2024-03-28T14:25:29Z
https://tsukuba.repo.nii.ac.jp/oai
oai:tsukuba.repo.nii.ac.jp:00047179
2022-04-27T09:16:44Z
2780:4866
2780:6228
3:62:5587:1048
Myosin Id localizes in dendritic spines through the tail homology 1 domain
越田, 隆介
武井, 陽介
Koshida, Ryusuke
Tome, Saki
Takei, Yosuke
© 2018 Elsevier Inc.
Dendritic spines, the postsynaptic compartments at excitatory synapses, are capable of changing their shape and size to modulate synaptic transmission. The actin cytoskeleton and a variety of actin-binding proteins play a critical role in the dynamics of dendritic spines. Class I myosins are monomeric motor proteins that move along actin filaments using the energy of ATP hydrolysis. Of these class I myosins, myosin Id, the mammalian homolog of Drosophila Myo31DF, has been reported to be expressed in neurons, whereas its subcellular localization in neurons remained unknown. Here, we investigated the subcellular localization of myosin Id and determined the domain responsible for it. We found that myosin Id is enriched in the F-actin-rich pseudopodia of HEK293T cells and in the dendritic spines of primary hippocampal neurons. Both deletion and substitution of the tail homology 1 (TH1) domain drastically diminishes its colocalization with F-actin. In addition, the mutant form lacking the TH1 domain is less distributed in dendritic spines than is the full-length form. Taken together, our findings reveal that myosin Id localizes in dendritic spines through the TH1 domain.
Elsevier Inc.
2018-06
eng
journal article
http://hdl.handle.net/2241/00152547
https://tsukuba.repo.nii.ac.jp/records/47179
29559226
10.1016/j.yexcr.2018.03.021
0014-4827
AA00641011
Experimental cell research
367
1
65
72
https://tsukuba.repo.nii.ac.jp/record/47179/files/ECR_367-1.pdf
application/pdf
9.4 MB
2019-07-01