The Erbin PDZ Domain Binds with High Affinity and Specificity to the Carboxyl Termini of δ-Catenin and ARVCF

Erbin is a recently described member of the LAP (leucine-rich repeat and PDZ domain) protein family. We used a C-terminally displayed phage peptide library to identify optimal ligands for the Erbin PDZ domain. Phage-selected peptides were type 1 PDZ ligands that bound with high affinity and specificity to the Erbin PDZ domain in vitro. These peptides most closely resembled the C-terminal PDZ domain-binding motifs of three p120-related catenins: δ-catenin, ARVCF, and p0071 (DSWV-COOH). Analysis of the interactions of the Erbin PDZ domain with synthetic peptides matching the C termini of ARVCF or δ-catenin also demonstrated specific high affinity binding. We characterized the interactions between the Erbin PDZ domain and both ARVCF and δ-catenin in vitro and in vivo. The Erbin PDZ domain co-localized and coprecipitated with ARVCF or δ-catenin complexed with β-catenin and E/N-cadherin. Mutagenesis and peptide competition experiments showed that the association of Erbin with the cadherin-catenin complex was mediated by the interaction of its PDZ domain with the C-terminal PDZ domain-binding motifs (DSWV-COOH) of ARVCF and δ-catenin. Finally, we showed that endogenous δ-catenin and Erbin co-localized in and co-immunoprecipitated from neurons. These results suggest that δ-catenin and ARVCF may function to mediate the association of Erbin with the junctional cadherin-catenin complex. They also demonstrate that C-terminal phage-display technology can be used to predict physiologically relevant ligands for PDZ domains. Erbin is a recently described member of the LAP (leucine-rich repeat and PDZ domain) protein family. We used a C-terminally displayed phage peptide library to identify optimal ligands for the Erbin PDZ domain. Phage-selected peptides were type 1 PDZ ligands that bound with high affinity and specificity to the Erbin PDZ domain in vitro. These peptides most closely resembled the C-terminal PDZ domain-binding motifs of three p120-related catenins: δ-catenin, ARVCF, and p0071 (DSWV-COOH). Analysis of the interactions of the Erbin PDZ domain with synthetic peptides matching the C termini of ARVCF or δ-catenin also demonstrated specific high affinity binding. We characterized the interactions between the Erbin PDZ domain and both ARVCF and δ-catenin in vitro and in vivo. The Erbin PDZ domain co-localized and coprecipitated with ARVCF or δ-catenin complexed with β-catenin and E/N-cadherin. Mutagenesis and peptide competition experiments showed that the association of Erbin with the cadherin-catenin complex was mediated by the interaction of its PDZ domain with the C-terminal PDZ domain-binding motifs (DSWV-COOH) of ARVCF and δ-catenin. Finally, we showed that endogenous δ-catenin and Erbin co-localized in and co-immunoprecipitated from neurons. These results suggest that δ-catenin and ARVCF may function to mediate the association of Erbin with the junctional cadherin-catenin complex. They also demonstrate that C-terminal phage-display technology can be used to predict physiologically relevant ligands for PDZ domains. PSD-95/Discs Large/ZO-1 Erb2-interacting protein leucine-rich repeat and PDZ domain membrane-associated guanylate kinase with inverted orientation Armadillo protein deleted invelo-cardiofacial syndrome glutathione S-transferase enzyme-linked immunosorbent assay phosphate-buffered saline green fluorescent protein enhanced green fluorescent protein red fluorescent protein human embryonic kidney PDZ1 domains are 80–100-amino acid compact globular motifs that are usually embedded in larger multidomain scaffolding proteins (1.Craven S. Bredt D. Cell. 1998; 93: 495-498Abstract Full Text Full Text PDF PubMed Scopus (429) Google Scholar, 2.Fanning A. Anderson J. J. Clin. Invest. 1999; 103: 767-772Crossref PubMed Scopus (401) Google Scholar, 3.Harris B. Lim W. J. Cell Sci. 2001; 114: 3219-3231Crossref PubMed Google Scholar). PDZ domains predominantly mediate protein/protein interactions by recognizing the C termini of various intracellular and cell-surface proteins. Type 1 PDZ domains interact with the C-terminal consensus sequence X(S/T)X(V/I/L)-COOH, whereas type 2 domains bind to the C-terminal consensus sequence X-hydrophobe-X-hydrophobe-COOH (3.Harris B. Lim W. J. Cell Sci. 2001; 114: 3219-3231Crossref PubMed Google Scholar, 4.Songyang Z. Fanning A.S. Fu C. Xu J. Marfatia S.M. Chishti A.H. Crompton A. Chan A.C. Anderson J.M. Cantley L.C. Science. 