The Experts below are selected from a list of 38658 Experts worldwide ranked by ideXlab platform
Keiko Mizuno - One of the best experts on this subject based on the ideXlab platform.
-
Involvement of ASIP/PAR-3 in the promotion of epithelial tight Junction Formation.
Journal of cell science, 2002Co-Authors: Tomonori Hirose, Yasushi Izumi, Yoji Nagashima, Yoko Tamai-nagai, Hidetake Kurihara, Tatsuo Sakai, Yukari Suzuki, Tomoyuki Yamanaka, Atsushi Suzuki, Keiko MizunoAbstract:The mammalian protein ASIP/PAR-3 interacts with atypical protein kinase C isotypes (aPKC) and shows overall sequence similarity to the invertebrate proteins C. elegans PAR-3 and Drosophila Bazooka, which are crucial for the establishment of polarity in various cells. The physical interaction between ASIP/PAR-3 and aPKC is also conserved in C. elegans PAR-3 and PKC-3 and in Drosophila Bazooka and DaPKC. In mammals, ASIP/PAR-3 colocalizes with aPKC and concentrates at the tight Junctions of epithelial cells, but the biological meaning of ASIP/PAR-3 in tight Junctions remains to be clarified. In the present study, we show that ASIP/PAR-3 staining distributes to the subapical domain of epithelial cell-cell Junctions, including epithelial cells with less-developed tight Junctions, in clear contrast with ZO-1, another tight-Junction-associated protein, the staining of which is stronger in cells with well-developed tight Junctions. Consistently, immunogold electron microscopy revealed that ASIP/PAR-3 concentrates at the apical edge of tight Junctions, whereas ZO-1 distributes alongside tight Junctions. To clarify the meaning of this characteristic localization of ASIP, we analyzed the effects of overexpressed ASIP/PAR-3 on tight Junction Formation in cultured epithelial MDCK cells. The induced overexpression of ASIP/PAR-3, but not its deletion mutant lacking the aPKC-binding sequence, promotes cell-cell contact-induced tight Junction Formation in MDCK cells when evaluated on the basis of transepithelial electrical resistance and occludin insolubilization. The significance of the aPKC-binding sequence in tight Junction Formation is also supported by the finding that the conserved PKC-phosphorylation site within this sequence, ASIP-Ser827, is phosphorylated at the most apical tip of cell-cell contacts during the initial phase of tight Junction Formation in MDCK cells. Together, our present data suggest that ASIP/PAR-3 regulates epithelial tight Junction Formation positively through interaction with aPKC.
-
involvement of asip par 3 in the promotion of epithelial tight Junction Formation
Journal of Cell Science, 2002Co-Authors: Tomonori Hirose, Yasushi Izumi, Yoji Nagashima, Hidetake Kurihara, Tatsuo Sakai, Yukari Suzuki, Tomoyuki Yamanaka, Atsushi Suzuki, Yoko Tamainagai, Keiko MizunoAbstract:The mammalian protein ASIP/PAR-3 interacts with atypical protein kinase C isotypes (aPKC) and shows overall sequence similarity to the invertebrate proteins C. elegans PAR-3 and Drosophila Bazooka, which are crucial for the establishment of polarity in various cells. The physical interaction between ASIP/PAR-3 and aPKC is also conserved in C. elegans PAR-3 and PKC-3 and in Drosophila Bazooka and DaPKC. In mammals, ASIP/PAR-3 colocalizes with aPKC and concentrates at the tight Junctions of epithelial cells, but the biological meaning of ASIP/PAR-3 in tight Junctions remains to be clarified. In the present study, we show that ASIP/PAR-3 staining distributes to the subapical domain of epithelial cell-cell Junctions, including epithelial cells with less-developed tight Junctions, in clear contrast with ZO-1, another tight-Junction-associated protein, the staining of which is stronger in cells with well-developed tight Junctions. Consistently, immunogold electron microscopy revealed that ASIP/PAR-3 concentrates at the apical edge of tight Junctions, whereas ZO-1 distributes alongside tight Junctions. To clarify the meaning of this characteristic localization of ASIP, we analyzed the effects of overexpressed ASIP/PAR-3 on tight Junction Formation in cultured epithelial MDCK cells. The induced overexpression of ASIP/PAR-3, but not its deletion mutant lacking the aPKC-binding sequence, promotes cell-cell contact-induced tight Junction Formation in MDCK cells when evaluated on the basis of transepithelial electrical resistance and occludin insolubilization. The significance of the aPKC-binding sequence in tight Junction Formation is also supported by the finding that the conserved PKC-phosphorylation site within this sequence, ASIP-Ser827, is phosphorylated at the most apical tip of cell-cell contacts during the initial phase of tight Junction Formation in MDCK cells. Together, our present data suggest that ASIP/PAR-3 regulates epithelial tight Junction Formation positively through interaction with aPKC.
