Podoplanin Protein, Rat (HEK293, hFc)

Podoplanin, a multifaceted protein, orchestrates diverse cellular functions related to migration and adhesion through its interactions with various partners. In developmental processes, it contributes to the separation of blood and lymphatic vessels by binding CLEC1B, activating platelets, and inducing platelet activation or aggregation. Conversely, its interaction with CD9 attenuates platelet aggregation and pulmonary metastasis induced by Podoplanin. Furthermore, Podoplanin plays a crucial role in epithelial-mesenchymal transition (EMT) by promoting ERZ phosphorylation and triggering RHOA activation through interactions with MSN or EZR, leading to increased cell migration and invasiveness. Its binding with CD44 facilitates directional cell migration in epithelial and tumor cells. Within lymph nodes, Podoplanin controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and actomyosin contraction by maintaining ERM proteins (EZR, MSN, and RDX) and MYL9 activation. Engagement with CLEC1B promotes FRC relaxation by blocking lateral membrane interactions. Additionally, Podoplanin participates in connecting lymphatic endothelium to the ECM through binding with LGALS8. In keratinocytes, it induces morphological changes, including an elongated shape and increased motility. Podoplanin also regulates invadopodia stability and maturation in tumor cells, influencing extracellular matrix degradation. Moreover, it is essential for normal lung cell proliferation and alveolus formation at birth. Podoplanin exhibits homodimeric structure and interacts with various proteins, including CLEC1B, CD9, LGALS8, HSPA9, CD44, MSN, EZR, and CCL21, playing a critical role in mediating diverse cellular functions.