Bridging integrator 2 (BIN2)

Bridging integrator 2 (BIN2) is a BAR domain-containing adaptor protein that primarily mediates membrane remodeling in hematopoietic cells[1][3][5]. Its N-BAR domain directs it to actin-rich regions of the plasma membrane, where BIN2 interacts with phospholipids and shapes membrane curvature, especially in immune cells[1]. BIN2’s C-terminus selectively interacts with multiple SH3 domain proteins, contributing to its ability to modulate the formation and dynamics of podosomes—adhesion structures important for cell motility, adhesion, and phagocytosis[1][3][5]. Overexpression of BIN2 promotes podosome formation and cell migration, while loss or silencing of BIN2 reduces migration and enhances phagocytosis, highlighting its regulatory role in cytoskeletal organization[1][2][3]. Experimental and structural data indicate that BIN2 is especially important in leukocytes, where it influences innate immune functions such as phagocytosis and migration, and it has also been loosely associated with breast cancer[3]. BIN2 is not a classic therapeutic target such as an enzyme, receptor, or transporter but rather functions as a scaffolding/adaptor protein involved in cytoskeletal and membrane dynamics. There is currently no evidence for approved or clinical drugs directly targeting BIN2, nor are established biomarkers or specific safety concerns directly linked to targeting this protein[1][2][3][5].

Other names

BRAP-1Breast cancer-associated protein 1BRAP1bridging integrator 2