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      Microvilli regulate the release modes of alpha-tectorin to organize the domain-specific matrix architecture of the tectorial membrane

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          Abstract

          The tectorial membrane (TM) is an apical extracellular matrix (ECM) in the cochlea essential for auditory transduction. The TM exhibits highly ordered domain-specific architecture. Alpha-tectorin/TECTA is a glycosylphosphatidylinositol (GPI)-anchored ECM protein essential for TM organization. Here, we identified that TECTA is released by distinct modes: proteolytic shedding by TMPRSS2 and GPI-anchor-dependent release from the microvillus tip. In the medial/limbal domain, proteolytically shed TECTA forms dense fibers. In the lateral/body domain produced by the supporting cells displaying dense microvilli, the proteolytic shedding restricts TECTA to the microvillus tip and compartmentalizes the collagen-binding site. The tip-localized TECTA, in turn, is released in a GPI-anchor-dependent manner to form collagen-crosslinking fibers, required for maintaining the spacing and parallel organization of collagen fibrils. Overall, we showed that distinct release modes of TECTA determine the domain-specific organization pattern, and the microvillus coordinates the release modes along its membrane to organize the higher-order ECM architecture.

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          Reassessment of Exosome Composition

          Dennis Jeppesen, Aidan M. Fenix, Jeffrey L. Franklin … (2019)
          The heterogeneity of small extracellular vesicles and presence of non-vesicular extracellular matter have led to debate about contents and functional properties of exosomes. Here, we employ high-resolution density gradient fractionation and direct immunoaffinity capture to precisely characterize the RNA, DNA, and protein constituents of exosomes and other non-vesicle material. Extracellular RNA, RNA-binding proteins and other cellular proteins are differentially expressed in exosomes and non-vesicle compartments. Argonaute 1–4, glycolytic enzymes and cytoskeletal proteins are absent from exosomes. We identify Annexin A1 as a specific marker for microvesicles that are shed directly from the plasma membrane. We further show that small extracellular vesicles are not vehicles of active DNA release. Instead, we propose a new model for active secretion of extracellular DNA through an autophagy- and multivesicular endosome-dependent, but exosome-independent mechanism. This study demonstrates the need for a reassessment of exosome composition and offers a framework for a clearer understanding of extracellular vesicle heterogeneity. A reassessment of exosome composition establishes the differential distribution of protein, RNA, and DNA between small extracellular vesicles and non-vesicular extracellular matter and establishes that small extracellular vesicles are not vehicles of active DNA release.
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            The extracellular matrix at a glance.

            Christian Frantz, Kathleen Stewart, Valerie Weaver (2010)
            Article 0 comments Cited 848 times – based on 0 reviews     Review now
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              The collagen family.

              Sylvie Ricard-Blum (2010)
              Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that contain at least one triple-helical domain. Collagens are deposited in the extracellular matrix where most of them form supramolecular assemblies. Four collagens are type II membrane proteins that also exist in a soluble form released from the cell surface by shedding. Collagens play structural roles and contribute to mechanical properties, organization, and shape of tissues. They interact with cells via several receptor families and regulate their proliferation, migration, and differentiation. Some collagens have a restricted tissue distribution and hence specific biological functions.
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                Author and article information

                Journal
                Journal ID (nlm-ta): bioRxiv
                Journal ID (publisher-id): BIORXIV
                Title: bioRxiv
                Publisher: Cold Spring Harbor Laboratory
                Publication date (Electronic): 05 January 2024
                Electronic Location Identifier: 2024.01.04.574255
                Affiliations
                [1. ]Department of Neurobiology, University of Utah, Salt Lake City, Utah, USA
                [2. ]Neuroscience Program, University of Utah, Salt Lake City, Utah, USA
                [3. ]Current affiliation: Department of Otorhinolaryngology-Head and Neck Surgery, Seoul National University College of Medicine, Seoul National University Bundang Hospital, Seongnam, South Korea
                [4. ]Current affiliation: Genetics & Genome Biology, The Hospital for Sick Children, Toronto, Ontario, Canada
                Author notes
                Correspondence: Sungjin Park, Department of Neurobiology, University of Utah School of Medicine, Salt Lake City, UT 84112. sungjin.park@ 123456neuro.utah.edu
                Author information
                http://orcid.org/0000-0003-4430-3305
                Article
                DOI: 10.1101/2024.01.04.574255
                PMC ID: 10802356
                PubMed ID: 38260557
                SO-VID: 5c18d185-6e5b-4215-8762-084fdfd57e20
                License:

                This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator.

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                Subject: Article

                Keywords: extracellular matrix,ecm,tectorial membrane,alpha-tectorin,tecta,microvilli,collagen,tmprss2
                Data availability:
                Keywords: extracellular matrix, ecm, tectorial membrane, alpha-tectorin, tecta, microvilli, collagen, tmprss2

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