Journal
ISCIENCE
Volume 23, Issue 5, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.isci.2020.101053
Keywords
-
Categories
Funding
- Academy of Finland [SA 266351]
- Doctoral Programme Brain Mind
- Australian Research Council [DP180101473]
- Australian National Health and Medical Research Council [APP1083209, APP1079866, APP1100202]
- Kids Cancer Project
Ask authors/readers for more resources
The axon initial segment (AIS) is the site of action potential initiation and serves as a cargo transport filter and diffusion barrier that helps maintain neuronal polarity. The AIS actin cytoskeleton comprises actin patches and periodic sub-membranous actin rings. We demonstrate that tropomyosin isoform Tpm3.1 co-localizes with actin patches and that the inhibition of Tpm3.1 led to a reduction in the density of actin patches. Furthermore, Tpm3.1 showed a periodic distribution similar to sub-membranous actin rings but Tpm3.1 was only partially congruent with sub-membranous actin rings. Nevertheless, the inhibition of Tpm3.1 affected the uniformity of the periodicity of actin rings. Furthermore, Tpm3.1 inhibition led to reduced accumulation of AIS structural and functional proteins, disruption in sorting somatodendritic and axonal proteins, and a reduction in firing frequency. These results show that Tpm3.1 is necessary for the structural and functional maintenance of the AIS.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available