論文

査読有り 国際誌
2018年

Assembly of protein complexes restricts diffusion of Wnt3a proteins.

Communications biology
  • Ritsuko Takada
  • ,
  • Yusuke Mii
  • ,
  • Elena Krayukhina
  • ,
  • Yuusuke Maruyama
  • ,
  • Kazuhiro Mio
  • ,
  • Yoshikazu Sasaki
  • ,
  • Takao Shinkawa
  • ,
  • Chan-Gi Pack
  • ,
  • Yasushi Sako
  • ,
  • Chikara Sato
  • ,
  • Susumu Uchiyama
  • ,
  • Shinji Takada

1
開始ページ
165
終了ページ
165
記述言語
英語
掲載種別
DOI
10.1038/s42003-018-0172-x

Members of the Wnt protein family play roles in many aspects of embryogenesis and homeostasis. Despite their biological significance, characteristics of Wnt proteins still remain unclear, mainly due to their insolubility after the removal of serum. Here we examine Wnt proteins in serum-containing media by using analytical ultracentrifugation with a fluorescence detection system. This analysis reveals that Wnt3a assembles into high-molecular-weight complexes that become dissociable by interaction with the extracellular domain of the Frizzled8 receptor or secreted Wnt-binding protein sFRP2. Cross-linking and single-particle analyses of Wnt3a fractionated by gel filtration chromatography show the homo-trimer to be the smallest form of the assembled Wnt3a complexes. Fluorescence correlation spectroscopy and immunohistochemistry reveal that the assembly of Wnt3a complexes restricted their diffusion and signaling range in Xenopus laevis embryos. Thus, we propose that the Wnt diffusion range can be controlled by a balance between the assembly of Wnt complexes and their dissociation.

リンク情報
DOI
https://doi.org/10.1038/s42003-018-0172-x
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/30320232
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6179999
URL
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=MEDLINE&KeyUT=MEDLINE:30320232&KeyUID=MEDLINE:30320232
URL
http://orcid.org/0000-0002-1655-8231

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