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10.1002/pro.3089 http://scihub22266oqcxt.onion/10.1002/pro.3089 C5326560!5326560 !27879017     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27879017 &cmd=llinks): Failed to open stream: HTTP request failed! 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Domain architecture of vasohibins required for their chaperone-dependent unconventional extracellular release |pdf=|usr=}}{{27879017 }} gab.com Text Domain architecture of vasohibins required for their chaperone-dependent unconventional extracellular release JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=27879017 #FOAvip 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(91-180) and VASH2(80-169) , regulate the cytosolic punctate structure formation in the absence of SVBP. We also demonstrate that SVBP form a complex with VASH1 through the VASH1(274-282) (SIa), VASH1(139-144) (SIb), and VASH1(133-137) (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. Twit Text FOAVip Domain architecture of vasohibins required for their chaperone-dependent unconventional extracellular release ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=27879017 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27879017 #FOAvip English Wikipedia <ref>{{Cite pmid|27879017 }}</ref> Domain architecture of vasohibins required for their chaperone-dependent unconventional extracellular release #MMPMID27879017 Kadonosono T ; Yimchuen W ; Tsubaki T ; Shiozawa T ; Suzuki Y ; Kuchimaru T ; Sato Y ; Kizaka-Kondoh S Protein Sci 2017[Mar]; 26 (3 ): 452-463 PMID27879017 show ga 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(91-180) and VASH2(80-169) , regulate the cytosolic punctate structure formation in the absence of SVBP. We also demonstrate that SVBP form a complex with VASH1 through the VASH1(274-282) (SIa), VASH1(139-144) (SIb), and VASH1(133-137) (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. |Angiogenic Proteins/chemistry/genetics/*metabolism [MESH] |Carrier Proteins/chemistry/genetics/*metabolism [MESH] |Cell Cycle Proteins/chemistry/genetics/*metabolism [MESH] |Cytosol/chemistry/metabolism [MESH] |HeLa Cells [MESH] |Humans [MESH] |Molecular Chaperones/chemistry/genetics/*metabolism [MESH]Domain architecture of vasohibins required for their chaperone-depende(epmc).pdf DeepDyve Pubget Overpricing