Podoplanin Protein, Human (HEK293, His)

Podoplanin Protein emerges as a multifaceted regulator, exerting diverse effects on cell migration and adhesion through interactions with various partners. During development, Podoplanin plays a crucial role in the separation of blood and lymphatic vessels by binding to CLEC1B, triggering platelet activation and aggregation. Conversely, its interaction with CD9 attenuates platelet aggregation induced by Podoplanin. The protein, through interactions with MSN or EZR, promotes epithelial-mesenchymal transition (EMT), leading to increased cell migration and invasiveness. Binding with CD44 facilitates directional cell migration in epithelial and tumor cells. In 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. Podoplanin also participates in connecting the lymphatic endothelium to the surrounding ECM through its interaction with LGALS8. In keratinocytes, Podoplanin induces morphological changes, increased motility, and decreased cell adhesion. Furthermore, Podoplanin regulates invadopodia stability and maturation in tumor cells, contributing to efficient ECM degradation. The protein is homodimeric and interacts with a range of partners, including CLEC1B, CD9, LGALS8, CD44, MSN, EZR, and CCL21, showcasing its intricate involvement in various cellular processes and signaling pathways. Further research is crucial to unravel the precise molecular mechanisms and broader implications of Podoplanin in these diverse cellular functions.