A Common Substrate Recognition Mode Conserved between Katanin p60 and VPS4 Governs Microtubule Severing and Membrane Skeleton Reorganization

Katanin p60 (kp60), a microtubule-severing enzyme, plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. We show that a single domain isolated from the N terminus of mouse katanin p60 (kp60-NTD) binds to tubulin. The solution structure of kp60-NTD...

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Published in:The Journal of biological chemistry 2010-05, Vol.285 (22), p.16822-16829
Main Authors: Iwaya, Naoko, Kuwahara, Yohta, Fujiwara, Yoshie, Goda, Natsuko, Tenno, Takeshi, Akiyama, Kohei, Mase, Shogo, Tochio, Hidehito, Ikegami, Takahisa, Shirakawa, Masahiro, Hiroaki, Hidekazu
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - chemistry
Amino Acid Sequence
Animals
ATPases
ATPases Associated with Diverse Cellular Activities
Cell Membrane - metabolism
Cytoskeleton
Endosomal Sorting Complexes Required for Transport - chemistry
Endosomes
Endosomes - metabolism
Humans
Katanin
Magnetic Resonance Spectroscopy
Membrane Biology
Membrane Trafficking
Mice
Microtubules
Microtubules - metabolism
Molecular Sequence Data
Mutation
Protein Structure and Folding
Protein Structure, Tertiary
Sequence Homology, Amino Acid
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Summary:Katanin p60 (kp60), a microtubule-severing enzyme, plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner. We show that a single domain isolated from the N terminus of mouse katanin p60 (kp60-NTD) binds to tubulin. The solution structure of kp60-NTD was determined by NMR. Although their sequence similarities were as low as 20%, the structure of kp60-NTD revealed a striking similarity to those of the microtubule interacting and trafficking (MIT) domains, which adopt anti-parallel three-stranded helix bundle. In particular, the arrangement of helices 2 and 3 is well conserved between kp60-NTD and the MIT domain from Vps4, which is a homologous protein that promotes disassembly of the endosomal sorting complexes required for transport III membrane skeleton complex. Mutation studies revealed that the positively charged surface formed by helices 2 and 3 binds tubulin. This binding mode resembles the interaction between the MIT domain of Vps4 and Vps2/CHMP1a, a component of endosomal sorting complexes required for transport III. Our results show that both the molecular architecture and the binding modes are conserved between two AAA-ATPases, kp60 and Vps4. A common mechanism is evolutionarily conserved between two distinct cellular events, one that drives microtubule severing and the other involving membrane skeletal reorganization.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M110.108365