Tomonori Hirose - One of the best experts on this subject based on the ideXlab platform.
-
Involvement of ASIP/PAR-3 in the promotion of epithelial tight Junction Formation.
Journal of cell science, 2002Co-Authors: Tomonori Hirose, Yasushi Izumi, Yoji Nagashima, Yoko Tamai-nagai, Hidetake Kurihara, Tatsuo Sakai, Yukari Suzuki, Tomoyuki Yamanaka, Atsushi Suzuki, Keiko MizunoAbstract:The mammalian protein ASIP/PAR-3 interacts with atypical protein kinase C isotypes (aPKC) and shows overall sequence similarity to the invertebrate proteins C. elegans PAR-3 and Drosophila Bazooka, which are crucial for the establishment of polarity in various cells. The physical interaction between ASIP/PAR-3 and aPKC is also conserved in C. elegans PAR-3 and PKC-3 and in Drosophila Bazooka and DaPKC. In mammals, ASIP/PAR-3 colocalizes with aPKC and concentrates at the tight Junctions of epithelial cells, but the biological meaning of ASIP/PAR-3 in tight Junctions remains to be clarified. In the present study, we show that ASIP/PAR-3 staining distributes to the subapical domain of epithelial cell-cell Junctions, including epithelial cells with less-developed tight Junctions, in clear contrast with ZO-1, another tight-Junction-associated protein, the staining of which is stronger in cells with well-developed tight Junctions. Consistently, immunogold electron microscopy revealed that ASIP/PAR-3 concentrates at the apical edge of tight Junctions, whereas ZO-1 distributes alongside tight Junctions. To clarify the meaning of this characteristic localization of ASIP, we analyzed the effects of overexpressed ASIP/PAR-3 on tight Junction Formation in cultured epithelial MDCK cells. The induced overexpression of ASIP/PAR-3, but not its deletion mutant lacking the aPKC-binding sequence, promotes cell-cell contact-induced tight Junction Formation in MDCK cells when evaluated on the basis of transepithelial electrical resistance and occludin insolubilization. The significance of the aPKC-binding sequence in tight Junction Formation is also supported by the finding that the conserved PKC-phosphorylation site within this sequence, ASIP-Ser827, is phosphorylated at the most apical tip of cell-cell contacts during the initial phase of tight Junction Formation in MDCK cells. Together, our present data suggest that ASIP/PAR-3 regulates epithelial tight Junction Formation positively through interaction with aPKC.
-
involvement of asip par 3 in the promotion of epithelial tight Junction Formation
Journal of Cell Science, 2002Co-Authors: Tomonori Hirose, Yasushi Izumi, Yoji Nagashima, Hidetake Kurihara, Tatsuo Sakai, Yukari Suzuki, Tomoyuki Yamanaka, Atsushi Suzuki, Yoko Tamainagai, Keiko MizunoAbstract:The mammalian protein ASIP/PAR-3 interacts with atypical protein kinase C isotypes (aPKC) and shows overall sequence similarity to the invertebrate proteins C. elegans PAR-3 and Drosophila Bazooka, which are crucial for the establishment of polarity in various cells. The physical interaction between ASIP/PAR-3 and aPKC is also conserved in C. elegans PAR-3 and PKC-3 and in Drosophila Bazooka and DaPKC. In mammals, ASIP/PAR-3 colocalizes with aPKC and concentrates at the tight Junctions of epithelial cells, but the biological meaning of ASIP/PAR-3 in tight Junctions remains to be clarified. In the present study, we show that ASIP/PAR-3 staining distributes to the subapical domain of epithelial cell-cell Junctions, including epithelial cells with less-developed tight Junctions, in clear contrast with ZO-1, another tight-Junction-associated protein, the staining of which is stronger in cells with well-developed tight Junctions. Consistently, immunogold electron microscopy revealed that ASIP/PAR-3 concentrates at the apical edge of tight Junctions, whereas ZO-1 distributes alongside tight Junctions. To clarify the meaning of this characteristic localization of ASIP, we analyzed the effects of overexpressed ASIP/PAR-3 on tight Junction Formation in cultured epithelial MDCK cells. The induced overexpression of ASIP/PAR-3, but not its deletion mutant lacking the aPKC-binding sequence, promotes cell-cell contact-induced tight Junction Formation in MDCK cells when evaluated on the basis of transepithelial electrical resistance and occludin insolubilization. The significance of the aPKC-binding sequence in tight Junction Formation is also supported by the finding that the conserved PKC-phosphorylation site within this sequence, ASIP-Ser827, is phosphorylated at the most apical tip of cell-cell contacts during the initial phase of tight Junction Formation in MDCK cells. Together, our present data suggest that ASIP/PAR-3 regulates epithelial tight Junction Formation positively through interaction with aPKC.
