GP1BA encodes glycoprotein Ib-alpha (GPIb-α), a platelet surface receptor critical for hemostasis. Functionally, GPIb-α mediates initial platelet adhesion by binding von Willebrand factor (vWF) already engaged with subendothelial components, thereby initiating platelet plug formation 1. The protein signals through both vWF-dependent mechanisms and integrin αIIbβ3-mediated outside-in pathways, with dysregulation of downstream RhoA signaling contributing to platelet dysfunction 1. GP1BA mutations cause Bernard-Soulier syndrome (BSS), a severe inherited bleeding disorder characterized by macrothrombocytopenia, prolonged bleeding, and platelet dysfunction 23. Both biallelic and heterozygous mutations impair platelet generation and vWF binding affinity 21. Heterozygous mutations show distinct pathophysiology with heightened stress fiber formation and RhoA overactivation amenable to ROCK inhibitor therapy, whereas biallelic cases display different molecular mechanisms 1. Clinically, GP1BA variants associate with stroke risk across multiple ancestries, identifying GPIb-α as a potential therapeutic target for thromboembolic disease 4. Additionally, the JAK2 V617F mutation in platelets expressing Gp1ba accelerates arterial thrombosis through enhanced platelet activation and thromboxane-mediated cross-talk 5, suggesting GP1BA's role in prothrombotic states extends beyond classical bleeding disorders.