Neuronal cell-surface protein neurexin 1 interaction with multi-PDZ domain protein MUPP1

Jang, Won Hee; Choi, Sun Hee; Jeong, Joo Young; Park, Jung-Hwa; Kim, Sang-Jin; Seog, Dae‐Hyun

doi:10.1080/09168451.2014.890031

Cited by 7 publications

(7 citation statements)

References 13 publications

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“…1C, the MUPP1 and muskelin interaction was impaired by the C-terminal deletion and the substitution of the last C-terminal residue of muskelin. These results indicate that MUPP1 and muskelin interact each other through their PDZ domain and PDZ-association motif, respectively, similar to the previously described class II PDZ interaction [16,26].…”

Section: Plasmid Constructssupporting

confidence: 85%

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

Jang¹,

Jeong²,

Choi³

et al. 2015

Journal of Life Science

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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 3 rd 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.

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Section: Plasmid Constructssupporting

confidence: 85%

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

Jang¹,

Jeong²,

Choi³

et al. 2015

Journal of Life Science

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“…These results indicate that MUPP1 and Wdpcp interact with each other through its PDZ domain and PDZ-binding motif, respectively, consistent with the previously described class II PDZ interaction [26]. Next, we compared the binding of Wdpcp to MUPP1 with those of two known MUPP1 interacting proteins, muskelin and neurexin 1 [15,16]. A yeast two-hybrid assay ( Fig.…”

Section: Identification Of Mupp1 Interacting Proteins By Yeast Two-hysupporting

confidence: 82%

“…MUPP1 is expressed in the brain, enriched in synapse, especially in post-synaptic density (PSD) and tight junctions, and has been reported to interact with a variety of integral membrane proteins, including a synaptic adhesion molecule Cadm1 using its PDZ1-5 domain, junctional adhesion molecule-A (JAM-A) using PDZ9, neurexin 1 using PDZ2, and sodium channel Nav1.4, melatonin receptor (MT1), Claudin-1, and γ-aminobutyric acid receptor 2 (GABAR2) using PDZ13 [1,2,3,6,13,16,18]. MUPP1 may act as a scaffold for the proper assembling and localization of its interacting proteins [11].…”

Section: Introductionmentioning

confidence: 99%

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

Jang¹,

Jeong²,

Choi³

et al. 2016

Journal of Life Science

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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.

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“…Various PDZ domains of MUPP1 can bind to diverse target proteins specifically, which is the base of the macromolecular assemblies [15]. MUPP1-PDZ4, the fourth PDZ of the protein, is highly conserved in different species according to amino acid sequences analysis.…”

Section: Discussionmentioning

confidence: 99%

“…Among the transcripts, the longest transcript encodes ∼2000 amino acid-long MUPP1 which is abundant in the brain as well as in several peripheral organs [13]. MUPP1 regulates cell processes such as cytoskeletal organization, cell polarity, cell proliferation, and many signal transduction pathways through its PDZ domains [14,15]. The MUPP1 gene is associated with some human diseases [16,17] and its mutations have been found in human congenital hydrocephalus [18], leber congenital amaurosis, and retinitis pigmentosa [19].…”

Section: Introductionmentioning

confidence: 99%

Biochemical and structural characterization of MUPP1-PDZ4 domain from <italic>Mus musculus</italic>

Zhu¹,

Liu²,

Huang³

et al. 2015

ABBS

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Specific protein-protein interactions are important for biological signal transduction. The postsynaptic density-95, disc-large, and zonulin-1 (PDZ) domain is one of the most abundant protein interaction modules. Multi-PDZ-domain protein 1 (MUPP1), as a scaffold protein, contains 13 PDZ domains and plays an important role in cytoskeletal organization, cell polarity, and cell proliferation. The study on PDZ domain of MUPP1 helps to understand the mechanisms and functions of MUPP1. In the present study, the fourth PDZ domain of MUPP1 (MUPP1-PDZ4) from Mus musculus was cloned, expressed, purified, and characterized. The MUPP1-PDZ4 domain was subcloned into a pET-vector and expressed in Escherichia coli. Affinity chromatography and sizeexclusion chromatography were used to purify the protein. MUPP1-PDZ4 protein was a monomer with a molar mass of 16.4 kDa in solution and had a melting point of 60.3°C. Using the sitting-drop vapor-diffusion method, MUPP1-PDZ4 protein crystals were obtained in a solution ( pH 7.0) containing 2% (v/v) polyethylene glycol 400, 0.1 M imidazole, and 24% (w/v) polyethylene glycol monoethyl ether 5000. Finally, the crystal was diffracted with 1.6 Å resolution. The crystal structure showed that MUPP1-PDZ4 domain contained three α-helices and six β-strands in the core. The GLGI motif, L562/A564 on the β-strand B, and H605/V608/L612 on the α-helix B formed a PDZ binding pocket which could bind to the C-terminal of the binding partners. This biochemical and structural information will provide insights into how PDZ binds to its target peptide and the theoretical foundation for the function of MUPP1.

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Neuronal cell-surface protein neurexin 1 interaction with multi-PDZ domain protein MUPP1

Cited by 7 publications

References 13 publications

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

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

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

Biochemical and structural characterization of MUPP1-PDZ4 domain from <italic>Mus musculus</italic>

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Neuronal cell-surface protein neurexin 1 interaction with multi-PDZ domain protein MUPP1

Cited by 7 publications

References 13 publications

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

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

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

Biochemical and structural characterization of MUPP1-PDZ4 domain from &lt;italic&gt;Mus musculus&lt;/italic&gt;

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Biochemical and structural characterization of MUPP1-PDZ4 domain from <italic>Mus musculus</italic>