α-Catenin-independent Recruitment of ZO-1 to Nectin-based Cell-Cell Adhesion Sites through Afadin

Yokoyama, Shigekazu; Tachibana, Kunihide; Nakanishi, Hiroyuki; Yamamoto, Yasunori; Irie, Kenji; Mandai, Kenji; Nagafuchi, Akira; Monden, Morito; Takai, Yoshimi

doi:10.1091/mbc.12.6.1595

Cited by 89 publications

(80 citation statements)

References 60 publications

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“…Conversely, the amount of afadin and ZO-1 in Fractions 10 ± 15 from nectin-2a-DC-EL cells were more than those from nectin-2a-full-EL cells. These results are consistent with our earlier observations (Yokoyama et al, 2001) and indicate that proteins possibly interacting with the cadherin ± catenin and nectin ± afadin systems may be more enriched in Fractions 4 ± 6 from nectin-2a-full-EL cells than in those from nectin-2a-DC-EL cells.…”

Section: Resultssupporting

confidence: 93%

“…However, at least, the latrunculin Asensitive actin cytoskeleton is not required for the localization of mLin-7C at the nectin-based cell ± cell junctions. We have previously shown that ZO-1 is associated with the nectin ± afadin system in a cadherin-independent manner (Yokoyama et al, 2001). It is possible that mLin-7C is associated with the nectin ± afadin system through ZO-1, but mLin-7C did not directly interact with ZO-1 (data not shown).…”

Section: Discussionmentioning

confidence: 81%

“…MBP-Afadin-PDZ, GSTnectin-2a-CP, and Myc-His6-afadin were prepared as described Yokoyama et al, 2001). These recombinant proteins contained the following aa: MBPafadin-PDZ, aa 1007 ± 1125 (PDZ domain); GST-nectin-2a-CP, aa 387 ± 467 (cytoplasmic region of nectin-2a); and MycHis6-afadin, aa 1 ± 1829 (full length).…”

Section: Constructionmentioning

confidence: 99%

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Localization of mLin-7 at nectin-based cell–cell junctions

et al. 2002

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In C. elegans, lin-7 as well as lin-2/lin-10 is involved in the proper localization of the LET-23 receptor tyrosine kinase that regulates vulval induction. The mammalian homologue, mLin-7, forms a ternary complex with the mammalian homologues of LIN-2 and LIN-10 and localizes at cell ± cell junctions in epithelial cells, but the mechanism of this localization of mLin-7 is unknown. Nectin is an immunoglobulin-like cell ± cell adhesion molecule that is involved in organization of adherens and tight junctions in epithelial cells. Nectin is indirectly associated with the cadherin ± catenin system and the actin cytoskeleton through afadin, an actin ®lament-binding protein. We showed here that mLin-7 localized at the nectin-based cell ± cell junctions. This localization of mLin-7 required the interaction of nectin with afadin, but not the cadherin ± catenin system or the actin cytoskeleton. mLin-7 did not directly interact with nectin or afadin. The results indicate that mLin-7 localizes at cell ± cell junctions through the nectin ± afadin system.

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Section: Resultssupporting

confidence: 93%

Section: Discussionmentioning

confidence: 81%

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Localization of mLin-7 at nectin-based cell–cell junctions

et al. 2002

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“…They bind to gap junction connexin proteins via PDZ2 and regulate the size and gating properties of these cell-to-cell channels. They also bind directly to adherens junction proteins, such as ARVCF (PDZ1), AF-6/afadin (SH3) and ␣-catenin (GUK) and regulate the assembly of actomyosin at the adherens junction in polarized epithelial cells (21)(22)(23). However, ZO proteins only localize to the adherens junction early in epithelial biogenesis, prior to the formation of tight junctions, and their localization to gap junctions is spatially distinct from tight junctions.…”

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confidence: 99%

The Src Homology 3 Domain Is Required for Junctional Adhesion Molecule Binding to the Third PDZ Domain of the Scaffolding Protein ZO-1

Nomme

Fanning

Caffrey

et al. 2011

Journal of Biological Chemistry

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Background: ZO-1 is a scaffolding protein implicated in the assembly of tight junctions. Results: Structures of core PDZ-SH3-GUK, plus and minus JAM-A peptide, and isolated PDZ are presented. Conclusion: The SH3 domain is required for JAM-A binding to PDZ3. Significance: This is the first demonstration for the role of an adjacent domain to the binding of ligands to PDZ domains in the MAGUK family.

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“…Several reasons lead us to suggest that ZO-1 and PAR3 are the most likely candidates to functionally interact with JAM-A in our system. First, ZO-1 is an early player for junction formation in epithelia (73), and JAM-A is not far behind (20). Second, PAR3 is a member of the PAR/ aPKC complex (17,26), which is required for establishing and maintaining TJs in epithelia, and JAM is the only known membrane anchor for it (reviewed in Refs.…”

Section: Jam-a's Cytoplasmic Pdz-binding Domain Is Essential For Its mentioning

confidence: 99%

JAM-A is both essential and inhibitory to development of hepatic polarity in WIF-B cells

Braiterman¹,

Heffernan²,

Nyasae³

et al. 2008

American Journal of Physiology-Gastrointestinal and Liver Physi

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Junctional adhesion molecule (JAM) is involved in tight junction (TJ) formation in epithelial cells. Three JAMs (A, B, and C) are expressed in rat hepatocytes, but only rat JAM-A is present in polarized WIF-B cells, a rat-human hepatic line. We used knockdown (KD) and overexpression in WIF-B cells to determine the role of JAM-A in the development of hepatic polarity. Expression of rat JAM-A short hairpin RNA resulted in ϳ50% KD of JAM-A and substantial loss of hepatic polarity, as measured by the absence of apical cysts formed by adjacent cells and sealed by TJ belts. When inhibitory RNA-resistant human JAM-A (huWT) was expressed in KD cells, hepatic polarity was restored. In contrast, expression of JAM-A that either lacked its PDZ-binding motif (hu⌬C-term) or harbored a point mutation (T273A) did not complement, indicating that multiple sites within JAM-A's cytoplasmic tail are required for the development of hepatic polarity. Overexpression of huWT in normal WIF-B cells unexpectedly blocked WIF-B maturation to the hepatic phenotype, as did expression of three huJAM-A constructs with single point mutations in putative phosphorylation sites. In contrast, hu⌬C-term was without effect, and the T273A mutant only partially blocked maturation. Our results show that JAM-A is essential for the development of polarity in cultured hepatic cells via its possible phosphorylation and recruitment of relevant PDZ proteins and that hepatic polarity is achieved within a narrow range of JAM-A expression levels. Importantly, formation/ maintenance of TJs and the apical domain in hepatic cells are linked, unlike simple epithelia.partitioning-defective polarity protein/atypical protein kinase C complex

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α-Catenin-independent Recruitment of ZO-1 to Nectin-based Cell-Cell Adhesion Sites through Afadin

Cited by 89 publications

References 60 publications

Localization of mLin-7 at nectin-based cell–cell junctions

Localization of mLin-7 at nectin-based cell–cell junctions

The Src Homology 3 Domain Is Required for Junctional Adhesion Molecule Binding to the Third PDZ Domain of the Scaffolding Protein ZO-1

JAM-A is both essential and inhibitory to development of hepatic polarity in WIF-B cells

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