Propagation of F-actin disassembly via Myosin15-Mical interactions

Shannon K. Rich, Raju Baskar, Jonathan R. Terman

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


The F-actin cytoskeleton drives cellular form and function. However, how F-actin-based changes occur with spatiotemporal precision and specific directional orientation is poorly understood. Here, we identify that the unconventional class XV myosin [Myosin 15 (Myo15)] physically and functionally interacts with the F-actin disassembly enzyme Mical to spatiotemporally position cellular breakdown and reconstruction. Specifically, while unconventional myosins have been associated with transporting cargo along F-actin to spatially target cytoskeletal assembly, we now find they also target disassembly. Myo15 specifically positions this F-actin disassembly by associating with Mical and using its motor and MyTH4-FERM cargo-transporting functions to broaden Mical’s distribution. Myo15’s broadening of Mical’s distribution also expands and directionally orients Mical-mediated F-actin disassembly and subsequent cellular remodeling, including in response to Semaphorin/Plexin cell surface activation signals. Thus, we identify a mechanism that spatiotemporally propagates F-actin disassembly while also proposing that other F-actin-trafficked-cargo is derailed by this disassembly to directionally orient rebuilding.

Original languageEnglish (US)
Article numbereabg0147
JournalScience Advances
Issue number20
StatePublished - May 2021

ASJC Scopus subject areas

  • General


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