1997; 275: 73-77Crossref PubMed Scopus (1224) Google Scholar, 5.Harrison S. Cell. 1996; 86: 341-343Abstract Full Text Full Text PDF PubMed Scopus (153) Google Scholar). Structural analyses of peptides bound to PDZ domains suggest necessary interactions at both positions 0 and −2 (6.Doyle D.A. Lee A. Lewis J. Kim E. Sheng M. Mackinnon R. Cell. 1996; 85: 1067-1076Abstract Full Text Full Text PDF PubMed Scopus (976) Google Scholar, 7.Daniels D.L. Cohen A.R. Anderson J.M. Brunger A.T. Nat. Struct. Biol. 1998; 5: 317-325Crossref PubMed Scopus (161) Google Scholar, 8.Tochio H. Zhang Q. Mandal P. Li M. Zhang M. Nat. Struct. Biol. 1999; 6: 417-421Crossref PubMed Scopus (139) Google Scholar). However, among type 1 PDZ ligands, these residues are relatively invariant, indicating that other residues within the C terminus likely contribute to the specificity of PDZ domain/ligand interactions (3.Harris B. Lim W. J. Cell Sci. 2001; 114: 3219-3231Crossref PubMed Google Scholar). For example, two previous studies (9.Fuh G. Pisabarro M.T. Li Y. Quan C. Lasky L.A. Sidhu S. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google Scholar, S. G. G. J. J. Biol. 2001; PubMed Scopus Google Scholar, S. J. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google demonstrated the of residues and for specificity and affinity for PDZ domain/ligand a for of PDZ proteins scaffolding that to various For example, the domain protein was to of the to for in to S. J. R. E. A. M. 1997; PubMed Scopus Google Scholar, S. J. 1998; PubMed Scopus Google Scholar). in the demonstrated that the of the kinase is to the PDZ domain of S.M. Kim Cell. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar, C. A. Kim J.M. Cell. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar). that interaction the of the kinase and a of with a of other these suggest that a function of the PDZ domains embedded within scaffolding proteins is to at specific Erbin is a recently described member of the LAP protein J. S. A. H. E. J. B. D. Nat. Cell Biol. PubMed Scopus Google Scholar). the most closely to human Erbin human in the C. is a protein that a in the of of a in of the and results in R. A. S. J. D. M. Nat. Cell Biol. PubMed Scopus Google Scholar, R. J. M. J. Cell Sci. 2001; 114: Google Scholar). is kinase that is in a high of and is a in the of M. M. Y. PubMed Scopus Google Scholar). is the of and a PDZ domain-binding at its C terminus that is for J. S. A. H. E. J. B. D. Nat. Cell Biol. PubMed Scopus Google Scholar). to the kinase described of the PDZ domain-binding results in the of the to to interact with a PDZ protein necessary for its to or at the J. S. A. H. E. J. B. D. Nat. Cell Biol. PubMed Scopus Google Scholar). Erbin the protein that of the of its PDZ domain to the C terminus J. S. A. H. E. J. B. D. Nat. Cell Biol. PubMed Scopus Google Scholar). of the of we to identify peptide ligands for the Erbin PDZ domain that its interaction with the C we used a recently described phage that a and of peptides to the C terminus of the protein (9.Fuh G. Pisabarro M.T. Li Y. Quan C. Lasky L.A. Sidhu S. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google Scholar). two PDZ domains from the protein was demonstrated that be to high affinity peptides that type 1 or 2 PDZ domain-binding the PDZ domain used for We used to peptides that bind to the Erbin PDZ domain. of the Erbin PDZ domain-binding peptides that closely resembled the C termini of three ARVCF, and the C terminus of P. A. J. Cell Sci. PubMed Google Scholar). and studies δ-catenin and ARVCF demonstrated that the interaction with Erbin is of high affinity and these results suggest that δ-catenin and ARVCF bind to the Erbin PDZ domain in vivo. described library of to the C terminus of the protein was of with a PDZ domain protein the were in in with phage to phage and to of the three of phage were and in a phage S. J. PubMed Google Scholar). that bound to the PDZ domain to a were to sequence The of peptides for the Erbin PDZ domain were a described competition (9.Fuh G. Pisabarro M.T. Li Y. Quan C. Lasky L.A. Sidhu S. