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Review
. 2017 Feb:44:68-78.
doi: 10.1016/j.ceb.2016.10.002. Epub 2016 Nov 9.

MyTH4-FERM myosins in the assembly and maintenance of actin-based protrusions

Meredith L Weck  1 , Nathan E Grega-Larson  1 , Matthew J Tyska  2
Affiliations
Review

MyTH4-FERM myosins in the assembly and maintenance of actin-based protrusions

Meredith L Weck et al. Curr Opin Cell Biol. 2017 Feb.

Abstract

Unconventional myosins are actin-based molecular motors that serve a multitude of roles within the cell. One group of myosin motors, the MyTH4-FERM myosins, play an integral part in building and maintaining finger-like protrusions, which allow cells to interact with their external environment. Suggested to act primarily as transporters, these motor proteins enrich adhesion molecules, actin-regulatory proteins and other factors at the tips of filopodia, microvilli, and stereocilia. Below we review data from biophysical, biochemical, and cell biological studies, which implicate these myosins as central players in the assembly, maintenance and function of actin-based protrusions.

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Figures

Figure 1
Figure 1
Finger-like membrane protrusions featured in this review: (A) filopodia, (B) microvilli, and (C) stereocilia. The relevant MyTH4-FERM myosins and their cargoes are listed in each case.
Figure 2
Figure 2
Domain diagram of the MyTH4-FERM myosins. Numbers indicate amino acids. Figure depicts isoform 1 for Myo15a; isoform 2 (2307 amino acids) does not include the N-terminal extension. Hs, Homo sapiens; IQs, IQ calmodulin- or light chain-binding motifs; SAH, stable alpha helix; anti-CC, anti-parallel coiled coil; PEST, proline, glutamate, serine, threonine peptide sequence for protein degradation; PDZ, post synaptic density protein (PSD95), Disc large homolog 1 (Dlg1), and zonula occludens-1 (ZO-1).
See this image and copyright information in PMC

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