P-selectin binds to the D'-D3 domains of von Willebrand factor in Weibel-Palade bodies.

@article{Michaux2006PselectinBT,
  title={P-selectin binds to the D'-D3 domains of von Willebrand factor in Weibel-Palade bodies.},
  author={Gr{\'e}goire Michaux and Timothy J. Pullen and Sandra L Haberichter and Daniel F. Cutler},
  journal={Blood},
  year={2006},
  volume={107 10},
  pages={
          3922-4
        }
}
It has recently been shown that the ultralarge platelet-recruiting von Willebrand factor (VWF) strings formed immediately at exocytosis from endothelial cells may be anchored to the cell surface by interaction with the integral membrane protein P-selectin. This finding of a new binding partner for VWF immediately prompts the question which domains of VWF bind to P-selectin. We have exploited the fact that VWF expression in HEK293 cells triggers the formation of Weibel-Palade body-like… 
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Intracellular cotrafficking of factor VIII and von Willebrand factor type 2N variants to storage organelles.
TLDR
The finding that VWF type 2N variants are still capable of cotargeting FVIII to storage granules implies that trafficking of WPB cargo proteins does not necessarily require high-affinity assembly with VWF.
Type II PI4-kinases control Weibel-Palade body biogenesis and von Willebrand factor structure in human endothelial cells
TLDR
This is the first demonstration that lipid kinases can control the biosynthesis of VWF and the formation of WPBs that are capable of full haemostatic function, and it is shown that phosphatidylinositol 4 kinases regulate the formation and function of an endothelial secretory organelle that is crucial for haemOSTasis in mammals.
Inhibitors of the interaction between von Willebrand factor and platelet GPIb/IX/V.
TLDR
The present knowledge on the different classes of drugs targeting the VWF-GPIb interaction is summarized and an account of their level of clinical development is given.
vWF maturation and release are controlled by two regulators of Weibel-Palade body biogenesis: exocyst and BLOC-2.
TLDR
These studies show that while BLOC-2 and exocyst cooperate in WPB formation, only exocystic function in vWF maturation and release are separable, a feature that can be exploited to enhance vWF release.
The unfolded von Willebrand factor response in bloodstream: the self-association perspective
TLDR
Evidence is emerging that lipid rafts also play important roles in various phases of hemostasis and thrombosis and facilitate the interaction between the key signaling molecules.
Selective release of molecules from Weibel-Palade bodies during a lingering kiss.
TLDR
It is shown that WPBs can undergo a form of exocytosis during which VWF and Proregion are retained while smaller molecules, such as IL-8, are released, which is not inextricably associated with secretion of VWF.
The Manifold Cellular Functions of von Willebrand Factor
TLDR
This review summarizes the current knowledge on VWF’s versatile cellular functions and the resulting pathophysiological consequences of their dysregulation.
Solution structure of the factor VIII binding region on von Willebrand factor
TLDR
The high resolution NMR structure of the major FVIII binding region (D') on VWF, and the dynamics and flexibility of its substructure, are presented in this thesis and provide important insights into VWF.
Von Willebrand factor processing.
TLDR
The individual steps of VWF multimer biosynthesis rely on distinct posttranslational modifications at specific pH conditions, which are realized by spatial separation of the involved processes to different cell organelles, including background information on the occurring biochemical reactions.
New light on an old story: von Willebrand factor binding to collagen
TLDR
A novel approach is used to shed new light on the mechanisms by which von Willebrand factor binds collagen and finds that both a mutant VWF lacking the A3 domain and one with a point mutation in A3 were able to bind collagen through the A1 domain under conditions of flow.
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References

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TLDR
P-selectin may anchor ULVWF strings to endothelial cells and facilitate their cleavage by ADAMTS13, which is shown to be important for its rapid proteolysis.
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TLDR
A system for examining the ability of VWF to drive both the formation of a storage compartment and the function of that compartment with respect to regulated secretion is described and it is found that all 3 mutants can, to some extent, make pseudo-WPBs that recruit appropriate membrane proteins and that are responsive to secretagogues.
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TLDR
The data show that vWF pseudogranules specifically recruit a subset of membrane proteins, and that in a process explicitly driven by the Pseudogranule content, the active recruitment of at least one component of the pseudog Granule membrane is dependent on residues of P-selectin that are cytosolic and therefore unable to directly interact with vWF.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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