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Wdpcp, a Protein that Regulates Planar Cell Polarity, Interacts with Multi‐PDZ Domain Protein 1 (MUPP1) through a PDZ Interaction
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  • Journal title : Journal of Life Science
  • Volume 26, Issue 3,  2016, pp.282-288
  • Publisher : Korean Society of Life Science
  • DOI : 10.5352/JLS.2016.26.3.282
 Title & Authors
Wdpcp, a Protein that Regulates Planar Cell Polarity, Interacts with Multi‐PDZ Domain Protein 1 (MUPP1) through a PDZ Interaction
Jang, Won Hee; Jeong, Young Joo; Choi, Sun Hee; Yea, Sung Su; Lee, Won Hee; Kim, Mooseong; Kim, Sang-Jin; Urm, Sang-Hwa; Moon, Il Soo; Seog, Dae-Hyun;
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 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;
 Language
English
 Cited by
 References
1.
Adachi, M., Hamazaki, Y., Kobayashi, Y., Itoh, M., Tsukita, S., Furuse, M. and Tsukita, S. 2009. Similar and distinct properties of MUPP1 and Patj, two homologous PDZ domain-containing tight-junction proteins. Mol. Cell. Biol. 29, 2372-2389. crossref(new window)

2.
Garner, C. C., Nash, J. and Huganir, R. L. 2000. PDZ domains in synapse assembly and signalling. Trends Cell. Biol. 10, 274-280. crossref(new window)

3.
Becamel, C., Figge, A., Poliak, S., Dumuis, A., Peles, E., Bockaert, J., Lubbert, H. and Ullmer, C. 2001. Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10 of the multi-PDZ domain protein MUPP1. J. Biol. Chem. 276, 12974-12982. crossref(new window)

4.
Collier, S., Lee, H., Burgess, R. and Adler, P. 2005. The WD40 repeat protein fritz links cytoskeletal planar polarity to frizzled subcellular localization in the Drosophila epidermis. Genetics 169, 2035-2045. crossref(new window)

5.
Cui, C., Chatterjee, B., Lozito, T. P., Zhang, Z., Francis, R. J., Yagi, H., Swanhart, L. M., Sanker, S., Francis, D., Yu, Q., San Agustin, J. T., Puligilla, C., Chatterjee, T., Tansey, T., Liu, X., Kelley, M. W., Spiliotis, E. T., Kwiatkowski, A. V., Tuan, R., Pazour, G. J., Hukriede, N. A. and Lo, C. W. 2013. Wdpcp, a PCP protein required for ciliogenesis, regulates directional cell migration and cell polarity by direct modulation of the actin cytoskeleton. PLoS Biol. 11, e1001720. crossref(new window)

6.
Dooley, R., Baumgart, S., Rasche, S., Hatt, H. and Neuhaus, E. M. 2009. Olfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1. FEBS J. 276, 7279-7290. crossref(new window)

7.
Doyle, D. A., Lee, A., Lewis, J., Kim, E., Sheng, M. and MacKinnon, R. 1996. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85, 1067-1076

8.
Field, C. M. and Kellogg, D. 1999. Septins: cytoskeletal polymers or signaling GTPases? Trends Cell. Biol. 9, 387-394. crossref(new window)

9.
Garner, C. C., Nash, J. and Huganir, R. L. 2000. PDZ domains in synapse assembly and signalling. Trends Cell. Biol. 10, 274-280. crossref(new window)

10.
Gomperts, S. N. 1996. Clustering membrane proteins: It's all coming together with the PSD-95/SAP90 protein family. Cell 84, 659-662. crossref(new window)

11.
Guillaume, J. L., Daulat, A. M., Maurice, P., Levoye, A., Migaud, M., Brydon, L., Malpaux, B., Borg-Capra, C. and Jockers, R. 2008. The PDZ protein mupp1 promotes Gi coupling and signaling of the Mt1 melatonin receptor. J. Biol. Chem. 283, 16762-16771. crossref(new window)

12.
Guillemot, L., Foglia, A., Paschoud, S., Pulimeno, P. and Citi, S. 2008. The cytoplasmic plaque of tight junctions: a scaffolding and signalling center. Biochim. Biophys. Acta. 1778, 601-613. crossref(new window)

13.
Hamazaki, Y., Itoh, M., Sasaki, H., Furuse, M. and Tsukita, S. 2002. Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interactionwith claudin-1 and junctional adhesion molecule. J. Biol. Chem. 277, 455-461. crossref(new window)