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google Scholar). The was the of peptide that of PDZ domain to were by peptide with and with of the PDZ domain protein in and was for with of peptide and to the assay a the were with with a of and in and with was used to identify proteins with C termini that the peptides for to the Erbin PDZ domain. of peptides a consensus sequence of the for to the Erbin PDZ domain. We used consensus sequence to the to the C-terminal residues of proteins within the these we proteins that with C-terminal proteins protein domains are were a of that are or of the of the that three intracellular were δ-catenin, ARVCF, and p0071 These three proteins are of the Armadillo of C-terminal are in ligands for the Erbin PDZ domain. the PDZ domains of were by a of human Y. D. S. R. Lee J. Q. Lasky L.A. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google the the The PDZ1 and domains were the of with the C terminus of of the and domains were the of with the terminus of The PDZ domain of human Erbin to was from sequence and three the a with the C terminus of the of a with the terminus of and the of a with the C terminus of was and described G. R. M. J. Biol. Chem. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). δ-catenin and δ-catenin a of δ-catenin the C-terminal acid were with the C terminus of of β-catenin S. B. P. Cell. Biol. 1996; PubMed Google was a with the C terminus of ARVCF the described D. J. A. J. Cell Sci. Google and was a from the of Erbin described Y. Q. W. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google and was a from the of The Erbin PDZ domain or the domain were the or of the E. and The PDZ domain of human to was the of and affinity of E. proteins were by the and were in high acid and For of were to and with were with 1 of 1 and with for and by for at in a in the were and for by of were in a and at were from for from were with of a with a in 1 of and were and described for For were and in of of were at for at in the were were in a and at For peptide experiments with PDZ domains of was to with and with peptide and of for 2 a at The were three with 1 of and in of of was with of for experiments with were that of protein and of were used for these For experiments with δ-catenin, δ-catenin ARVCF, and of was to in and by The were with of E. protein of for 2 a at were three and bound proteins were by For of 1 of was to a of 1 with and by of the were described for For and experiments were in 1 of and were described of was with of for or with of of protein for and for 2 at a The were three with 1 of and proteins were by Erbin PDZ domain-binding peptides in were with peptides for or to The peptide was to a at the terminus of a high affinity peptide or a peptide the intracellular results in of the the PDZ domain-binding peptide in the For from were to 1 in and bound to protein for 1 a The were with of the and of protein were from the by for in the of of of the and of both and were and to for For the was to were with peptides for 2 were to and with the the were with for in with in and with The Erbin PDZ domain and δ-catenin were and and be ARVCF and were by with these proteins and with were with and with were a to a with a were from the of embryonic and in with 2 and in were for in in with and in were with in in were to a of 2 for Erbin and for δ-catenin in and in The were with at and three with with to a of in for 1 at The were three with and with to a of in for 1 at The were with by a with to Finally, the were with were a with a to a with a with fluorescent of in both the red and green was to be a of protein were with of of and of and acid in The and were and for 2 in the at and to a of and at were a were with and with and in for 1 at The were at with in and in and were to 2 and were three with and for 1 with to a in in was by three with The were with to a of in in Finally, the were with and with The were described were from with residues of protein to were the of both and the were of Erbin or δ-catenin, and were from was from was from and or were from were a from the of described C-terminally displayed phage peptide (9.Fuh G. Pisabarro M.T. Li Y. Quan C. Lasky L.A. Sidhu S. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google were to peptides that bound with high affinity to a protein of the PDZ domain of Erbin to that bound to the Erbin PDZ domain were and the of the displayed C-terminal peptides were consensus sequence was in the peptides with ligands for type 1 PDZ domains (3.Harris B. Lim W. J. Cell Sci. 2001; 114: 3219-3231Crossref PubMed Google the C-terminal was to be The Erbin PDZ domain and are also at The at was −2 was to be or with a of the of or at the Erbin PDZ domain to be a type 1 domain. consensus for or was at consensus was at of the peptides a or consensus was at or for the PDZ ligands are ligands three of to the Erbin PDZ the consensus sequence for high affinity to the Erbin PDZ domain from sequence among the the C termini of ligands for the Erbin PDZ in with ARVCF, and or in a previous with that the consensus sequence are in in the peptide from the C terminus to the are for the PDZ ligands are ligands three of to the Erbin PDZ the consensus sequence for high affinity to the Erbin PDZ domain from sequence among the the C termini of ligands for the Erbin PDZ in with ARVCF, and or in a previous with that the consensus sequence are in in the peptide from the C terminus to the are in a of the consensus sequence with the C-terminal sequence of and C-terminal in the that the Erbin PDZ domain may bind to proteins the human protein C termini that consensus sequence to a of three proteins in the with the sequence P. A. J. Cell Sci. PubMed Google Scholar). of the C terminus with the also at −2 is be the type of by a type 2 PDZ whereas the Erbin PDZ of and peptide to be a type 1 PDZ domain. at −2 was in a that of a type 2 is The C terminus also at whereas peptides the Erbin PDZ domain the C termini of the three at these results suggest that the Erbin PDZ domain may bind most to the δ-catenin, ARVCF, and the interactions between the Erbin PDZ domain and various we used to the between the Erbin PDZ domain and peptides in We (9.Fuh G. Pisabarro M.T. Li Y. Quan C. Lasky L.A. Sidhu S. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google and (3.Harris B. Lim W. J. Cell Sci. 2001; 114: 3219-3231Crossref PubMed Google Scholar, B. B. Lim W. 2001; PubMed Scopus Google that type of the of PDZ ligands the peptides in are and the assay is from to that can with that the of the peptides are relatively with the sequence at from the C termini of ARVCF or δ-catenin bound the Erbin PDZ domain with in the these are that of the are the for the PDZ domain-binding C-terminal motifs of and β-catenin for PDZ domain-binding synthetic synthetic peptides to from peptide phage or to the C termini of human for to the Erbin PDZ for to the Erbin PDZ to the of at of high affinity peptides for to the Erbin PDZ to the of at of high affinity peptides for to the Erbin PDZ for to the domain are the of peptide that of PDZ domain to peptide in were with The synthetic peptides to from peptide phage or to the C termini of human for to the Erbin PDZ to the of at of high affinity peptides for to the Erbin PDZ for to the domain (9.Fuh G. Pisabarro M.T. Li Y. Quan C. Lasky L.A. Sidhu S. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google Scholar). in a The are the of peptide that of PDZ domain to peptide in were with is that from the optimal sequence for the Erbin PDZ domain in within the residues at by the phage is likely a of For example, the of for at peptide affinity by with in and are both among the phage from the consensus sequence in larger in by the of at of the with most or to in affinity ARVCF and δ-catenin bind the Erbin PDZ domain with to of optimal ligands C-terminal the both and β-catenin C termini are with the high affinity consensus sequence at and the C termini of these proteins for the Erbin PDZ domain. these results suggest C-terminal ARVCF and δ-catenin likely are high affinity ligands for the Erbin PDZ domain. a C-terminal peptide is to interact with the Erbin PDZ we the of these to proteins the PDZ we used the PDZ domain of a for C-terminal phage and the high affinity (9.Fuh G. Pisabarro M.T. Li Y. Quan C. Lasky L.A. Sidhu S. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google Scholar, Y. D. S. R. Lee J. Q. Lasky L.A. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google Scholar). We the specificity of peptide that of the peptide in experiments PDZ domains from the protein Y. D. S. R. Lee J. Q. Lasky L.A. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google the Erbin PDZ domain. that peptide and with the PDZ domain was the peptide the whereas the peptide the Erbin PDZ domain. We that the two peptides were at three of the most residues for PDZ and in both the and the the peptide for to the domain bound to the Erbin PDZ domain. we the at of the Erbin PDZ peptide Erbin PDZ domain-binding specificity the We a peptide by at of the peptide for in the Erbin PDZ that the peptide with the Erbin PDZ with the the of in These results are also with of peptides the Erbin PDZ showed that the residues are most However, the phage also for a acid at in Erbin PDZ domain-binding the of the at is to the of the at positions 0 and in the in Finally, we used these peptides to that the is for of endogenous the PDZ protein from experiments a of the Erbin PDZ domain were to ARVCF and δ-catenin are in high affinity ligands for the Erbin PDZ by the peptide that δ-catenin and ARVCF were with the PDZ domain The of the C terminus in the δ-catenin interaction was demonstrated by the that a of δ-catenin the C-terminal was to bind to the Erbin PDZ domain. also that β-catenin was from by the PDZ domain we were to a of in the These suggest from the peptide affinity in δ-catenin and ARVCF bind to the Erbin PDZ domain and interaction between and the Erbin PDZ domain J. S. A. H. E. J. B. D. Nat. Cell Biol. PubMed Scopus Google and the in that interaction from the of the C terminus to the of the Erbin PDZ domain. we used competition to δ-catenin and bind to the the Erbin PDZ domain the that a peptide was to with the interactions between the Erbin PDZ domain and δ-catenin or that both proteins interact with the of the Erbin PDZ domain. from the affinity the interaction between δ-catenin and the Erbin PDZ domain to be that between and the Erbin PDZ domain. the peptide that bound to the domain and that three residues with the Erbin PDZ domain-binding peptide was at the δ-catenin showed a of competition with the that other affinity interactions may also with the of the Erbin PDZ domain. of is mediated by interaction between Armadillo and the of proteins C. Z. M. C. B. B. H. A. J. Cell Sci. Google Scholar). demonstrated that δ-catenin with the at of Q. M. M. J. R. M. J. Cell Biol. 1999; PubMed Scopus Google Scholar). the Erbin PDZ domain a in the Erbin PDZ domain and δ-catenin from the of the Erbin PDZ domain to the The was in in a C-terminal acid of δ-catenin with the the in a in the of the Erbin PDZ domain to the was in of δ-catenin and the Erbin PDZ domain. in was in the of δ-catenin and the Erbin PDZ domain. the in may suggest that is interaction between the Erbin PDZ domain and δ-catenin that is of the C-terminal of δ-catenin. or is C terminus was for of δ-catenin with the Erbin PDZ domain in to the cell-surface of δ-catenin, ARVCF to be predominantly in with a at the with the of the protein in D. J. A. J. Cell Sci. Google Scholar). with δ-catenin, of the ARVCF co-localized with the Erbin PDZ domain. these with the experiments described and suggest that a function of δ-catenin and ARVCF in is to the Erbin protein to the cadherin-catenin complex PDZ We and experiments to the interaction between ARVCF and the Erbin PDZ domain in be in by a that ARVCF be coprecipitated with the PDZ domain protein both were in that interaction was were for with a peptide to a of the the were with a peptide in the C-terminal was to the peptide is to the we that was with a the peptides to also the and the Erbin PDZ interaction These suggest that between Erbin and δ-catenin or ARVCF in interaction between the PDZ domain and the C terminus of these Finally, to of the Erbin PDZ domain to its C-terminal ligands is by other domains within the Erbin we a and with Erbin and that ARVCF was by in the of of ARVCF with both the Erbin PDZ domain and Erbin that the of the Erbin PDZ domain are by other domains within the Erbin The in the of the in that endogenous Erbin is in The of endogenous Erbin ARVCF or the results of experiments in is likely of the relatively of endogenous protein with the of proteins in is by the of endogenous Erbin with of Erbin in Erbin Y. Q. W. