title: The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL.
abstract: The small adaptor protein RIL consists of two segments, the C-terminal LIM and the N-terminal PDZ domain, which mediate multiple protein-protein interactions. The RIL LIM domain can interact with PDZ domains in the protein tyrosine phosphatase PTP-BL and with the PDZ domain of RIL itself. Here, we describe and characterise the interaction of the RIL PDZ domain with the zyxin-related protein TRIP6, a protein containing three C-terminal LIM domains. The second LIM domain in TRIP6 is sufficient for a strong interaction with RIL. A weaker interaction with the third LIM domain in TRIP6, including the proper C-terminus, is also evident. TRIP6 also interacts with the second out of five PDZ motifs in PTP-BL. For this interaction to occur both the third LIM domain and the proper C-terminus are necessary. RNA expression analysis revealed overlapping patterns of expression for TRIP6, RIL and PTP-BL, most notably in tissues of epithelial origin. Furthermore, in transfected epithelial cells TRIP6 can be co-precipitated with RIL and PTP-BL PDZ polypeptides, and a co-localisation of TRIP6 and RIL with Factin structures is evident. Taken together, PTP-BL, RIL and TRIP6 may function as components of multi-protein complexes at actin-based sub-cellular structures.
authors.affiliation: Department of Cell Biology, Institute of Cellular Signalling, University of Nijmegen, The Netherlands.
authors.forename: E
authors.initials: E
authors.lastname: Cuppen
authors.forename: M
authors.initials: M
authors.lastname: van Ham
authors.forename: D G
authors.initials: DG
authors.lastname: Wansink
authors.forename: A
authors.initials: A
authors.lastname: de Leeuw
authors.forename: B
authors.initials: B
authors.lastname: Wieringa
authors.forename: W
authors.initials: W
authors.lastname: Hendriks
mesh_terms: D000074183:ATPases Associated with Diverse Cellular Activities; D000199:Actins / Q000378:metabolism; D048868:Adaptor Proteins, Signal Transducing; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D018938:Caco-2 Cells; D003001:Cloning, Molecular; D003598:Cytoskeletal Proteins; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D015723:Gene Library; D006023:Glycoproteins; D006801:Humans; D017403:In Situ Hybridization; D060588:LIM Domain Proteins; D008667:Metalloproteins / Q000378:metabolism*; D051379:Mice; D008840:Microfilament Proteins; D008969:Molecular Sequence Data; D010957:Plasmids; D011233:Precipitin Tests; D046988:Proteasome Endopeptidase Complex; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D054595:Protein Tyrosine Phosphatase, Non-Receptor Type 13; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*; D014162:Transfection; D020798:Two-Hybrid System Techniques; D060589:Zyxin
chemical_list: D000199:Actins; D048868:Adaptor Proteins, Signal Transducing; D003598:Cytoskeletal Proteins; D004268:DNA-Binding Proteins; D006023:Glycoproteins; D060588:LIM Domain Proteins; D008667:Metalloproteins; D008840:Microfilament Proteins; C486247:PDLIM4 protein, human; C092282:PSMC5 protein, human; C486248:Pdlim4 protein, mouse; D012333:RNA, Messenger; D014157:Transcription Factors; C092842:ZYX protein, human; C498285:Zyx protein, mouse; D060589:Zyxin; C516742:PTPN13 protein, human; D054595:Protein Tyrosine Phosphatase, Non-Receptor Type 13; D017027:Protein Tyrosine Phosphatases; C516743:Ptpn13 protein, mouse; D046988:Proteasome Endopeptidase Complex; D000074183:ATPases Associated with Diverse Cellular Activities