Similar and Distinct Properties of MUPP1 and Patj, Two Homologous PDZ Domain-Containing Tight-Junction Proteins
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Published in | Molecular and Cellular Biology Vol. 29; no. 9; pp. 2372 - 2389 |
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AbstractList | MUPP1 and Patj are both composed of an L27 domain and multiple PDZ domains (13 and 10 domains, respectively) and are localized to tight junctions (TJs) in epithelial cells. Although Patj is known to be responsible for the organization of TJs and epithelial polarity, characterization of MUPP1 is lacking. In this study, we found that MUPP1 and Patj share several binding partners, including JAM1, ZO-3, Pals1, Par6, and nectins (cell-cell adhesion molecules at adherens junctions). MUPP1 and Patj exhibited similar subcellular distributions, and the mechanisms with which they localize to TJs also appear to overlap. Despite these similarities, functional studies have revealed that Patj is indispensable for the establishment of TJs and epithelial polarization, whereas MUPP1 is not. Thus, although MUPP1 and Patj share several molecular properties, their functions are entirely different. We present evidence that the signaling mediated by Pals1, which has a higher affinity for Patj than for MUPP1 and is involved in the activation of the Par6-aPKC complex, is of principal importance for the function of Patj in epithelial cells. Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB |
Author | Masahiko Itoh Shoichiro Tsukita Yoko Hamazaki Yuka Kobayashi Sachiko Tsukita Mikio Furuse Makoto Adachi |
AuthorAffiliation | Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan, 1 Department of Immunology and Cell Biology, Graduate School of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan, 2 Research Unit for Immune Surveillance, RIKEN Research Center for Allergy and Immunology, Yokohama, Kanagawa 230-0045, Japan, 3 Division of Molecular and Cell Biology, Institute for Medical Science, Dokkyo University School of Medicine, Mibu-machi, Tochigi 321-0293, Japan, 4 Laboratory of Biological Science, Graduate School of Frontier Biosciences/Department of Pathology, Graduate School of Medicine, Osaka University, Suita, Osaka 565-0871, Japan, 5 Division of Cellular and Molecular Medicine, Kobe University Graduate School of Medicine, Chuo-ku, Kobe 650-0017, Japan 6 |
AuthorAffiliation_xml | – name: Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan, 1 Department of Immunology and Cell Biology, Graduate School of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan, 2 Research Unit for Immune Surveillance, RIKEN Research Center for Allergy and Immunology, Yokohama, Kanagawa 230-0045, Japan, 3 Division of Molecular and Cell Biology, Institute for Medical Science, Dokkyo University School of Medicine, Mibu-machi, Tochigi 321-0293, Japan, 4 Laboratory of Biological Science, Graduate School of Frontier Biosciences/Department of Pathology, Graduate School of Medicine, Osaka University, Suita, Osaka 565-0871, Japan, 5 Division of Cellular and Molecular Medicine, Kobe University Graduate School of Medicine, Chuo-ku, Kobe 650-0017, Japan 6 |
Author_xml | – sequence: 1 givenname: Makoto surname: Adachi fullname: Adachi, Makoto email: ada@mfour.med.kyoto-u.ac.jp organization: Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku – sequence: 2 givenname: Yoko surname: Hamazaki fullname: Hamazaki, Yoko organization: Department of Immunology and Cell Biology, Graduate School of Medicine, Kyoto University, Sakyo-ku – sequence: 3 givenname: Yuka surname: Kobayashi fullname: Kobayashi, Yuka organization: Research Unit for Immune Surveillance, RIKEN Research Center for Allergy and Immunology, Yokohama – sequence: 4 givenname: Masahiko surname: Itoh fullname: Itoh, Masahiko organization: Division of Molecular and Cell Biology, Institute for Medical Science, Dokkyo University School of Medicine, Mibu-machi – sequence: 5 givenname: Sachiko surname: Tsukita fullname: Tsukita, Sachiko organization: Laboratory of Biological Science, Graduate School of Frontier Biosciences/Department of Pathology, Graduate School of Medicine, Osaka University, Suita – sequence: 6 givenname: Mikio surname: Furuse fullname: Furuse, Mikio organization: Division of Cellular and Molecular Medicine, Kobe University Graduate School of Medicine, Chuo-ku – sequence: 7 givenname: Shoichiro surname: Tsukita fullname: Tsukita, Shoichiro organization: Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Corresponding author. Mailing address: Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. Phone: 81-75-753-4375. Fax: 81-75-753-4660. E-mail: ada@mfour.med.kyoto-u.ac.jp |
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Mendeley... MUPP1 and Patj are both composed of an L27 domain and multiple PDZ domains (13 and 10 domains, respectively) and are localized to tight junctions (TJs) in... |
SourceID | pubmedcentral proquest crossref pubmed informaworld highwire |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 2372 |
SubjectTerms | Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Animals Carrier Proteins - genetics Carrier Proteins - metabolism Cell Adhesion Molecules - genetics Cell Adhesion Molecules - metabolism Cell Line Epithelial Cells - cytology Epithelial Cells - metabolism Humans Membrane Proteins - genetics Membrane Proteins - metabolism Mice Nectins Nucleoside-Phosphate Kinase - genetics Nucleoside-Phosphate Kinase - metabolism PDZ Domains Phosphoproteins - genetics Phosphoproteins - metabolism Protein Binding Receptors, Cell Surface - genetics Receptors, Cell Surface - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RNA Interference Signal Transduction - physiology Tight Junction Proteins Tight Junctions - metabolism Zonula Occludens Proteins Zonula Occludens-1 Protein |
Title | Similar and Distinct Properties of MUPP1 and Patj, Two Homologous PDZ Domain-Containing Tight-Junction Proteins |
URI | http://mcb.asm.org/content/29/9/2372.abstract https://www.tandfonline.com/doi/abs/10.1128/MCB.01505-08 https://www.ncbi.nlm.nih.gov/pubmed/19255144 https://search.proquest.com/docview/67128418 https://pubmed.ncbi.nlm.nih.gov/PMC2668367 |
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