Johannes L. Bos - One of the best experts on this subject based on the ideXlab platform.
-
Cell-cell Junction Formation: the role of Rap1 and Rap1 guanine nucleotide exchange factors.
Biochimica et biophysica acta, 2009Co-Authors: Willem-jan Pannekoek, Matthijs R H Kooistra, Fried J T Zwartkruis, Johannes L. BosAbstract:Rap proteins are Ras-like small GTP-binding proteins that amongst others are involved in the control of cell-cell and cell-matrix adhesion. Several Rap guanine nucleotide exchange factors (RapGEFs) function to activate Rap. These multi-domain proteins, which include C3G, Epacs, PDZ-GEFs, RapGRPs and DOCK4, are regulated by various different stimuli and may function at different levels in Junction Formation. Downstream of Rap, a number of effector proteins have been implicated in Junctional control, most notably the adaptor proteins AF6 and KRIT/CCM1. In this review, we will highlight the latest findings on the Rap signaling network in the control of epithelial and endothelial cell-cell Junctions.
-
Rap1: a key regulator in cell-cell Junction Formation.
Journal of cell science, 2007Co-Authors: Matthijs R H Kooistra, Nadia Dubé, Johannes L. BosAbstract:Rap1 is a Ras-like small GTPase that is activated by many extracellular stimuli and strongly implicated in the control of integrin-mediated cell adhesion. Recent evidence indicates that Rap1 also plays a key role in Formation of cadherin-based cell-cell Junctions. Indeed, inhibition of Rap1 generates immature adherens Junctions, whereas activation of Rap1 tightens cell-cell Junctions. Interestingly, Rap1 guanine nucleotide exchange factors, such as C3G and PDZ-GEF, are directly linked to E-cadherin or to other Junction proteins. Furthermore, several Junction proteins, such as afadin/AF6 and proteins controlling the actin cytoskeleton, function as effectors of Rap1. These findings point to a role of Rap1 in spatial and temporal control of cell-cell Junction Formation.
Yasushi Izumi - One of the best experts on this subject based on the ideXlab platform.
-
Involvement of ASIP/PAR-3 in the promotion of epithelial tight Junction Formation.
