Myosin IIIa boosts elongation of stereocilia by transporting espin 1 to the plus ends of actin filaments

Two proteins implicated in inherited deafness, myosin IIIa, a plus-end-directed motor, and espin, an actin-bundling protein containing the actin-monomer-binding motif WH2, have been shown to influence the length of mechanosensory stereocilia. Here we report that espin 1, an ankyrin repeat-containing...

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Published in	Nature cell biology Vol. 11; no. 4; pp. 443 - 450
Main Authors	Yengo, Christopher M, Kachar, Bechara, Merritt, Raymond C, Sousa, Aurea D, Salles, Felipe T, Manor, Uri, Dougherty, Gerard W, Moore, Judy E, Dosé, Andréa C
Format	Journal Article
Language	English
Published	London Nature Publishing Group UK 01.04.2009 Nature Publishing Group
Subjects	Actin Actin Cytoskeleton - metabolism Actin Cytoskeleton - ultrastructure Animals Ankyrin Repeat Biological transport Biomedical and Life Sciences Cancer Research Cell Biology Cellular control mechanisms Chlorocebus aethiops Cilia - metabolism Cilia - ultrastructure COS Cells Developmental Biology Genetic aspects letter Life Sciences Mice Microfilament Proteins - chemistry Microfilament Proteins - metabolism Myosin Myosin Type III - metabolism Physiological aspects Physiology Protein Binding Protein Transport Proteins Pseudopodia - metabolism Pseudopodia - ultrastructure Rats Stem Cells Transfection United States Italy
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Abstract	Two proteins implicated in inherited deafness, myosin IIIa, a plus-end-directed motor, and espin, an actin-bundling protein containing the actin-monomer-binding motif WH2, have been shown to influence the length of mechanosensory stereocilia. Here we report that espin 1, an ankyrin repeat-containing isoform of espin, colocalizes with myosin IIIa at stereocilia tips and interacts with a unique conserved domain of myosin IIIa. We show that combined overexpression of these proteins causes greater elongation of stereocilia, compared with overexpression of either myosin IIIa alone or espin 1 alone. When these two proteins were co-expressed in the fibroblast-like COS-7 cell line they induced a tenfold elongation of filopodia. This extraordinary filopodia elongation results from the transport of espin 1 to the plus ends of F-actin by myosin IIIa and depends on espin 1 WH2 activity. This study provides the basis for understanding the role of myosin IIIa and espin 1 in regulating stereocilia length, and presents a physiological example where myosins can boost elongation of actin protrusions by transporting actin regulatory factors to the plus ends of actin filaments.
AbstractList	Actin filaments in stereocilia on the surface of inner ear sensory hair cells are continually renewed. Myosin IIIa transports the actin-binding/bundling protein espin to stereocilia tips and cooperates with espin in actin filament elongation. Two proteins implicated in inherited deafness, myosin IIIa 1 , a plus-end-directed motor 2 , and espin 3 , 4 , 5 , 6 , an actin-bundling protein containing the actin-monomer-binding motif WH2, have been shown to influence the length of mechanosensory stereocilia 7 , 8 . Here we report that espin 1, an ankyrin repeat-containing isoform of espin 6 , colocalizes with myosin IIIa at stereocilia tips and interacts with a unique conserved domain of myosin IIIa. We show that combined overexpression of these proteins causes greater elongation of stereocilia, compared with overexpression of either myosin IIIa alone or espin 1 alone. When these two proteins were co-expressed in the fibroblast-like COS-7 cell line they induced a tenfold elongation of filopodia. This extraordinary filopodia elongation results from the transport of espin 1 to the plus ends of F-actin by myosin IIIa and depends on espin 1 WH2 activity. This study provides the basis for understanding the role of myosin IIIa and espin 1 in regulating stereocilia length, and presents a physiological example where myosins can boost elongation of actin protrusions by transporting actin regulatory factors to the plus ends of actin filaments. Two proteins implicated in inherited deafness, myosin IIIa (1), a plus-end-directed motor (2), and espin (3-6), an actin-bundling protein containing the actin-monomer-binding motif WH2, have been shown to influence the length of mechanosensory stereocilia (7,8). Here we report that espin 1, an ankyrin repeat-containing isoform of espin (6), colocalizes with myosin IIIa at stereocilia tips and interacts with a unique conserved domain of myosin IIIa. We show that combined overexpression of these proteins causes greater elongation of stereocilia, compared with overexpression of either myosin IIIa alone or espin 1 alone. When these two proteins were co-expressed in the fibroblast-like COS-7 cell line they induced a tenfold elongation of filopodia. This extraordinary filopodia elongation results from the transport of espin 1 to the plus ends of F-actin by myosin IIIa and depends on espin 1 WH2 activity. This study provides the basis for understanding the role of myosin IIIa and espin 1 in regulating stereocilia length, and presents a physiological example where myosins can boost elongation of actin protrusions by transporting actin regulatory factors to the plus ends of actin filaments. Two proteins implicated in inherited deafness, myosin IIIa, a plus-end-directed motor, and espin, an actin-bundling protein containing the actin-monomer-binding motif WH2, have been shown to influence the length of mechanosensory stereocilia. Here we report that espin 1, an ankyrin repeat-containing isoform of espin, colocalizes with myosin IIIa at stereocilia tips and interacts with a unique conserved domain of myosin IIIa. We show that combined overexpression of these proteins causes greater elongation of stereocilia, compared with overexpression of either myosin IIIa alone or espin 1 alone. When these two proteins were co-expressed in the fibroblast-like COS-7 cell line they induced a tenfold elongation of filopodia. This extraordinary filopodia elongation results from the transport of espin 1 to the plus ends of F-actin by myosin IIIa and depends on espin 1 WH2 activity. This study provides the basis for understanding the role of myosin IIIa and espin 1 in regulating stereocilia length, and presents a physiological example where myosins can boost elongation of actin protrusions by transporting actin regulatory factors to the plus ends of actin filaments.
