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http://dx.doi.org/10.5352/JLS.2015.25.5.594

Muskelin Interacts with Multi-PDZ Domain Protein 1 (MUPP1) through the PDZ Domain  

Jang, Won Hee (Department of Biochemistry and u-HARC, Inje University College of Medicine)
Jeong, Young Joo (Department of Biochemistry and u-HARC, Inje University College of Medicine)
Choi, Sun Hee (Department of Biochemistry and u-HARC, Inje University College of Medicine)
Lee, Won Hee (Department of Neurosurgery, Inje University College of Medicine)
Kim, Mooseong (Department of Neurosurgery, Inje University College of Medicine)
Kim, Sang-Jin (Department of Neurology, Inje University College of Medicine)
Urm, Sang-Hwa (Department of Preventive Medicine, Inje University College of Medicine)
Moon, Il Soo (Department of Anatomy & Dongguk Medical Institute, College of Medicine, Dongguk University)
Seog, Dae-Hyun (Department of Biochemistry and u-HARC, Inje University College of Medicine)
Publication Information
Journal of Life Science / v.25, no.5, 2015 , pp. 594-600 More about this Journal
Abstract
Protein-protein interactions have a critical role in the regulation of many cellular functions. Postsynaptic density-95/disks large/zonula occludens-1 (PDZ) domain is one of domains that mediate protein-protein interactions. PDZ domains typically bind to the specific motif at the carboxyl (C)-terminal end of partner proteins. Multi-PDZ domain protein 1 (MUPP1), which has 13 PDZ domains, serves a scaffolding function for structure proteins and signaling proteins, but the cellular function of MUPP1 has not been fully elucidated. We used the yeast two-hybrid system to identify proteins that interact with PDZ domains of MUPP1. We found an interaction between MUPP1 and muskelin. Muskelin was recently identified as a GABAA receptor (GABAAR) α1 subunit binding protein and known to have a role in receptor endocytosis and degradation. Muskelin bound to the 3rd PDZ domain, but not to other PDZ domains of MUPP1. The C-terminal end of muskelin was essential for the interaction with MUPP1 in the yeast two-hybrid assay. When co-expressed in HEK-293T cells, muskelin but not the C-terminal deleted muskelin was co-immunoprecipitated with MUPP1. In addition, MUPP1 co-localized with muskelin at the same subcellular region in cells. These findings collectively suggest that MUPP1 or its interacting proteins could modulate GABAAR trafficking and turnover through the interaction with muskelin.
Keywords
Adaptor protein; MUPP1; muskelin; PDZ domain; protein-protein interaction;
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