Zheng, J, Furness, D, Duan, C, Miller, KK, Edge, RM, Chen, J, Homma, K, Hackney, CM, Dallos, P and Cheatham, MA (2013) Marshalin, a microtubule minus-end binding protein, regulates cytoskeletal structure in the organ of Corti. Biology Open, 2 (11). 1192 -1202.

Marshalin, a microtubule minus-end binding protein, regulates cytoskeletal structure in the organ of Corti.pdf - Published Version
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Dramatic structural changes in microtubules (MT) and the assembly of complicated intercellular connections are seen during the development of the cellular matrix of the sense organ for hearing, the organ of Corti. This report examines the expression of marshalin, a minus-end binding protein, during this process of cochlear development. We discovered that marshalin is abundantly expressed in both sensory hair cells and supporting cells. In the adult, prominent marshalin expression is observed in the cuticular plates of hair cells and in the noncentrosomal MT organization centers (MTOC) of Deiters' and pillar cells. Based upon differences in marshalin expression patterns seen in the organ of Corti, we identified eight isoforms ranging from 863 to 1280 amino acids. mRNAs/proteins associated with marshalin's isoforms are detected at different times during development. These isoforms carry various protein-protein interacting domains, including coiled-coil (CC), calponin homology (CH), proline-rich (PR), and MT-binding domains, referred to as CKK. We, therefore, examined membranous organelles and structural changes in the cytoskeleton induced by expressing two of these marshalin isoforms in vitro. Long forms containing CC and PR domains induce thick, spindle-shaped bundles, whereas short isoforms lacking CC and PR induce more slender variants that develop into densely woven networks. Together, these data suggest that marshalin is closely associated with noncentrosomal MTOCs, and may be involved in MT bundle formation in supporting cells. As a scaffolding protein with multiple isoforms, marshalin is capable of modifying cytoskeletal networks, and consequently organelle positioning, through interactions with various protein partners present in different cells.

Item Type: Article
Additional Information: This is the final published version of the article (version of record). It first appeared online via [insert publisher name] at [insert hyperlink]. Please refer to any applicable terms of use of the publisher.
Uncontrolled Keywords: CAMSAP3, Cochlea, Microtubule minus-end binding protein, Nezha, Noncentrosomal MTOC, Patronin
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Natural Sciences > School of Life Sciences
Related URLs:
Depositing User: Symplectic
Date Deposited: 05 May 2017 14:32
Last Modified: 05 May 2017 14:53
URI: https://eprints.keele.ac.uk/id/eprint/3351

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