| First Author | van den Berk LC | Year | 2004 |
| Journal | Mol Biol Rep | Volume | 31 |
| Issue | 4 | Pages | 203-15 |
| PubMed ID | 15663004 | Mgi Jnum | J:250435 |
| Mgi Id | MGI:6103273 | Doi | 10.1007/s11033-005-1407-8 |
| Citation | van den Berk LC, et al. (2004) The interaction of PTP-BL PDZ domains with RIL: an enigmatic role for the RIL LIM domain. Mol Biol Rep 31(4):203-15 |
| abstractText | PDZ domains are protein-protein interaction modules that are crucial for the assembly of structural and signaling complexes. PDZ domains specifically bind short carboxyl-terminal peptides and occasionally internal sequences that structurally resemble peptide termini. Previously, using yeast two-hybrid methodology, we studied the interaction of two PDZ domains present in the large submembranous protein tyrosine phosphatase PTP-BL with' the C-terminal half of the LIM domain-containing protein RIL. Deletion of the extreme RIL C-terminus did not eliminate binding, suggesting the presence of a PDZ binding site within the RIL LIM moiety. We have now performed experiments in mammalian cell lysates and found that the RIL C-terminus proper, but not the RIL LIM domain, can interact with PTP-BL, albeit very weakly. However, this interaction with PTP-BL PDZ domains is greatly enhanced when the combined RIL LIM domain and C-terminus is used, pointing to synergistic effects. NMR titration experiments and site-directed mutagenesis indicate that this result is not dependent on specific interactions that require surface exposed residues on the RIL LIM domain, suggesting a stabilizing role in the association with PTP-BL. |
