Myomics: myosin VI structural and functional plasticity

Magistrati, Elisa; Polo, Simona

doi:10.1016/j.sbi.2020.09.005

Cited by 19 publications

(23 citation statements)

References 48 publications

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“…To further confirm this idea, we performed immunogold electron microscopy analysis of the endogenous myosin VI. As expected, myosin VI shows multiple signals corresponding to the various cytoplasmatic organelles where it performs its function (Magistrati & Polo, 2020 ). Notably, a specific signal was evident at the level of centriole walls in wild type but not in a myosin VI knock‐out (KO) cell line (Fig 1D ).…”

Section: Resultssupporting

confidence: 68%

“…The functional and phenotypic diversity associated with myosin VI arises from multiple interactors and the existence of alternatively spliced isoforms (Magistrati & Polo, 2020 ). Indeed, two distinct isoform types, myosin VI short and myosin VI long, differ in an isoform‐specific helix that modifies their conformation and restricts binding to their interactomes (Wollscheid et al , 2016 ).…”

Section: Resultsmentioning

confidence: 99%

“…Addition of the MIU domain is unable to strengthen the interaction (Fig EV2E ). Interestingly, the SAH domain, while it does not interact with OFD1 per se (Fig EV2F ), appears to be required for the maximum binding (Fig 1E ), implying that the conformation of the tail may be important for the interaction (Magistrati & Polo, 2020 ).…”

Section: Resultsmentioning

confidence: 99%

“…Myosin VI activity on OFD1 appears to be critical for maintaining the correct amount of the distal appendages at the mother centriole and for the removal of OFD1 from the centriolar satellites to promote primary ciliogenesis. Thus, OFD1 can be added to the list of specialised cargo‐adaptor proteins that link myosin VI to distinct cellular compartments and processes (Magistrati & Polo, 2020 ). Importantly, both myosin VI short and long isoforms (Wollscheid et al , 2016 ) interact with OFD1, indicating that this functional interaction is conserved in all cells and is maintained upon epithelial cell polarisation where a switch between isoforms was observed (Buss et al , 2001 ; Biancospino et al , 2019 ).…”

Section: Discussionmentioning

confidence: 99%

“…A proteomic study identified OFD1 as a possible interactor of myosin VI (O'Loughlin et al , 2018 ), a unique motor protein that moves towards the minus end of the actin filaments (Magistrati & Polo, 2020 ). The molecular pathways and the physiological relevance of this interaction remain unknown.…”

Section: Introductionmentioning

confidence: 99%

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Myosin VI regulates ciliogenesis by promoting the turnover of the centrosomal/satellite protein OFD1

et al. 2021

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The actin motor protein myosin VI is a multivalent protein with diverse functions. Here, we identified and characterised a myosin VI ubiquitous interactor, the oral‐facial‐digital syndrome 1 (OFD1) protein, whose mutations cause malformations of the face, oral cavity, digits and polycystic kidney disease. We found that myosin VI regulates the localisation of OFD1 at the centrioles and, as a consequence, the recruitment of the distal appendage protein Cep164. Myosin VI depletion in non‐tumoural cell lines causes an aberrant localisation of OFD1 along the centriolar walls, which is due to a reduction in the OFD1 mobile fraction. Finally, loss of myosin VI triggers a severe defect in ciliogenesis that could be, at least partially, ascribed to an impairment in the autophagic removal of OFD1 from satellites. Altogether, our results highlight an unprecedent layer of regulation of OFD1 and a pivotal role of myosin VI in coordinating the formation of the distal appendages and primary cilium with important implications for the genetic disorders known as ciliopathies.

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Section: Resultssupporting

confidence: 68%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Myosin VI regulates ciliogenesis by promoting the turnover of the centrosomal/satellite protein OFD1

et al. 2021

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Myosin motors on the pathway of viral infections

2022

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Molecular motors are microscopic machines that use energy from adenosine triphosphate (ATP) hydrolysis to generate movement. While kinesins and dynein are molecular motors associated with microtubule tracks, myosins bind to and move on actin filaments. Mammalian cells express several myosin motors. They power cellular processes such as endo‐ and exocytosis, intracellular trafficking, transcription, migration, and cytokinesis. As viruses navigate through cells, they may take advantage or be hindered by host components and machinery, including the cytoskeleton. This review delves into myosins' cell roles and compares them to their reported functions in viral infections. In most cases, the previously described myosin functions align with their reported role in viral infections, although not in all cases. This opens the possibility that knowledge obtained from studying myosins in viral infections might shed light on new physiological roles for myosins in cells. However, given the high number of myosins expressed and the variety of viruses investigated in the different studies, it is challenging to infer whether the interactions found are specific to a single virus or can be applied to other viruses with the same characteristics. We conclude that the participation of myosins in viral cycles is still a largely unexplored area, especially concerning unconventional myosins.

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Myosin VI Is Associated With the Endoplasmic Reticulum in Regions of Sertoli Cells Containing Tubulobulbar Complexes

Tretjakov,

Palia,

Vogl

2024

Cytoskeleton

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Myosin VI has been reported by others to localize in association with various regions of apical tubulobulbar complexes (TBCs) at sites of attachment between Sertoli cells and late spermatids in the mouse. Tubulobulbar complexes internalize “intact” intercellular junctions during sperm release and during spermatocyte translocation through the blood‐testis barrier. Here, we use super‐resolution (STED—stimulated emission depletion) and electron microscopy of immunolabeled sections of rat testis to clearly define the localization of anti‐myosin VI reactivity both at apical and basal sites in the epithelium. In data stacks collected by STED imaging, staining at TBCs was predominantly associated with bulb regions of the complexes. At apical sites, when data stacks were analyzed with an Imaris software, staining appeared around and extended between adjacent bulbs. At basal sites, in addition to labeling at TBC bulbs, reactive sites appeared concentrated in regions close to but not directly associated with intercellular junctions. At the ultrastructural level, labeling was predominantly associated with cisternae of the endoplasmic reticulum associated with the bulbs of TBCs and near to basal junction complexes. We conclude that myosin VI may be associated with specific subdomains of the endoplasmic reticulum related to TBC bulbs and associated basal junction complexes between Sertoli cells.

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Myomics: myosin VI structural and functional plasticity

Cited by 19 publications

References 48 publications

Myosin VI regulates ciliogenesis by promoting the turnover of the centrosomal/satellite protein OFD1

Myosin VI regulates ciliogenesis by promoting the turnover of the centrosomal/satellite protein OFD1

Myosin motors on the pathway of viral infections

Myosin VI Is Associated With the Endoplasmic Reticulum in Regions of Sertoli Cells Containing Tubulobulbar Complexes

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