Proteomic Analysis of Microtubule-associated Proteins during Macrophage Activation*□S

Classical activation of macrophages induces a wide range of signaling and vesicle trafficking events to produce a more aggressive cellular phenotype. The microtubule (MT) cytoskeleton is crucial for the regulation of immune responses. In the current study, we used a large scale proteomics approach to analyze the change in protein composition of the MT-associated protein (MAP) network by macrophage stimulation with the inflammatory cyto-kine interferon- and the endotoxin lipopolysaccharide. Overall the analysis identified 409 proteins that bound directly or indirectly to MTs. Of these, 52 were up-regu-lated 2-fold or greater and 42 were down-regulated 2-fold or greater after interferon-/lipopolysaccharide stimula-tion. Bioinformatics analysis based on publicly available binary protein interaction data produced a putative inter