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google and δ-catenin R. W. 1997; PubMed Scopus Google are in we to complex be of that both proteins were in the of the of these proteins at the were for and with Erbin and δ-catenin. of these of the of the Erbin PDZ domain can with the endogenous cadherin-catenin in experiments were with and proteins in the were by with various from previous the PDZ domain protein was to interact with δ-catenin in with the complex in and also that these three proteins are in the PDZ domain complex. The specificity of interaction is demonstrated by the that to in a from δ-catenin, a PDZ domain-binding P. A. J. Cell Sci. PubMed Google was from the PDZ domain These suggest that δ-catenin, and can complex. the that the Erbin PDZ domain also with we used experiments to that β-catenin was δ-catenin was δ-catenin PDZ domain-binding is also with in the interaction of the PDZ domain-binding of β-catenin with the Erbin PDZ domain was The PDZ domain the affinity of the interaction between the C terminus and the Erbin PDZ domain. However, with the that was from we that by the of by of were with in The of in the of affinity C termini at and is likely that to the affinity of the PDZ domain interaction in the Finally, we showed that endogenous Erbin and δ-catenin be co-immunoprecipitated from The specificity of interaction is by the that of the interaction of endogenous Erbin and δ-catenin be by of with a with a peptide a at the C terminus these results suggest that Erbin is within a physiologically relevant cadherin-catenin complex in results that δ-catenin and ARVCF are likely in ligands of the Erbin PDZ domain. ARVCF, and p0071 are three that PDZ domain-binding motifs and are the proteins within the human that optimal Erbin PDZ domain-binding motifs by C-terminal peptide phage vitro and in of the interactions between the Erbin PDZ domain and ARVCF or δ-catenin showed that the interactions are specific and of affinity to be we that interaction in is also likely to at the of ARVCF p0071 may be P. A. J. Cell Sci. PubMed Google Scholar). also that the interaction between the Erbin PDZ domain and J. S. A. H. E. J. B. D. Nat. Cell Biol. PubMed Scopus Google Scholar, H. A. S. D. J. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google is of affinity with that of the Erbin PDZ domain and the However, we the that interaction is physiologically relevant the experiments function of the interaction between the Erbin PDZ domain and the C termini of the is to Erbin a cadherin-catenin complex. are that the cadherin-catenin complex in is that three interact with we that Erbin can be the function of the and the of these interactions to be are by the of of Erbin M. M. J. 1996; PubMed Google Scholar). Erbin and are at the terminus in the of leucine-rich in the and with PDZ domain we results from a phage the PDZ domain of the consensus sequence for the peptides was closely the sequence for the Erbin PDZ domain. that likely with the cadherin-catenin complex is to that ARVCF, and p0071 are in P. A. J. Cell Sci. PubMed Google whereas δ-catenin and is to R. W. 1997; PubMed Scopus Google Scholar, M. M. J. 1996; PubMed Google Scholar). three likely bind both Erbin and PDZ domains in or interactions were of the PDZ is that we Erbin with δ-catenin from were the the or of that a LAP protein member with the cadherin-catenin complex in a physiologically relevant described analyses the for of protein/protein Analysis of in that and demonstrated that a LAP protein PDZ to be a of D. PubMed Scopus Google Scholar, D. Li M. Science. PubMed Scopus Google Scholar, A. Biol. Full Text Full Text PDF PubMed Scopus Google Scholar). in C. that a LAP protein that may be the of to also be in the of the R. A. S. J. D. M. Nat. Cell Biol. PubMed Scopus Google Scholar, R. J. M. J. Cell Sci. 2001; 114: Google Scholar). these that LAP proteins are in the and of in of these in the that for these proteins is to with and The of the between the cadherin-catenin complex and the is and is that we interaction between the cadherin-catenin complex and a LAP protein that is to both and of δ-catenin in kidney and with protein and its interaction with Erbin the Q. M. M. J. R. M. J. Cell Biol. 1999; PubMed Scopus Google Scholar). we can the by is For example, the leucine-rich repeat in and in Erbin are to a in a protein that to and the D. Q. M. Cell. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar, J. C. M. Sci. S. A. 1998; PubMed Scopus Google Scholar). in the are to the H. Y. Cell. PubMed Scopus Google Scholar). is that LAP proteins to the cadherin-catenin complex and the by in with is of that the the most closely C. of δ-catenin and ARVCF, also with the sequence most residues within the Erbin PDZ domain to interact with of positions 0 by (9.Fuh G. Pisabarro M.T. Li Y. Quan C. Lasky L.A. Sidhu S. J. Biol. Chem. 275: Full Text Full Text PDF PubMed Scopus Google are also in the PDZ domain of that of may a to that of and the of its in the a for to the by the cadherin-catenin complex interaction with LAP proteins.