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Myosin XI, a model of its conserved role in plant cell tip growth.
- Source :
-
Biochemical Society transactions [Biochem Soc Trans] 2024 Apr 24; Vol. 52 (2), pp. 505-515. - Publication Year :
- 2024
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Abstract
- In eukaryotic cells, organelle and vesicle transport, positioning, and interactions play crucial roles in cytoplasmic organization and function. These processes are governed by intracellular trafficking mechanisms. At the core of that trafficking, the cytoskeleton and directional transport by motor proteins stand out as its key regulators. Plant cell tip growth is a well-studied example of cytoplasm organization by polarization. This polarization, essential for the cell's function, is driven by the cytoskeleton and its associated motors. This review will focus on myosin XI, a molecular motor critical for vesicle trafficking and polarized plant cell growth. We will center our discussion on recent data from the moss Physcomitrium patens and the liverwort Marchantia polymorpha. The biochemical properties and structure of myosin XI in various plant species are discussed, highlighting functional conservation across species. We further explore this conservation of myosin XI function in the process of vesicle transport in tip-growing cells. Existing evidence indicates that myosin XI actively organizes actin filaments in tip-growing cells by a mechanism based on vesicle clustering at their tips. A hypothetical model is presented to explain the essential function of myosin XI in polarized plant cell growth based on vesicle clustering at the tip. The review also provides insight into the in vivo localization and dynamics of myosin XI, emphasizing its role in cytosolic calcium regulation, which influences the polymerization of F-actin. Lastly, we touch upon the need for additional research to elucidate the regulation of myosin function.<br /> (© 2024 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.)
Details
- Language :
- English
- ISSN :
- 1470-8752
- Volume :
- 52
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical Society transactions
- Publication Type :
- Academic Journal
- Accession number :
- 38629612
- Full Text :
- https://doi.org/10.1042/BST20220783