Journal of cell science, 2002Co-Authors: Tomonori Hirose, Yasushi Izumi, Yoji Nagashima, Yoko Tamai-nagai, Hidetake Kurihara, Tatsuo Sakai, Yukari Suzuki, Tomoyuki Yamanaka, Atsushi Suzuki, Keiko MizunoAbstract:The mammalian protein ASIP/PAR-3 interacts with atypical protein kinase C isotypes (aPKC) and shows overall sequence similarity to the invertebrate proteins C. elegans PAR-3 and Drosophila Bazooka, which are crucial for the establishment of polarity in various cells. The physical interaction between ASIP/PAR-3 and aPKC is also conserved in C. elegans PAR-3 and PKC-3 and in Drosophila Bazooka and DaPKC. In mammals, ASIP/PAR-3 colocalizes with aPKC and concentrates at the tight Junctions of epithelial cells, but the biological meaning of ASIP/PAR-3 in tight Junctions remains to be clarified. In the present study, we show that ASIP/PAR-3 staining distributes to the subapical domain of epithelial cell-cell Junctions, including epithelial cells with less-developed tight Junctions, in clear contrast with ZO-1, another tight-Junction-associated protein, the staining of which is stronger in cells with well-developed tight Junctions. Consistently, immunogold electron microscopy revealed that ASIP/PAR-3 concentrates at the apical edge of tight Junctions, whereas ZO-1 distributes alongside tight Junctions. To clarify the meaning of this characteristic localization of ASIP, we analyzed the effects of overexpressed ASIP/PAR-3 on tight Junction Formation in cultured epithelial MDCK cells. The induced overexpression of ASIP/PAR-3, but not its deletion mutant lacking the aPKC-binding sequence, promotes cell-cell contact-induced tight Junction Formation in MDCK cells when evaluated on the basis of transepithelial electrical resistance and occludin insolubilization. The significance of the aPKC-binding sequence in tight Junction Formation is also supported by the finding that the conserved PKC-phosphorylation site within this sequence, ASIP-Ser827, is phosphorylated at the most apical tip of cell-cell contacts during the initial phase of tight Junction Formation in MDCK cells. Together, our present data suggest that ASIP/PAR-3 regulates epithelial tight Junction Formation positively through interaction with aPKC.
-
involvement of asip par 3 in the promotion of epithelial tight Junction Formation
Journal of Cell Science, 2002Co-Authors: Tomonori Hirose, Yasushi Izumi, Yoji Nagashima, Hidetake Kurihara, Tatsuo Sakai, Yukari Suzuki, Tomoyuki Yamanaka, Atsushi Suzuki, Yoko Tamainagai, Keiko MizunoAbstract:The mammalian protein ASIP/PAR-3 interacts with atypical protein kinase C isotypes (aPKC) and shows overall sequence similarity to the invertebrate proteins C. elegans PAR-3 and Drosophila Bazooka, which are crucial for the establishment of polarity in various cells. The physical interaction between ASIP/PAR-3 and aPKC is also conserved in C. elegans PAR-3 and PKC-3 and in Drosophila Bazooka and DaPKC. In mammals, ASIP/PAR-3 colocalizes with aPKC and concentrates at the tight Junctions of epithelial cells, but the biological meaning of ASIP/PAR-3 in tight Junctions remains to be clarified. In the present study, we show that ASIP/PAR-3 staining distributes to the subapical domain of epithelial cell-cell Junctions, including epithelial cells with less-developed tight Junctions, in clear contrast with ZO-1, another tight-Junction-associated protein, the staining of which is stronger in cells with well-developed tight Junctions. Consistently, immunogold electron microscopy revealed that ASIP/PAR-3 concentrates at the apical edge of tight Junctions, whereas ZO-1 distributes alongside tight Junctions. To clarify the meaning of this characteristic localization of ASIP, we analyzed the effects of overexpressed ASIP/PAR-3 on tight Junction Formation in cultured epithelial MDCK cells. The induced overexpression of ASIP/PAR-3, but not its deletion mutant lacking the aPKC-binding sequence, promotes cell-cell contact-induced tight Junction Formation in MDCK cells when evaluated on the basis of transepithelial electrical resistance and occludin insolubilization. The significance of the aPKC-binding sequence in tight Junction Formation is also supported by the finding that the conserved PKC-phosphorylation site within this sequence, ASIP-Ser827, is phosphorylated at the most apical tip of cell-cell contacts during the initial phase of tight Junction Formation in MDCK cells. Together, our present data suggest that ASIP/PAR-3 regulates epithelial tight Junction Formation positively through interaction with aPKC.
Tomoyuki Yamanaka - One of the best experts on this subject based on the ideXlab platform.
-
Involvement of ASIP/PAR-3 in the promotion of epithelial tight Junction Formation.
