Distinct Actin-tropomyosin Cofilament Populations Drive the Functional Diversification of Cytoskeletal Myosin Motor Complexes
Overview
Authors
Affiliations
The effects of N-terminal acetylation of the high molecular weight tropomyosin isoforms Tpm1.6 and Tpm2.1 and the low molecular weight isoforms Tpm1.12, Tpm3.1, and Tpm4.2 on the actin affinity and the thermal stability of actin-tropomyosin cofilaments are described. Furthermore, we show how the exchange of cytoskeletal tropomyosin isoforms and their N-terminal acetylation affects the kinetic and chemomechanical properties of cytoskeletal actin-tropomyosin-myosin complexes. Our results reveal the extent to which the different actin-tropomyosin-myosin complexes differ in their kinetic and functional properties. The maximum sliding velocity of the actin filament as well as the optimal motor density for continuous unidirectional movement, parameters that were previously considered to be unique and invariant properties of each myosin isoform, are shown to be influenced by the exchange of the tropomyosin isoform and the N-terminal acetylation of tropomyosin.
Functional and Structural Properties of Cytoplasmic Tropomyosin Isoforms Tpm1.8 and Tpm1.9.
Lapshina K, Nefedova V, Nabiev S, Roman S, Shchepkin D, Kopylova G Int J Mol Sci. 2024; 25(13).
PMID: 38999987 PMC: 11240984. DOI: 10.3390/ijms25136873.
Structure, regulation, and mechanisms of nonmuscle myosin-2.
Chinthalapudi K, Heissler S Cell Mol Life Sci. 2024; 81(1):263.
PMID: 38878079 PMC: 11335295. DOI: 10.1007/s00018-024-05264-6.
Cagigas M, Ariotti N, Hook J, Rae J, Parton R, Bryce N Cytoskeleton (Hoboken). 2024; 82(1-2):45-54.
PMID: 38872463 PMC: 11748362. DOI: 10.1002/cm.21883.
Kengyel A, Palarz P, Krohn J, Marquardt A, Greve J, Heiringhoff R Front Physiol. 2024; 15:1394040.
PMID: 38606007 PMC: 11008601. DOI: 10.3389/fphys.2024.1394040.
Focal adhesions contain three specialized actin nanoscale layers.
Kumari R, Ven K, Chastney M, Kokate S, Peranen J, Aaron J Nat Commun. 2024; 15(1):2547.
PMID: 38514695 PMC: 10957975. DOI: 10.1038/s41467-024-46868-7.