, we show that ASPM forms a complex with another protein linked to microcephaly, the microtubule-severing ATPase katanin. ASPM and katanin localize to spindle poles in a mutually dependent manner and regulate spindle flux. X-ray crystallography revealed that the heterodimer formed by the N- and C-terminal domains of the katanin subunits p60 and p80, respectively, binds conserved motifs in ASPM. Reconstitution experiments demonstrated that ASPM autonomously tracks growing microtubule minus ends and inhibits their growth, while katanin decorates and bends both ends of dynamic microtubules and potentiates the minus-end blocking activity of ASPM. ASPM also binds along microtubules, recruits katanin and promotes katanin-mediated severing of dynamic microtubules. We propose that the ASPM-katanin complex controls microtubule disassembly at spindle poles and that misregulation of this process can lead to microcephaly.

PubMed: 28436967
DOI: 10.1038/ncb3511

実験手法

X-RAY DIFFRACTION (1.5 Å)