Multiple PDZ domain protein (MUPP1) (MUPP1)

Multiple PDZ domain protein (MUPP1), also known as MPDZ, is a large scaffolding protein containing 13 PDZ domains that serves as a critical organizer of signaling complexes in various tissues [1.1.2, 1.3.1]. It is primarily localized to tight junctions in epithelial cells and postsynaptic densities in neurons, where it facilitates the assembly of multi-protein networks by binding to the C-termini of transmembrane receptors, ion channels, and adhesion molecules [1.2.5, 1.4.2]. MUPP1 interacts with a wide array of partners, including the 5-HT2C serotonin receptor, claudins, and CaMKII, thereby regulating cell polarity, paracellular permeability, and synaptic plasticity [1.1.2, 1.4.1, 1.4.3]. Mutations in the MPDZ gene are a known cause of autosomal recessive congenital hydrocephalus and have been linked to epilepsy and alcohol dependence [1.2.1, 1.2.2, 1.3.1]. Furthermore, MUPP1 is a cellular target for viral oncoproteins such as HPV E6 and Adenovirus E4-ORF1, which inactivate or degrade the protein to promote oncogenic transformation [1.1.1, 1.1.3]. While no approved drugs currently target MUPP1, it is being investigated as a therapeutic node for modulating opioid tolerance and as a potential target for peptide-based inhibitors of protein-protein interactions in cancer and neurological disorders [1.4.1, 1.5.2]. The protein's role in maintaining the blood-brain barrier and epithelial integrity makes it a complex but significant candidate for future drug development [1.2.5, 1.4.3].

Other names

Multi-PDZ domain protein 1Multiple PDZ domain proteinMPDZ9BP-1DKFZp781P216FLJ25909FLJ34626FLJ90240

Scaffolding and protein-protein interaction (PPI) modulation