A point mutation in Semaphorin 4A associates with defective endosomal sorting and causes retinal degeneration

نویسندگان

  • Satoshi Nojima
  • Toshihiko Toyofuku
  • Hiroyuki Kamao
  • Chie Ishigami
  • Jun Kaneko
  • Tatsusada Okuno
  • Hyota Takamatsu
  • Daisuke Ito
  • Sujin Kang
  • Tetsuya Kimura
  • Yuji Yoshida
  • Keiko Morimoto
  • Yohei Maeda
  • Atsushi Ogata
  • Masahito Ikawa
  • Eiichi Morii
  • Katsuyuki Aozasa
  • Junichi Takagi
  • Masayo Takahashi
  • Atsushi Kumanogoh
چکیده

Semaphorin 4A (Sema4A) has an essential role in photoreceptor survival. In humans, mutations in Sema4A are thought to contribute to retinal degenerative diseases. Here we generate a series of knock-in mouse lines with corresponding mutations (D345H, F350C or R713Q) in the Sema4A gene and find that Sema4A(F350C) causes retinal degeneration phenotypes. The F350C mutation results in abnormal localization of the Sema4A protein, leading to impaired endosomal sorting of molecules indispensable for photoreceptor survival. Additionally, protein structural modelling reveals that the side chain of the 350th amino acid is critical to retain the proper protein conformation. Furthermore, Sema4A gene transfer successfully prevents photoreceptor degeneration in Sema4A(F350C/F350C) and Sema4A(-/-) mice. Thus, our findings not only indicate the importance of the Sema4A protein conformation in human and mouse retina homeostasis but also identify a novel therapeutic target for retinal degenerative diseases.

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عنوان ژورنال:

دوره 4  شماره 

صفحات  -

تاریخ انتشار 2013