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Maekawa M, Tanigawa K, Sakaue T, et al. Cullin-3 and its adaptor protein ANKFY1 determine the surface level of integrin β1 in endothelial cells. Biol Open. 2017;6(11):1707-1719doi: 10.1242/bio.029579.
Maekawa, M., Tanigawa, K., Sakaue, T., Hiyoshi, H., Kubota, E., Joh, T., Watanabe, Y., Taguchi, T., & Higashiyama, S. (2017). Cullin-3 and its adaptor protein ANKFY1 determine the surface level of integrin β1 in endothelial cells. Biology open, 6(11), 1707-1719. https://doi.org/10.1242/bio.029579
Maekawa, Masashi, et al. "Cullin-3 and its adaptor protein ANKFY1 determine the surface level of integrin β1 in endothelial cells." Biology open vol. 6,11 (2017): 1707-1719. doi: https://doi.org/10.1242/bio.029579
Maekawa M, Tanigawa K, Sakaue T, Hiyoshi H, Kubota E, Joh T, Watanabe Y, Taguchi T, Higashiyama S. Cullin-3 and its adaptor protein ANKFY1 determine the surface level of integrin β1 in endothelial cells. Biol Open. 2017 Nov 15;6(11):1707-1719. doi: 10.1242/bio.029579. PMID: 29038302; PMCID: PMC5703617.
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Biol Open. 2017 Nov 15;6(11):1707-1719. doi: 10.1242/bio.029579.

Cullin-3 and its adaptor protein ANKFY1 determine the surface level of integrin β1 in endothelial cells.

Biology open

Masashi Maekawa, Kazufumi Tanigawa, Tomohisa Sakaue, Hiromi Hiyoshi, Eiji Kubota, Takashi Joh, Yuji Watanabe, Tomohiko Taguchi, Shigeki Higashiyama

Affiliations

  1. Division of Cell Growth and Tumor Regulation, Proteo-Science Center, Ehime University, Matsuyama 791-0295, Japan [email protected] [email protected].
  2. Department of Biochemistry and Molecular Genetics, Ehime University Graduate School of Medicine, Matsuyama 791-0295, Japan.
  3. Department of Gastrointestinal Surgery and Surgical Oncology, Ehime University Graduate School of Medicine, Matsuyama 791-0295, Japan.
  4. Division of Cell Growth and Tumor Regulation, Proteo-Science Center, Ehime University, Matsuyama 791-0295, Japan.
  5. Department of Cardiovascular and Thoracic Surgery, Ehime University Graduate School of Medicine, Matsuyama 791-0295, Japan.
  6. Department of Gastroenterology and Metabolism, Nagoya City University Graduate School of Medical Sciences, Nagoya City 467-8601, Japan.
  7. Department of Health Chemistry, Graduate School of Pharmaceutical Science, University of Tokyo, Tokyo 113-0033, Japan.
  8. Pathological Cell Biology Laboratory, Graduate School of Pharmaceutical Science, University of Tokyo, Tokyo 113-0033, Japan.

PMID: 29038302 PMCID: PMC5703617 DOI: 10.1242/bio.029579

Abstract

Angiogenesis, the formation of new blood vessels from the pre-existing vasculature, is related to numerous pathophysiological events. We previously reported that a RING ubiquitin ligase complex scaffold protein, cullin-3 (CUL3), and one of its adaptor proteins, BAZF, regulated angiogenesis in the mouse retina by suppressing Notch signaling. However, the degree of inhibition of angiogenesis was made greater by CUL3 depletion than by BAZF depletion, suggesting other roles of CUL3 in angiogenesis besides the regulation of Notch signaling. In the present study, we found that CUL3 was critical for the cell surface level of integrin β1, an essential cell adhesion molecule for angiogenesis in HUVECs. By siRNA screening of 175 BTBPs, a family of adaptor proteins for CUL3, we found that ANKFY1/Rabankyrin-5, an early endosomal BTBP, was also critical for localization of surface integrin β1 and angiogenesis. CUL3 interacted with ANKFY1 and was required for the early endosomal localization of ANKFY1. These data suggest that CUL3/ANKFY1 regulates endosomal membrane traffic of integrin β1. Our results highlight the multiple roles of CUL3 in angiogenesis, which are mediated through distinct CUL3-adaptor proteins.

© 2017. Published by The Company of Biologists Ltd.

Keywords: Angiogenesis; Cullin-3 (CUL3); Endothelial cells; Integrin; Membrane trafficking

Conflict of interest statement

Competing interestsThe authors declare no competing or financial interests.

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