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KMID : 0613820140240080820
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Journal of Life Science
2014 Volume.24 No. 8 p.820 ~ p.826
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Parkin Interacts with the PDZ Domain of Multi-PDZ Domain Protein MUPP1
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Jang Won-Hee
Joung Young-Ju
Choi Sun-Hee
Lee Won-Hee
Kim Moo-Seong
Kim Sang-Jin
Urm Sang-Hwa
Moon Il-Soo
Seog Dae-Hyun
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Abstract
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The localization to specific subcellular sites and the regulation of cell surface receptors and channels are crucial for proper functioning. Postsynaptic density-95/Disks large/Zonula occludens-1 (PDZ)-domain is involved in recognition of and interaction between various proteins, by which the localization and the regulation are mediated. Multi-PDZ domain protein 1 (MUPP1) contains 13 PDZ domains. MUPP1 serves a scaffolding function for structure proteins and signaling proteins, but the mechanism how MUPP1 is stabilized and signalized 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 Parkin. Parkin is an E3 ubiquitin ligase. Loss-of-function mutations of Parkin gene are known to cause an autosomal recessive juvenile parkinsonism. Parkin bound to the 12th PDZ domain, but not to other PDZ domains of MUPP1. The C-terminal end of Parkin has a type II PDZ-association motif, which was essential for the interaction with MUPP1 in the yeast two-hybrid assay. When co-expressed in HEK-293T cells, Parkin co-localized with MUPP1. When co-expressed with ubiquitin in HEK-293T cells, MUPP1 has been strongly ubiquitinated by Parkin. These findings collectively suggest that MUPP1 is a novel substrate of Parkin and its function or stability could be modulated by Parkin-mediated ubiquitination.
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KEYWORD
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MUPP1, Parkin, PDZ domain, protein-protein interaction, ubiquitination
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