2017年3月1日
Domain architecture of vasohibins required for their chaperone-dependent unconventional extracellular release
Protein Science
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- 巻
- 26
- 号
- 3
- 開始ページ
- 452
- 終了ページ
- 463
- 記述言語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1002/pro.3089
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 VASH1 and VASH2 , regulate the cytosolic punctate structure formation in the absence of SVBP. We also demonstrate that SVBP form a complex with VASH1 through the VASH1 (SIa), VASH1 (SIb), and VASH1 (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. 91–180 80–169 274–282 139-144 133–137
- リンク情報
- ID情報
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- DOI : 10.1002/pro.3089
- ISSN : 0961-8368
- eISSN : 1469-896X
- ORCIDのPut Code : 59405048
- PubMed ID : 27879017
- SCOPUS ID : 85012888259