Journal of cell science, 2002Co-Authors: Tomonori Hirose, Yasushi Izumi, Yoji Nagashima, Yoko Tamai-nagai, Hidetake Kurihara, Tatsuo Sakai, Yukari Suzuki, Tomoyuki Yamanaka, Atsushi Suzuki, Keiko MizunoAbstract:The mammalian protein ASIP/PAR-3 interacts with atypical protein kinase C isotypes (aPKC) and shows overall sequence similarity to the invertebrate proteins C. elegans PAR-3 and Drosophila Bazooka, which are crucial for the establishment of polarity in various cells. The physical interaction between ASIP/PAR-3 and aPKC is also conserved in C. elegans PAR-3 and PKC-3 and in Drosophila Bazooka and DaPKC. In mammals, ASIP/PAR-3 colocalizes with aPKC and concentrates at the tight Junctions of epithelial cells, but the biological meaning of ASIP/PAR-3 in tight Junctions remains to be clarified. In the present study, we show that ASIP/PAR-3 staining distributes to the subapical domain of epithelial cell-cell Junctions, including epithelial cells with less-developed tight Junctions, in clear contrast with ZO-1, another tight-Junction-associated protein, the staining of which is stronger in cells with well-developed tight Junctions. Consistently, immunogold electron microscopy revealed that ASIP/PAR-3 concentrates at the apical edge of tight Junctions, whereas ZO-1 distributes alongside tight Junctions. To clarify the meaning of this characteristic localization of ASIP, we analyzed the effects of overexpressed ASIP/PAR-3 on tight Junction Formation in cultured epithelial MDCK cells. The induced overexpression of ASIP/PAR-3, but not its deletion mutant lacking the aPKC-binding sequence, promotes cell-cell contact-induced tight Junction Formation in MDCK cells when evaluated on the basis of transepithelial electrical resistance and occludin insolubilization. The significance of the aPKC-binding sequence in tight Junction Formation is also supported by the finding that the conserved PKC-phosphorylation site within this sequence, ASIP-Ser827, is phosphorylated at the most apical tip of cell-cell contacts during the initial phase of tight Junction Formation in MDCK cells. Together, our present data suggest that ASIP/PAR-3 regulates epithelial tight Junction Formation positively through interaction with aPKC.
-
involvement of asip par 3 in the promotion of epithelial tight Junction Formation
Journal of Cell Science, 2002Co-Authors: Tomonori Hirose, Yasushi Izumi, Yoji Nagashima, Hidetake Kurihara, Tatsuo Sakai, Yukari Suzuki, Tomoyuki Yamanaka, Atsushi Suzuki, Yoko Tamainagai, Keiko MizunoAbstract:The mammalian protein ASIP/PAR-3 interacts with atypical protein kinase C isotypes (aPKC) and shows overall sequence similarity to the invertebrate proteins C. elegans PAR-3 and Drosophila Bazooka, which are crucial for the establishment of polarity in various cells. The physical interaction between ASIP/PAR-3 and aPKC is also conserved in C. elegans PAR-3 and PKC-3 and in Drosophila Bazooka and DaPKC. In mammals, ASIP/PAR-3 colocalizes with aPKC and concentrates at the tight Junctions of epithelial cells, but the biological meaning of ASIP/PAR-3 in tight Junctions remains to be clarified. In the present study, we show that ASIP/PAR-3 staining distributes to the subapical domain of epithelial cell-cell Junctions, including epithelial cells with less-developed tight Junctions, in clear contrast with ZO-1, another tight-Junction-associated protein, the staining of which is stronger in cells with well-developed tight Junctions. Consistently, immunogold electron microscopy revealed that ASIP/PAR-3 concentrates at the apical edge of tight Junctions, whereas ZO-1 distributes alongside tight Junctions. To clarify the meaning of this characteristic localization of ASIP, we analyzed the effects of overexpressed ASIP/PAR-3 on tight Junction Formation in cultured epithelial MDCK cells. The induced overexpression of ASIP/PAR-3, but not its deletion mutant lacking the aPKC-binding sequence, promotes cell-cell contact-induced tight Junction Formation in MDCK cells when evaluated on the basis of transepithelial electrical resistance and occludin insolubilization. The significance of the aPKC-binding sequence in tight Junction Formation is also supported by the finding that the conserved PKC-phosphorylation site within this sequence, ASIP-Ser827, is phosphorylated at the most apical tip of cell-cell contacts during the initial phase of tight Junction Formation in MDCK cells. Together, our present data suggest that ASIP/PAR-3 regulates epithelial tight Junction Formation positively through interaction with aPKC.
