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A neuropathy-associated kinesin KIF1A mutation hyper-stabilizes the motor-neck interaction during the ATPase cycle
Journal article   Open access   Peer reviewed

A neuropathy-associated kinesin KIF1A mutation hyper-stabilizes the motor-neck interaction during the ATPase cycle

Manatsu Morikawa, Nivedita U Jerath, Tadayuki Ogawa, Momo Morikawa, Yosuke Tanaka, Michael E Shy, Stephan Zuchner and Nobutaka Hirokawa
The EMBO journal, Vol.41(5), pp.e108899-e108899
02/08/2022
DOI: 10.15252/embj.2021108899
PMCID: PMC8886545
PMID: 35132656
url
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8886545View
Published (Version of record) Open Access

Abstract

The mechanochemical coupling of ATPase hydrolysis and conformational dynamics in kinesin motors facilitates intramolecular interaction cycles between the kinesin motor and neck domains, which are essential for microtubule-based motility. Here, we characterized a charge-inverting KIF1A-E239K mutant that we identified in a family with axonal-type Charcot-Marie-Tooth disease and also in 24 cases in human neuropathies including spastic paraplegia and hereditary sensory and autonomic neuropathy. We show that Glu239 in the β7 strand is a key residue of the motor domain that regulates the motor-neck interaction. Expression of the KIF1A-E239K mutation has decreased ability to complement Kif1a neurons, and significantly decreases ATPase activity and microtubule gliding velocity. X-ray crystallography shows that this mutation causes an excess positive charge on β7, which may electrostatically interact with a negative charge on the neck. Quantitative mass spectrometric analysis supports that the mutation hyper-stabilizes the motor-neck interaction at the late ATP hydrolysis stage. Thus, the negative charge of Glu239 dynamically regulates the kinesin motor-neck interaction, promoting release of the neck from the motor domain upon ATP hydrolysis.
axonal transport human neuropathies motor-neck interaction KIF1A neuropathy-related mutation

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