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Pleckstrin homology-like domain family B member 2 is a multi-domain cytoplasmic protein characterized by two coiled-coil domains and a pleckstrin homology (PH) domain. It functions as a key adaptor that links the cell cortex to microtubules by anchoring microtubule plus-ends at the plasma membrane through PI(3,4,5)P₃ binding. This anchoring promotes microtubule stability, regulates focal adhesion disassembly, and facilitates directed cell migration and polarity. In neurons, PHLDB2 is pivotal for dendritic spine maturation and synaptic plasticity via interaction with drebrin A. It also organizes cytoskeletal platforms for cell motility, interacting with components such as CLASPs, ERC1a, liprin-α1, Amotl2, and FLNC. While not currently considered a direct therapeutic target, altered expression is correlated with prognosis in several breast cancer subtypes, making it a candidate biomarker for disease progression.
Not applicable (no drugs directly target PHLDB2)
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