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5NBT

Apo structure of p60N/p80C katanin

Summary for 5NBT
Entry DOI10.2210/pdb5nbt/pdb
DescriptorKatanin p80 WD40 repeat-containing subunit B1, Katanin p60 ATPase-containing subunit A1 (3 entities in total)
Functional Keywordskatanin, severing enzyme, microtubule, cytoskeleton, hydrolase
Biological sourceMus musculus (Mouse)
More
Cellular locationCytoplasm : Q8BG40 Q9WV86
Total number of polymer chains4
Total formula weight65740.05
Authors
Jiang, K.,Rezabkova, L.,Hua, S.,Liu, Q.,Capitani, G.,Altelaar, A.F.M.,Heck, A.J.R.,Kammerer, R.A.,Steinmetz, M.O.,Akhmanova, A. (deposition date: 2017-03-02, release date: 2017-04-26, Last modification date: 2024-05-08)
Primary citationJiang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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