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- W2806871275 abstract "While unconventional myosins interact with different stages of the endocytic pathway, they are ascribed a transport function that is secondary to the protein complexes that control organelle identity. Endosomes are subject to a dynamic, continuous flux of proteins that control their characteristic properties, including their motility within the cell. Efforts to describe the changes in identity of this compartment have largely focused on the adaptors present on the compartment and not on the motile properties of the compartment itself. In this study, we use a combination of optogenetic and chemical‐dimerization strategies to target exogenous myosin VI to early endosomes, and probe its influence on organelle motility, morphology and identity. Our analysis across timescales suggests a model wherein the artificial engagement of myosin VI motility on early endosomes restricts microtubule‐based motion, followed by morphological changes characterized by the rapid condensation and disintegration of organelles, ultimately leading to the enhanced overlap of markers that demarcate endosomal compartments. Together, our findings show that synthetic engagement of myosin VI motility is sufficient to alter organelle homeostasis in the endocytic pathway." @default.
- W2806871275 created "2018-06-13" @default.
- W2806871275 creator A5008386120 @default.
- W2806871275 creator A5055771278 @default.
- W2806871275 date "2018-07-16" @default.
- W2806871275 modified "2023-09-26" @default.
- W2806871275 title "Engaging myosin VI tunes motility, morphology and identity in endocytosis" @default.
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- W2806871275 doi "https://doi.org/10.1111/tra.12583" @default.
- W2806871275 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6437008" @default.
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- W2806871275 hasPublicationYear "2018" @default.
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