Proteomics

Dataset Information

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Syntaxin 5 determines Weibel-Palade body size and Von Willebrand factor secretion by controlling Golgi architecture


ABSTRACT: Abstract Von Willebrand factor (VWF) is a multimeric hemostatic protein primarily synthesized in endothelial cells (ECs). VWF is stored in endothelial storage organelles, the Weibel-Palade bodies (WPBs), whose biogenesis strongly depends on VWF anterograde trafficking and Golgi architecture. Elongated WPB morphology is correlated to longer VWF strings with better adhesive properties. We previously identified the SNARE SEC22B, which is involved in anterograde ER-to-Golgi transport, as a novel regulator of WPB elongation. To elucidate novel determinants of WPB morphology we explored endothelial SEC22B interaction partners in a mass spectrometry-based approach, identifying the Golgi SNARE Syntaxin 5 (STX5). We established STX5 knockdown in ECs using shRNA-dependent silencing and analyzed WPB and Golgi morphology, using confocal and electron microscopy. STX5-depleted ECs exhibited extensive Golgi fragmentation and decreased WPB length, which was associated with reduced intracellular VWF levels, and impaired stimulated VWF secretion. However, the secretion incompetent organelles in shSTX5 cells maintained WPB markers such as Angiopoietin 2, P-selectin, Rab27A, and CD63. Taken together, our study has identified SNARE protein STX5 as a novel regulator of WPB biogenesis

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Cell, Endothelial Cell

SUBMITTER: Arie Hoogendijk  

LAB HEAD: Maartje van den Biggelaar

PROVIDER: PXD027516 | Pride | 2022-01-27

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
HUVEC_GFP_GFPbeads_1.raw Raw
HUVEC_GFP_GFPbeads_2.raw Raw
HUVEC_GFP_GFPbeads_3.raw Raw
HUVEC_SEC22BGFP_CTRLbeads_1.raw Raw
HUVEC_SEC22BGFP_CTRLbeads_2.raw Raw
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Publications

Syntaxin 5 determines Weibel-Palade body size and von Willebrand factor secretion by controlling Golgi architecture.

Kat Marije M   Karampini Ellie E   Hoogendijk Arie J AJ   Bürgisser Petra E PE   Mulder Aat A AA   Van Alphen Floris P J FPJ   Olins Jenny J   Geerts Dirk D   Van den Biggelaar Maartje M   Margadant Coert C   Voorberg Jan J   Bierings Ruben R  

Haematologica 20220801 8


Von Willebrand factor (VWF) is a multimeric hemostatic protein primarily synthesized in endothelial cells. VWF is stored in endothelial storage organelles, the Weibel-Palade bodies (WPB), whose biogenesis strongly depends on VWF anterograde trafficking and Golgi architecture. Elongated WPB morphology is correlated to longer VWF strings with better adhesive properties. We previously identified the SNARE SEC22B, which is involved in anterograde endoplasmic reticulum-to-Golgi transport, as a novel  ...[more]

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