AI Article Synopsis
- The inner ear has tiny hair cells that help us hear by having special structures called stereocilia that are arranged in rows.
- Scientists found two types of a protein called myosin 15 that help these stereocilia grow and stay strong, but they work in different ways.
- When they studied mice that only had one type of myosin 15, the hair cells looked normal at first, but some stereocilia then shrank because they needed the other type of myosin to keep them stable.
Article Abstract
The precise assembly of inner ear hair cell stereocilia into rows of increasing height is critical for mechanotransduction and the sense of hearing. Yet, how the lengths of actin-based stereocilia are regulated remains poorly understood. Mutations of the molecular motor myosin 15 stunt stereocilia growth and cause deafness. We found that hair cells express two isoforms of myosin 15 that differ by inclusion of an 133-kDa N-terminal domain, and that these isoforms can selectively traffic to different stereocilia rows. Using an isoform-specific knockout mouse, we show that hair cells expressing only the small isoform remarkably develop normal stereocilia bundles. However, a critical subset of stereocilia with active mechanotransducer channels subsequently retracts. The larger isoform with the 133-kDa N-terminal domain traffics to these specialized stereocilia and prevents disassembly of their actin core. Our results show that myosin 15 isoforms can navigate between functionally distinct classes of stereocilia, and are independently required to assemble and then maintain the intricate hair bundle architecture.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4592939 | PMC |
| http://dx.doi.org/10.7554/eLife.08627 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The 133-kDa N-terminal domain enables myosin 15 to maintain mechanotransducing stereocilia and is essential for hearing.
Elife
August 2015
Laboratory of Molecular Genetics, National Institutes of Health, Bethesda, United States.
Article Synopsis
- The inner ear has tiny hair cells that help us hear by having special structures called stereocilia that are arranged in rows.
- Scientists found two types of a protein called myosin 15 that help these stereocilia grow and stay strong, but they work in different ways.
- When they studied mice that only had one type of myosin 15, the hair cells looked normal at first, but some stereocilia then shrank because they needed the other type of myosin to keep them stable.
Expression, purification and initial characterization of human meprin β from Pichia pastoris.
Protein Expr Purif
December 2015
Fraunhofer Institute for Cell Therapy and Immunology, Department of Drug Design and Target Validation (IZI-MWT), Weinbergweg 22, 06120 Halle/Saale, Germany. Electronic address:
Human meprin β (h-meprin β), a single-zinc metalloendoprotease of the astacin family, is potentially involved in disorders such as fibrosis and Alzheimer's disease. Here, we describe the expression of the enzyme in the yeast Pichia pastoris. The N-terminal signal sequence was replaced by the α-leader of Saccharomyces, enabling efficient secretion of the mature enzyme, harboring either an N-terminal or C-terminal His-tag.
View Article and Find Full Text PDFStructural and molecular insights into novel surface-exposed mucus adhesins from Lactobacillus reuteri human strains.
Mol Microbiol
May 2014
Institute of Food Research, Norwich Research Park, Colney, Norwich, NR4 7UA, UK.
The mucus layer covering the gastrointestinal tract is the first point of contact of the intestinal microbiota with the host. Cell surface macromolecules are critical for adherence of commensal bacteria to mucus but structural information is scarce. Here we report the first molecular and structural characterization of a novel cell-surface protein, Lar_0958 from Lactobacillus reuteri JCM 1112(T) , mediating adhesion of L.
View Article and Find Full Text PDFStructural implication of the induced immune response by Bacillus thuringiensis Cry proteins: role of the N-terminal region.
Mol Immunol
November 2004
FES-IZTACALA, Universidad Nacional Autónoma de México, Biomedicine Av de los Barrios s/n Col. Los Reyes Iztacala 54090 Tlanepantla, Edo de México, Mexico.
The potential role of the regions (carboxil and amino) of the Cry proteins in the ability of these proteins to elicit strong immune responses was investigated. Intraperitoneal immunization of mice with the homologous Cry1A protoxins (130-133 kDa), with the long C-terminal half gave rise mostly to similar, strong serum and mucosal IgG and IgM antibody response but a lower induction of these Ab by intranasal route. Remarkably, Cry3A protoxin, devoid of C-terminal half was able to induce a significant mucosal IgG, and IgM Ab as well as Cry1A protoxins, suggesting us that immunogenic abilities are not restricted to C-terminal half but N-terminal half itself could be involved.
View Article and Find Full Text PDFRECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway.
Hum Mol Genet
October 2004
Laboratory of Genetics, National Institute on Aging, National Institutes of Health, 333 Cassell Drive, TRIAD Center Room 3000, Baltimore, MD 21224, USA.
The Rothmund-Thomson syndrome (growth retardation, skin and bone defects, predisposition to cancer) and the RAPADILINO syndrome are caused by mutations in the RECQL4 gene. The 133 kDa RECQL4 is a putative DNA helicase, a member of the family that includes the BLM and WRN helicases. The latter are mutated, respectively, in the Bloom and Werner syndromes, whose manifestations include predisposition to cancer.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!