Selective binding and transport of protocadherin 15 isoforms by stereocilia unconventional myosins in a heterologous expression system.

Bibliographic Details
Title: Selective binding and transport of protocadherin 15 isoforms by stereocilia unconventional myosins in a heterologous expression system.
Authors: Ballesteros, Angela, Yadav, Manoj, Cui, Runjia, Kurima, Kiyoto, Kachar, Bechara
Source: Scientific Reports; 8/12/2022, Vol. 12 Issue 1, p1-13, 13p
Subject Terms: CADHERINS, HAIR cells, ACTIN, MYOSIN, PROTEINS, HEPATOCYTE growth factor
Abstract: During hair cell development, the mechanoelectrical transduction (MET) apparatus is assembled at the stereocilia tips, where it coexists with the stereocilia actin regulatory machinery. While the myosin-based tipward transport of actin regulatory proteins is well studied, isoform complexity and built-in redundancies in the MET apparatus have limited our understanding of how MET components are transported. We used a heterologous expression system to elucidate the myosin selective transport of isoforms of protocadherin 15 (PCDH15), the protein that mechanically gates the MET apparatus. We show that MYO7A selectively transports the CD3 isoform while MYO3A and MYO3B transports the CD2 isoform. Furthermore, MYO15A showed an insignificant role in the transport of PCDH15, and none of the myosins tested transport PCDH15-CD1. Our data suggest an important role for MYO3A, MYO3B, and MYO7A in the MET apparatus formation and highlight the intricate nature of MET and actin regulation during development and functional maturation of the stereocilia bundle. [ABSTRACT FROM AUTHOR]
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  Data: Selective binding and transport of protocadherin 15 isoforms by stereocilia unconventional myosins in a heterologous expression system.
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  Data: <searchLink fieldCode="AR" term="%22Ballesteros%2C+Angela%22">Ballesteros, Angela</searchLink><br /><searchLink fieldCode="AR" term="%22Yadav%2C+Manoj%22">Yadav, Manoj</searchLink><br /><searchLink fieldCode="AR" term="%22Cui%2C+Runjia%22">Cui, Runjia</searchLink><br /><searchLink fieldCode="AR" term="%22Kurima%2C+Kiyoto%22">Kurima, Kiyoto</searchLink><br /><searchLink fieldCode="AR" term="%22Kachar%2C+Bechara%22">Kachar, Bechara</searchLink>
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  Data: Scientific Reports; 8/12/2022, Vol. 12 Issue 1, p1-13, 13p
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  Data: <searchLink fieldCode="DE" term="%22CADHERINS%22">CADHERINS</searchLink><br /><searchLink fieldCode="DE" term="%22HAIR+cells%22">HAIR cells</searchLink><br /><searchLink fieldCode="DE" term="%22ACTIN%22">ACTIN</searchLink><br /><searchLink fieldCode="DE" term="%22MYOSIN%22">MYOSIN</searchLink><br /><searchLink fieldCode="DE" term="%22PROTEINS%22">PROTEINS</searchLink><br /><searchLink fieldCode="DE" term="%22HEPATOCYTE+growth+factor%22">HEPATOCYTE growth factor</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: During hair cell development, the mechanoelectrical transduction (MET) apparatus is assembled at the stereocilia tips, where it coexists with the stereocilia actin regulatory machinery. While the myosin-based tipward transport of actin regulatory proteins is well studied, isoform complexity and built-in redundancies in the MET apparatus have limited our understanding of how MET components are transported. We used a heterologous expression system to elucidate the myosin selective transport of isoforms of protocadherin 15 (PCDH15), the protein that mechanically gates the MET apparatus. We show that MYO7A selectively transports the CD3 isoform while MYO3A and MYO3B transports the CD2 isoform. Furthermore, MYO15A showed an insignificant role in the transport of PCDH15, and none of the myosins tested transport PCDH15-CD1. Our data suggest an important role for MYO3A, MYO3B, and MYO7A in the MET apparatus formation and highlight the intricate nature of MET and actin regulation during development and functional maturation of the stereocilia bundle. [ABSTRACT FROM AUTHOR]
– Name: Abstract
  Label:
  Group: Ab
  Data: <i>Copyright of Scientific Reports is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1038/s41598-022-17757-0
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        Text: English
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              Text: 8/12/2022
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