Disease relevance of MPDZ

• A 5-HT(2C) receptor-dependent unmasking of a C-terminal vesicular stomatitis virus epitope of MUPP1 suggests that the interaction triggers a conformational change within the MUPP1 protein [1].
• We conclude that low levels of tight junction plaque molecules, such as ZO-1 and MUPP-1, in breast cancer are associated with poor patients prognosis [2].

High impact information on MPDZ

• Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2 [3].
• The highest MUPP1 mRNA levels were found in all cerebral cortical layers, the hippocampus, the granular layer of the dentate gyrus, as well as the choroid plexus, where 5-HT(2C) receptors are highly enriched [1].
• Co-immunoprecipitations of MUPP1 and 5-HT(2C) receptors from transfected COS-7 cells and from rat choroid plexus verified this interaction in vivo [1].
• These results suggest that in the context of HPV-induced transformation Dlg, MAGI-1 and MUPP1 can function as tumour suppressors [4].
• Q-PCR revealed a reduction in the levels of ZO-1 and MUPP-1 in patients with disease recurrence [2].

Biological context of MPDZ

• Cloning and characterization of MUPP1, a novel PDZ domain protein [5].
• The MUPP1 gene is localized on human chromosome 9p24-p22 [5].
• The protein, named MUPP1 (multi-PDZ-domain protein), contains thirteen PDZ domains and no obvious catalytic domain; it is related to hINADL and a putative C. elegans polypeptide referred to as C52A11.4 containing six or ten PDZ domains, respectively [5].

Anatomical context of MPDZ

• The urethra (UPP, MUPP, instability, LPP) [6].

Associations of MPDZ with chemical compounds

• The presentations were (1) The Multiple PDZ Domain Protein May Mediate Genetic Differences in Ethanol Withdrawal Severity Via Interaction With 5-HT2 Receptors, by Matthew T [7].

References