Similar and Distinct Properties of MUPP1 and Patj, Two Homologous PDZ Domain-Containing Tight-Junction Proteins

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Published inMolecular and Cellular Biology Vol. 29; no. 9; pp. 2372 - 2389
Main Authors Adachi, Makoto, Hamazaki, Yoko, Kobayashi, Yuka, Itoh, Masahiko, Tsukita, Sachiko, Furuse, Mikio, Tsukita, Shoichiro
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.05.2009
Taylor & Francis
American Society for Microbiology (ASM)
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Abstract 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       
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
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/19255144$$D View this record in MEDLINE/PubMed
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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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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...
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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
Volume 29
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