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http://dx.doi.org/10.5352/JLS.2016.26.3.282

Wdpcp, a Protein that Regulates Planar Cell Polarity, Interacts with Multi‐PDZ Domain Protein 1 (MUPP1) through a PDZ Interaction  

Jang, Won Hee (Department of Biochemistry, Inje University College of Medicine)
Jeong, Young Joo (Department of Biochemistry, Inje University College of Medicine)
Choi, Sun Hee (Department of Biochemistry, Inje University College of Medicine)
Yea, Sung Su (Department of Biochemistry, 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, Inje University College of Medicine)
Publication Information
Journal of Life Science / v.26, no.3, 2016 , pp. 282-288 More about this Journal
Abstract
Protein-protein interactions regulate the subcellular localization and function of receptors, enzymes, and cytoskeletal proteins. Proteins containing the postsynaptic density-95/disks large/zonula occludens-1 (PDZ) domain have potential to act as scaffolding proteins and play a pivotal role in various processes, such as synaptic plasticity, neural guidance, and development, as well as in the pathophysiology of many diseases. Multi-PDZ domain protein 1 (MUPP1), which has 13 PDZ domains, has a scaffolding function in the clustering of surface receptors, organization of signaling complexes, and coordination of cytoskeletal dynamics. However, the cellular function of MUPP1 has not been fully elucidated. In the present study, a yeast two-hybrid system was used to identify proteins that interacted with the N-terminal PDZ domain of MUPP1. The results revealed an interaction between MUPP1 and Wdpcp (formerly known as Fritz). Wdpcp was identified as a planar cell polarity (PCP) effector, which is known to have a role in collective cell migration and cilia formation. Wdpcp bound to the PDZ1 domain but not to other PDZ domains of MUPP1. The C-terminal end of Wdpcp was essential for the interaction with MUPP1 in the yeast two-hybrid assay. This interaction was further confirmed in a glutathione S-transferase (GST) pull-down assay. When coexpressed in HEK-293T cells, Wdpcp was coimmunoprecipitated with MUPP1. In addition, MUPP1 colocalized with Wdpcp at the same subcellular region in cells. Collectively, these results suggest that the MUPP1-Wdpcp interaction could modulate actin cytoskeleton dynamics and polarized cell migration.
Keywords
MUPP1; PDZ domain; Planar cell polarity (PCP); scaffolding protein; Wdpcp;
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