Tropomyosin Tpm3.1 is required to maintain the structure and function of the axon initial segment

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http://hdl.handle.net/10138/316268

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Abouelezz , A , Stefen , H , Segerstråle , M , Micinski , D , Minkeviciene , R , Lahti , L , Hardeman , E C , Gunning , P W , Hoogenraad , C C , Taira , T , Fath , T & Hotulainen , P 2020 , ' Tropomyosin Tpm3.1 is required to maintain the structure and function of the axon initial segment ' , iScience , vol. 23 , no. 5 , 101053 . https://doi.org/10.1016/j.isci.2020.101053

Title: Tropomyosin Tpm3.1 is required to maintain the structure and function of the axon initial segment
Author: Abouelezz, Amr; Stefen, Holly; Segerstråle, Mikael; Micinski, David; Minkeviciene, Rimante; Lahti, Lauri; Hardeman, Edna C.; Gunning, Peter W.; Hoogenraad, Casper C.; Taira, Tomi; Fath, Thomas; Hotulainen, Pirta
Contributor: University of Helsinki, Neuroscience Center
University of Helsinki, Molecular and Integrative Biosciences Research Programme
University of Helsinki, Minerva Foundation Institute for Medical Research
University of Helsinki, Medicum
University of Helsinki, Veterinary Physiology
University of Helsinki, Medicum
Date: 2020-05-22
Language: eng
Number of pages: 50
Belongs to series: iScience
ISSN: 2589-0042
URI: http://hdl.handle.net/10138/316268
Abstract: 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.
Subject: 1182 Biochemistry, cell and molecular biology
POLARIZED CARGO TRANSPORT
MYOSIN-II ACTIVITY
ANKYRIN-G
ACTIN CYTOSKELETON
MOLECULAR COMPOSITION
MEMBRANE SKELETON
BINDING PROTEINS
ISOFORMS
SPECTRIN
MAINTENANCE
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