Abstract：
:Katanin was the first microtubule (MT)-severing enzyme discovered, but how katanin executes MT severing remains poorly understood. Here, we report X-ray crystal structures of the apo and ATPγS-bound states of the catalytic AAA domain of human katanin p60 at 3.0 and 2.9 Å resolution, respectively. Comparison of the two structures reveals conformational changes induced by ATP binding and how such changes ensure hexamer stability. Moreover, we uncover structural details of pore loops (PLs) and show that Arg283, a residue unique to katanin among MT-severing enzymes, protrudes from PL1 and lines the entry of the catalytic pore. Functional studies suggest that PL1 and Arg283 play essential roles in the recognition and remodeling of the glutamylated, C-terminal tubulin tail and regulation of axon growth. In addition, domain-swapping experiments in katanin and spastin suggest that the non-homologous N-terminal region, which contains the MT-interacting and trafficking domain and a linker, confers specificity to the severing process.
journal_name
Cell Repjournal_title
Cell reportsauthors
Shin SC,Im SK,Jang EH,Jin KS,Hur EM,Kim EEdoi
10.1016/j.celrep.2019.01.020subject
Has Abstractpub_date
2019-01-29 00:00:00pages
1357-1367.e5issue
5issn
2211-1247pii
S2211-1247(19)30029-4journal_volume
26pub_type
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