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http://dx.doi.org/10.5352/JLS.2014.24.12.1276

Cadms/SynCAMs/Necls/TSLCs Interact with Multi-PDZ Domain Protein MUPP1  

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)
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.24, no.12, 2014 , pp. 1276-1283 More about this Journal
Abstract
Cell adhesion molecules determine the cell-cell binding and the interactions between cells and extracellular signals. Cell-cell junctional complexes, which maintain the structural integrity of tissues, consist of more than 50 proteins including multi-PDZ domain protein 1 (MUPP1). MUPP1 contains 13 postsynaptic density-95/disks large/zonula occludens-1 (PDZ) domains and serves a scaffolding function for transmembrane proteins and cytoskeletal proteins or signaling proteins, but the mechanism how MUPP1 links and stabilizes the juxtamembrane proteins has not yet been 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 cell adhesion molecule 1 (Cadm1, also known as SynCAM1, Necl-2, or TSLC1). Cadm1 bound to the second PDZ domain of MUPP1. The carboxyl (C)-terminal end of Cadm1 has a type II PDZ-association motif (-Y-F-I) which was essential for the interaction with MUPP1 in the yeast two-hybrid assay. MUPP1 also bound to the C-terminal cytoplasmic tail region of other Cadm family members (Cadm2, Cadm3, and Cadm4). In addition, these protein-protein interactions were observed in the glutathione S-transferase (GST) pull-down assay and by co-immunoprecipitation. Anti-MUPP1 antibody co-immunoprecipitated Cadm1 and Cadm4 with MUPP1 from mouse brain extracts. These results suggest that MUPP1 could mediate interaction between Cadms and cytoskeletal proteins.
Keywords
Cadm1 (cell adhesion molecule 1); cell junction; MUPP1 (multi-PDZ domain protein 1); PDZ (postsynaptic density-95/disks large/zonula occludens-1) domain; scaffold protein;
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