14.
Hirbec, H., Perestenko, O., Nishimune, A., Meyer, G., Nakanishi, S. and Henley, J. M. 2002. The PDZ proteins PICK1, GRIP and Syntenin bind multiple glutamate receptor subtypes. J. Biol. Chem. 277, 15221-15224. crossref(new window)

15.
Jang, W. H., Jeong, Y. J., Choi, S. H., Lee, W. H., Kim, M., Kim, S. H., Urm, S. H., Moon, I. S and Seog, D. H. 2015. Muskelin Interacts with Multi-PDZ Domain Protein 1 (MUPP1) through the PDZ Domain. J. Life Sci. 25. 594-600. crossref(new window)

16.
Jang, W. H., Choi, S. H., Jeong, J. Y., Park, J. H., Kim, S. J. and Seog, D. H. 2014. Neuronal cell-surface protein neurexin 1 interaction with multi-PDZ domain protein MUPP1. Biosci. Biotechnol. Biochem. 78, 644-646. crossref(new window)

17.
Javier, R. T. 2008. Cell polarity proteins: common targets for tumorigenic human viruses. Oncogene 27, 7031-7046. crossref(new window)

18.
Kimber, W. A., Trinkle-Mulcahy, L., Cheung, P., Deak, M., Marsden, L. J. and Kieloch, A. 2002. Evidence that the tandem-pleckstrin-homology-domain-containing protein TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-containing protein MUPP1 in vivo. Biochem. J. 361, 525-536. crossref(new window)

19.
Krapivinsky, G., Medina, I., Krapivinsky, L., Gapon, S. and Clapham, D. E. 2004. SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation. Neuron 43, 563-574. crossref(new window)

20.
Mostowy, S. and Cossart, P. 2012. Septins: the fourth component of the cytoskeleton. Nat. Rev. Mol. Cell Biol. 13. 183-194.

21.
Park, T. J., Kim, S. K. and Wallingford, J. B. 2015. The planar cell polarity effector protein Wdpcp (Fritz) controls epithelial cell cortex dynamics via septins and actomyosin. Biochem. Biophys. Res. Commun. 456. 562-566.

22.
Pearson, H. B., Perez-Mancera, P. A., Dow, L. E., Ryan, A., Tennstedt, P., Bogani, D., Elsum, I., Greenfield, A., Tuveson, D. A., Simon, R. and Humbert, P. O. 2011. SCRIB expression is deregulated in human prostate cancer, and its deficiency in mice promotes prostate neoplasia. J. Clin. Invest. 121, 4257-4267. crossref(new window)

23.
Pei, L., Teves, R. L., Wallace, M. C. and Gurd, J. W. 2001. Transient cerebral ischemia increases tyrosine phosphorylation of the synaptic RAS-GTPase activating protein, SynGAP. J. Cereb. Blood Flow Metab. 21, 955-963.

24.
Ponting, C. P., Phillips, C., Davies, K. E. and Blake, D. J. 1997. PDZ domains: targeting signalling molecules to submembranous sites. Bioessays 19, 469-479. crossref(new window)

25.
Sambrook, J., Fritsch, E. F. and Maniatis, T. 1989. Molecular cloning: a laboratory manual. Cold Spring Habor Laboratory, Cold Spring Habor, New York.

26.
Sheng, M. and Sala, C. 2001. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29. crossref(new window)

27.
Smith, T. F., Gaitatzes, C., Saxena, K. and Neer, E. J. 1999. The WD repeat: a common architecture for diverse functions. Trends Biochem. Sci. 24. 181-185. crossref(new window)

28.
Songyang, Z., Fanning, A. S., Fu, C., Xu, J., Marfatia, S. M. and Chishti, A. H. 1997. Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science 275, 73-77. crossref(new window)

29.
Ullmer, C., Schmuck, K., Figge, A. and Luëbbert, H. 1998. Cloning and characterization of MUPP1, a novel PDZ domain protein. FEBS Lett. 424, 63-68. crossref(new window)

30.
Zhan, L., Rosenberg, A., Bergami, K. C., Yu, M., Xuan, Z., Jaffe, A. B., Allred, C. and Muthuswamy, S. K. 2008. Deregulation of scribble promotes mammary tumorigenesis and reveals a role for cell polarity in carcinoma. Cell 135, 865-878. crossref(new window)