7D8V

Crystal Structure of A Kinesin-3 KIF13B mutant-T192Y

Summary for 7D8V

• Entry DOI: 10.2210/pdb7d8v/pdb
• Descriptor: Kinesin family member 13B, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: kinesin, atpase, transport protein
• Biological source: Rattus norvegicus (Rat)
• Total number of polymer chains: 1
• Total formula weight: 49666.02

Authors

Ren, J.Q.,Feng, W. (deposition date: 2020-10-10, release date: 2021-10-13, Last modification date: 2023-11-29)

Primary citation

Cong, D.Z.,Ren, J.Q.,Zhou, Y.R.,Wang, S.,Liang, J.J.,Ding, M.,Feng, W.
Motor domain-mediated autoinhibition dictates axonal transport by the kinesin UNC-104/KIF1A.
Plos Genet., 17:e1009940-e1009940, 2021

PubMed Abstract: The UNC-104/KIF1A motor is crucial for axonal transport of synaptic vesicles, but how the UNC-104/KIF1A motor is activated in vivo is not fully understood. Here, we identified point mutations located in the motor domain or the inhibitory CC1 domain, which resulted in gain-of-function alleles of unc-104 that exhibit hyperactive axonal transport and abnormal accumulation of synaptic vesicles. In contrast to the cell body localization of wild type motor, the mutant motors accumulate on neuronal processes. Once on the neuronal process, the mutant motors display dynamic movement similarly to wild type motors. The gain-of-function mutation on the motor domain leads to an active dimeric conformation, releasing the inhibitory CC1 region from the motor domain. Genetically engineered mutations in the motor domain or CC1 of UNC-104, which disrupt the autoinhibitory interface, also led to the gain of function and hyperactivation of axonal transport. Thus, the CC1/motor domain-mediated autoinhibition is crucial for UNC-104/KIF1A-mediated axonal transport in vivo.

PubMed: 34843479
DOI: 10.1371/journal.pgen.1009940

Experimental method

X-RAY DIFFRACTION (2.3 Å)