Domain architecture of vasohibins required for their chaperone-dependent unconventional extracellular release

Tetsuya Kadonosono, Wanaporn Yimchuen, Takuya Tsubaki, Tadashi Shiozawa, Yasuhiro Suzuki, Takahiro Kuchimaru, Yasufumi Sato, Shinae Kizaka-Kondoh

研究成果: Article

5 引用 (Scopus)

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Vasohibins (VASH1 and VASH2) are recently identified regulators of angiogenesis and cancer cell functions. They are secreted proteins without any classical secretion signal sequences, and are thought to be secreted instead via an unconventional protein secretion (UPS) pathway in a small vasohibin-binding protein (SVBP)-dependent manner. However, the precise mechanism of SVBP-dependent UPS is poorly understood. In this study, we identified a novel UPS regulatory system in which essential domain architecture (VASH-PS) of VASHs, comprising regions VASH191–180 and VASH280–169, regulate the cytosolic punctate structure formation in the absence of SVBP. We also demonstrate that SVBP form a complex with VASH1 through the VASH1274–282 (SIa), VASH1139-144 (SIb), and VASH1133–137 (SIc), leading to the dispersion in the cytosol and extracellular release of VASH1. The amino acid sequences of VASH-SIa and VASH-PS, containing SIb and SIc, are highly conserved among VASH family members in vertebrates, suggesting that SVBP-dependent UPS may be common within the VASH family. This novel UPS regulatory system may open up new avenues for understanding fundamental protein secretion in vertebrates.

元の言語English
ページ(範囲)452-463
ページ数12
ジャーナルProtein Science
26
発行部数3
DOI
出版物ステータスPublished - 2017 3 1

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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    Kadonosono, T., Yimchuen, W., Tsubaki, T., Shiozawa, T., Suzuki, Y., Kuchimaru, T., Sato, Y., & Kizaka-Kondoh, S. (2017). Domain architecture of vasohibins required for their chaperone-dependent unconventional extracellular release. Protein Science, 26(3), 452-463. https://doi.org/10.1002/pro.3089