Papin

Deguchi, Maki; Iizuka, Toshihiko; Hata, Yoshinobu; Nishimura, Wataru; Hirao, Kazuyo; Yao, Ikuko; Kawabe, Hiroshi; Takai, Yoshimi

doi:10.1074/jbc.m005384200

Cited by 52 publications

(14 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the previous study, we reported that PAPIN was detected not only at the cell -cell contacts but also on the apical membranes in the bronchial epithelial cells (Deguchi et al, 2000). We first confirmed the apical localization of PAPIN.…”

Section: Papin Is Localized On the Apical Membrane In Madin Darby Cansupporting

confidence: 68%

“…The rabbit anti-p0071 antibodies were described previously (Deguchi et al, 2000). The mouse monoclonal anti-PAPIN antibody was raised against the product of pGex4T-1 PAPIN-15.…”

Section: Antibodiesmentioning

confidence: 99%

“…Like other catenins, p0071 is localized at the cell junctions and interacts with various proteins. We have discovered a novel p0071-binding molecule with multiple PSD-95/Dlg-A/ ZO-1 (PDZ) domains and named it plakophilin-related armadillo-repeat protein-interacting protein (PAPIN) (Deguchi et al, 2000). PAPIN consists of 2766 amino acids.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Localization of p0071-interacting proteins, plakophilin-related armadillo-repeat protein-interacting protein (PAPIN) and ERBIN, in epithelial cells

et al. 2002

Self Cite

View full text Add to dashboard Cite

PAPIN has six PDZ domains and interacts with p0071, a catenin-related protein. Recent studies have revealed that catenins determine the subcellular localization of some PDZ proteins. We have examined whether the localization of PAPIN is determined by p0071 in epithelial cells. PAPIN was localized not only on the lateral membrane but also on the apical membrane, where p0071 was absent. The targeting to both membranes was mediated by the middle region of PAPIN and did not require the p0071-interacting PDZ domain. In cells that came into contact, PAPIN was diffusely distributed on the plasma membrane, while p0071 was concentrated at immature cell -cell contacts. When epithelial cells were exposed to the low concentration of calcium, p0071 was internalized, whereas PAPIN remained on the plasma membrane. We also confirmed that the interaction with p0071 was not essential for the membrane targeting of ERBIN, a recently identified p0071-and ErbB2-binding protein. PAPIN, p0071, and ERBIN formed a complex in 293T cells. Furthermore, ERBIN and ErbB2 were colocalized with PAPIN on the lateral membrane. These findings suggest that PAPIN, p0071, and ERBIN come to the cell -cell contacts independently and interact with each other on the lateral membrane.

show abstract

Section: Papin Is Localized On the Apical Membrane In Madin Darby Cansupporting

confidence: 68%

“…The rabbit anti-p0071 antibodies were described previously (Deguchi et al, 2000). The mouse monoclonal anti-PAPIN antibody was raised against the product of pGex4T-1 PAPIN-15.…”

Section: Antibodiesmentioning

confidence: 99%

See 1 more Smart Citation

Localization of p0071-interacting proteins, plakophilin-related armadillo-repeat protein-interacting protein (PAPIN) and ERBIN, in epithelial cells

et al. 2002

Self Cite

View full text Add to dashboard Cite

show abstract

“…Erbin is probably only one component of protein complexes involved in these processes, since other PDZ proteins, including Papin, bind to p0071. Papin, a novel PDZ domain protein, interacts with p0071 in the insoluble fraction of cell extracts, whereas we recover the p0071-Erbin interaction in a 1% Triton X-100 extraction buffer (43). Other studies have shown that protein complexes containing p0071 or ␦-catenin/NPRAP, a p0071-like protein, are extractable by a Tritonbased buffer (44,45).…”

Section: Discussionmentioning

confidence: 84%

Interaction between Erbin and a Catenin-related Protein in Epithelial Cells

Jaulin-Bastard¹,

Arsanto²,

Bivic³

et al. 2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

Integrity of epithelial tissues relies on the proper apical-basolateral polarity of epithelial cells. Members of the LAP (LRR and PDZ) protein family such as LET-413 and Scribble are involved in maintaining epithelial cell polarity in Caenorhabditis elegans and Drosophila melanogaster, respectively. We previously described Erbin as a mammalian LET-413 homologue interacting with ERBB2/HER2, an epidermal growth factor receptor family member. Erbin and ERBB2/HER2 are located in the basolateral membranes of epithelial cells. We show here that Erbin interacts with p0071 (also called plakophilin-4), an armadillo repeat protein linked to the cytoskeleton. Erbin binds to p0071 in vitro and in vivo in a PDZ domain-dependent manner, and both proteins colocalized in desmosomes of epithelial cells. Using a dominant negative approach, we found that integrity of epithelial cell monolayer is impaired when interaction between Erbin and p0071 is disrupted. We propose that Erbin is connected by p0071 to cytoskeletal networks in an interaction crucial for epithelial homeostasis.

show abstract

“…The carboxylterminal domain of p0071 (along with ARVCF and ␦-catenin) terminates with a PDZ domain-binding motif (30,31) and interacts with the PDZ motif-containing protein PAPIN (59) and with the LAP protein Erbin (57,58). LAP family proteins such as Erbin and Scribble play important roles in the development of cell polarity during morphogenic events in Caenorhabditis elegans and Drosophila (44).…”

Section: P0071 Binds Ve-cadherin and Desmoplakinmentioning

confidence: 99%

The Armadillo Family Protein p0071 Is a VE-cadherin- and Desmoplakin-binding Protein

Calkins¹,

Hoepner²,

Law³

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

p0071, a member of the armadillo protein family, localizes to both adherens junctions and desmosomes in epithelial cells and exhibits homology to the adherens junction protein p120 and the desmosomal protein plakophilin-1. p0071 is also present at dermal microvascular endothelial intercellular junctions and colocalizes with VE-cadherin, an endothelium-specific cadherin that associates with both actin and intermediate filament networks. To define the role of p0071 in junction assembly, p0071 was tested for interactions with other components of the endothelial junctional complex. In transient expression assays, p0071 colocalized with and formed complexes with both VE-cadherin and desmoplakin. Deletion analysis using the yeast two-hybrid system revealed that the armadillo repeat domain of p0071 bound directly to VE-cadherin. Site-directed mutagenesis experiments demonstrated that p0071 and p120 bound to the same region on the cytoplasmic tail of VE-cadherin and that overexpression of p0071 could displace p120 from intercellular junctions. In contrast to VE-cadherin, desmoplakin was found to associate with the non-armadillo head domain of p0071. Cotransfections and triple-label immunofluorescence analysis revealed that VE-cadherin colocalization with desmoplakin in transfected COS cells required p0071, suggesting that p0071 may couple VE-cadherin to desmoplakin. Based on previous findings that both VEcadherin and desmoplakin play central roles in vasculogenesis, these new results suggest that p0071 may play an important role in endothelial junction assembly and in the morphogenic events associated with vascular remodeling.

show abstract

Papin

Cited by 52 publications

References 48 publications

Localization of p0071-interacting proteins, plakophilin-related armadillo-repeat protein-interacting protein (PAPIN) and ERBIN, in epithelial cells

Localization of p0071-interacting proteins, plakophilin-related armadillo-repeat protein-interacting protein (PAPIN) and ERBIN, in epithelial cells

Interaction between Erbin and a Catenin-related Protein in Epithelial Cells

The Armadillo Family Protein p0071 Is a VE-cadherin- and Desmoplakin-binding Protein

Contact Info

Product

Resources

About