5OW5

p60p80-CAMSAP complex

5OW5 の概要

• エントリーDOI: 10.2210/pdb5ow5/pdb
• 分子名称: Katanin p80 WD40 repeat-containing subunit B1, Katanin p60 ATPase-containing subunit A1, Calmodulin-regulated spectrin-associated protein, ... (6 entities in total)
• 機能のキーワード: katanin, camsap, severing enzyme, microtubule, cytoskeleton, hydrolase
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 68246.93

構造登録者

Rezabkova, L.,Capitani, G.,Prota, A.E.,Kammerer, R.A.,Steinmetz, M.O. (登録日: 2017-08-30, 公開日: 2018-07-11, 最終更新日: 2024-01-17)

主引用文献

Jiang, K.,Faltova, L.,Hua, S.,Capitani, G.,Prota, A.E.,Landgraf, C.,Volkmer, R.,Kammerer, R.A.,Steinmetz, M.O.,Akhmanova, A.
Structural Basis of Formation of the Microtubule Minus-End-Regulating CAMSAP-Katanin Complex.
Structure, 26:375-382.e4, 2018

PubMed Abstract: CAMSAP/Patronin family members regulate the organization and stability of microtubule minus ends in various systems ranging from mitotic spindles to differentiated epithelial cells and neurons. Mammalian CAMSAP2 and CAMSAP3 bind to growing microtubule minus ends, where they form stretches of stabilized microtubule lattice. The microtubule-severing ATPase katanin interacts with CAMSAPs and limits the length of CAMSAP-decorated microtubule stretches. Here, by using biochemical, biophysical, and structural approaches, we reveal that a short helical motif conserved in CAMSAP2 and CAMSAP3 binds to the heterodimer formed by the N- and C-terminal domains of katanin subunits p60 and p80, respectively. The identified CAMSAP-katanin binding mode is supported by mutational analysis and genome-editing experiments. It is strikingly similar to the one seen in the ASPM-katanin complex, which is responsible for microtubule minus-end regulation in mitotic spindles. Our work provides a general molecular mechanism for the cooperation of katanin with major microtubule minus-end regulators.

PubMed: 29395789
DOI: 10.1016/j.str.2017.12.017

実験手法

X-RAY DIFFRACTION (1.7 Å)