ArticleScientific reports2016
Cadherin 23-C Regulates Microtubule Networks by Modifying CAMSAP3's Function.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Ploidy and Implantation Potential: Non-Invasive Small Non-Coding RNA-Based Health Assessment of Day 5 and 6 Blastocysts.International journal of molecular sciences · 2025Article
- Vestibular Hair Cells Require CAMSAP3, a Microtubule Minus-End Regulator, for Formation of Normal Kinocilia.Frontiers in cellular neuroscience · 2022Article
- Usher Syndrome: Genetics of a Human Ciliopathy.International journal of molecular sciences · 2021Review
- CAMSAP3 facilitates basal body polarity and the formation of the central pair of microtubules in motile cilia.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Usher Syndrome: Genetics and Molecular Links of Hearing Loss and Directions for Therapy.Frontiers in genetics · 2020Review
- Zooming in on Cadherin-23: Structural Diversity and Potential Mechanisms of Inherited Deafness.Structure (London, England : 1993) · 2018Article
- Beyond Cell-Cell Adhesion: Sensational Cadherins for Hearing and Balance.Cold Spring Harbor perspectives in biology · 2018Review
- Cadherin-26 (CDH26) regulates airway epithelial cell cytoskeletal structure and polarity.Cell discovery · 2018Article
- Usher syndrome type 1-associated cadherins shape the photoreceptor outer segment.The Journal of cell biology · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Cadherin-related 23 (CDH23) is an adhesive protein important for hearing and vision, while CAMSAP3/Marshalin is a microtubule (MT) minus-end binding protein that regulates MT networks. Although both CDH23 and CAMSAP3/Marshalin are expressed in the organ of Corti, and carry several protein-protein interaction domains, no functional connection between these two proteins has been proposed. In this report, we demonstrate that the C isoform of CDH23 (CDH23-C) directly binds to CAMSAP3/Marshalin and modifies its function by inhibiting CAMSAP3/Marshalin-induced bundle formation, a process that requires a tubulin-binding domain called CKK. We further identified a conserved N-terminal region of CDH23-C that binds to the CKK domain. This CKK binding motif (CBM) is adjacent to the domain that interacts with harmonin, a binding partner of CDH23 implicated in deafness. Because the human Usher Syndrome 1D-associated mutation, CDH23 R3175H, maps to the CBM, we created a matched mutation in mouse CDH23-C at R55H. Both in vivo and in vitro assays decreased the ability of CDH23-C to interact with CAMSAP3/Marshalin, indicating that the interaction between CDH23 and CAMSAP3/Marshalin plays a vital role in hearing and vision. Together, our data suggest that CDH23-C is a CAMSAP3/Marshalin-binding protein that can modify MT networks indirectly through its interaction with CAMSAP3/Marshalin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.