Audience	Academic
Author	Sousa, Aurea D Salles, Felipe T Merritt, Raymond C Dosé, Andréa C Dougherty, Gerard W Manor, Uri Moore, Judy E Yengo, Christopher M Kachar, Bechara
AuthorAffiliation	3 Department of Biology, University of North Carolina at Charlotte, Charlotte, NC 28223, USA 1 Laboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD 20892, USA 2 Department of Biology, University of Maryland, College Park, MD 20742, USA 4 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA
AuthorAffiliation_xml	– name: 1 Laboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD 20892, USA – name: 4 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA – name: 3 Department of Biology, University of North Carolina at Charlotte, Charlotte, NC 28223, USA – name: 2 Department of Biology, University of Maryland, College Park, MD 20742, USA
Author_xml	– givenname: Christopher M surname: Yengo fullname: Yengo, Christopher M organization: Department of Biology, University of North Carolina at Charlotte – givenname: Bechara surname: Kachar fullname: Kachar, Bechara organization: Laboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health – givenname: Raymond C surname: Merritt fullname: Merritt, Raymond C organization: Laboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health Department of Biology, University of Maryland – givenname: Aurea D surname: Sousa fullname: Sousa, Aurea D organization: Laboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health – givenname: Felipe T surname: Salles fullname: Salles, Felipe T organization: Laboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health – givenname: Uri surname: Manor fullname: Manor, Uri organization: Laboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health – givenname: Gerard W surname: Dougherty fullname: Dougherty, Gerard W organization: Laboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health Consorzio Mario Negri Sud, Department of Cell Biology and Oncology – givenname: Judy E surname: Moore fullname: Moore, Judy E organization: Department of Biology, University of North Carolina at Charlotte – givenname: Andréa C surname: Dosé fullname: Dosé, Andréa C organization: Department of Molecular and Cell Biology, University of California
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/19287378$$D View this record in MEDLINE/PubMed
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Notes	SourceType-Other Sources-1 ObjectType-Article-2 content type line 63 ObjectType-Correspondence-1 Author Contributions: R.C.M. designed probes and experiments, performed the GST pull-downs, cell culture, immunocytochemistry, and transfections; F.T.S. performed the dissections, cell and organotypic cultures, immuno-histochemistry, transfections, and confocal imaging; G.W.D. and A.C.D. designed probes, performed transfections, and contributed to experimental design; U.M. performed image and statistical analyses; A.D.S. characterized antibody and DNA probes; C.M.Y. and J.E.M. generated myosin IIIa kinase dead cDNA, purified, and performed kinase and motor activity assays.; B.K. performed electron microscopy, designed experiments, and analyzed the results together with all the other authors. All authors discussed and helped prepare the manuscript. Current address: Consorzio Mario Negri Sud, Department of Cell Biology and Oncology, Santa Maria Imbaro, Chieti, Italy 66030. Contributed equally
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Snippet	Two proteins implicated in inherited deafness, myosin IIIa, a plus-end-directed motor, and espin, an actin-bundling protein containing the... Actin filaments in stereocilia on the surface of inner ear sensory hair cells are continually renewed. Myosin IIIa transports the actin-binding/bundling... Two proteins implicated in inherited deafness, myosin IIIa (1), a plus-end-directed motor (2), and espin (3-6), an actin-bundling protein containing the...
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SubjectTerms	Actin Actin Cytoskeleton - metabolism Actin Cytoskeleton - ultrastructure Animals Ankyrin Repeat Biological transport Biomedical and Life Sciences Cancer Research Cell Biology Cellular control mechanisms Chlorocebus aethiops Cilia - metabolism Cilia - ultrastructure COS Cells Developmental Biology Genetic aspects letter Life Sciences Mice Microfilament Proteins - chemistry Microfilament Proteins - metabolism Myosin Myosin Type III - metabolism Physiological aspects Physiology Protein Binding Protein Transport Proteins Pseudopodia - metabolism Pseudopodia - ultrastructure Rats Stem Cells Transfection
Title	Myosin IIIa boosts elongation of stereocilia by transporting espin 1 to the plus ends of actin filaments
URI	http://dx.doi.org/10.1038/ncb1851 https://link.springer.com/article/10.1038/ncb1851 https://www.ncbi.nlm.nih.gov/pubmed/19287378 https://www.proquest.com/docview/222366060 https://search.proquest.com/docview/67100871 https://pubmed.ncbi.nlm.nih.gov/PMC2750890
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