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Figure 6. Introduction of the hypothesis derived from the <t>PRISMA</t> results Evidence of spatially localized mRNA coding TJ and AJ proteins in epithelial cells (Gutierrez et al., 2014; Nagaoka et al., 2012) in combination with our PRISMA results point to the C-terminal tails of some claudins as a scaffold for localized biolog- ical processes such as protein folding and protein degradation mediated by the proteasome. We also speculate that 14-3-3 proteins could possibly facilitate these interactions, although our data are not conclusive in this regard. Created with BioRender.com.
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Figure 6. Introduction of the hypothesis derived from the <t>PRISMA</t> results Evidence of spatially localized mRNA coding TJ and AJ proteins in epithelial cells (Gutierrez et al., 2014; Nagaoka et al., 2012) in combination with our PRISMA results point to the C-terminal tails of some claudins as a scaffold for localized biolog- ical processes such as protein folding and protein degradation mediated by the proteasome. We also speculate that 14-3-3 proteins could possibly facilitate these interactions, although our data are not conclusive in this regard. Created with BioRender.com.
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Figure 6. Introduction of the hypothesis derived from the <t>PRISMA</t> results Evidence of spatially localized mRNA coding TJ and AJ proteins in epithelial cells (Gutierrez et al., 2014; Nagaoka et al., 2012) in combination with our PRISMA results point to the C-terminal tails of some claudins as a scaffold for localized biolog- ical processes such as protein folding and protein degradation mediated by the proteasome. We also speculate that 14-3-3 proteins could possibly facilitate these interactions, although our data are not conclusive in this regard. Created with BioRender.com.
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Figure 6. Introduction of the hypothesis derived from the PRISMA results Evidence of spatially localized mRNA coding TJ and AJ proteins in epithelial cells (Gutierrez et al., 2014; Nagaoka et al., 2012) in combination with our PRISMA results point to the C-terminal tails of some claudins as a scaffold for localized biolog- ical processes such as protein folding and protein degradation mediated by the proteasome. We also speculate that 14-3-3 proteins could possibly facilitate these interactions, although our data are not conclusive in this regard. Created with BioRender.com.

Journal: Cell reports

Article Title: Pan-claudin family interactome analysis reveals shared and specific interactions.

doi: 10.1016/j.celrep.2022.111588

Figure Lengend Snippet: Figure 6. Introduction of the hypothesis derived from the PRISMA results Evidence of spatially localized mRNA coding TJ and AJ proteins in epithelial cells (Gutierrez et al., 2014; Nagaoka et al., 2012) in combination with our PRISMA results point to the C-terminal tails of some claudins as a scaffold for localized biolog- ical processes such as protein folding and protein degradation mediated by the proteasome. We also speculate that 14-3-3 proteins could possibly facilitate these interactions, although our data are not conclusive in this regard. Created with BioRender.com.

Article Snippet: REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies rabbit anti-ZO-1 Invitrogen Cat# 61-7300, RRID: AB_2533938 anti-Rabbit Alexa Fluor 647 Abcam Cat# ab150075, RRID:AB_2752244 GFP-Trap _A nanobodies Chromotek Cat# gta-100, RRID: AB_2631357 Actin Abcam Cat# ab179467, RRID:AB_2737344 histone H3 Abcam Cat# ab1791, RRID:AB_302613 TCP-1 b (D-8) (CCT2) Santa Cruz Biotechnology Cat# sc-374152, RRID:AB_10917207 TCP1 Z (F-4) (CCT6A) Santa Cruz Biotechnology sc-514466 20S Proteasome a6 (C-5) (PSMA3) Santa Cruz Biotechnology Cat# sc-271187, RRID:AB_10608973 Goat anti-rabbit HRP Abcam Cat# ab6721, RRID:AB_955447 Chemicals, peptides, and recombinant proteins Acetonitrile (ACN, MeCN, LC-MS grade) Honeywell Riedel de Haehn 34967 ammonium bicarbonate (ABC) Roth T871.2 Benzonase millipore 70664-3 BSA Serva 11926 cOmpleteTM Mini Roche 11836153001 DDM Bio Vision 2036-1 DTT Sigma D0632 EDTA Merck 1.08417.1000 Formic acid (FA) Merck-Millipore 1.002640100 G418-BC Biochrom A 2912 Gentamicin Gibco 15710049 Glycerol Alpha Aesar 38988 Glycine Roth 3908.2 HEPES Serva 25245.04 IAA Sigma I1149 IGEPAL-CA-630 Sigma I8896 KCl Sigma P9541 LipofectamineTM 2000 Invitrogen 11668027 Methanol (MeOH, LC-MS grade) Honeywell Riedel de Haehn 34966 MgCl2 Ambion AM9530 Modified trypsin, sequencing grade Promega V5113 NaCl Roth 3957.1 PBS Gibco 14190-094 Penicillin-Streptomycin solution 100X Sigma TMS-AB2-C Poly-L-Lysine solution Sigma P8920-100ML Ponceau S solution Sigma 81462 ProLong Gold Antifade liquid mountant Life Technologies P36934 Protein Interaction Screen on Peptide Matrix (PRISMA) JPT PRISMA SDS-polyacrylamide gels (mini protean TGX) Biorad 456-1095 Sep-Pak C18 96-well plates Waters SKU: 186003966 Serum-free DMEM Gibco 41965062 (Continued on next page) e1 Cell Reports 41, 111588, November 8, 2022

Techniques: Derivative Assay