Background of the antigen
MP1 (MEK partner 1) functions as a scaffolding protein in the mitogen activated protein (MAP) kinase signaling pathway. Growth factor induced MAP kinase activation is selectively mediated by the extracellular signal-regulated kinase (ERK) cascade. MAPBPIP (mitogen-activated protein-binding protein-interacting protein), also known as p14 and late endosomal/lysosomal MP1-interacting protein, functions as an adaptor protein augmenting the regulation of the MAP kinase cascade. Partner proteins MAPBPIP and MP1 are structurally almost identical each with a five-stranded ∫-sheet flanked between a two-helix and one-helix layer. MAPBPIP compels the recruitment of MP1 to late endosomes where they form a very stable heterodimeric complex required for ERK activation on endosomes. Knockdown of the individual proteins in the MP1/MAPBPIP complex resulted in decreased expression of the partner proteins which implies greater stability of the heterodimeric complex than either MP1 or MAPBPIP individually. Early research suggests the MP1-MAPBPIP-MEK-1 signaling complex may be critical in the regulation of tissue homeostasis.
