The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL

Eur J Cell Biol. 2000 Apr;79(4):283-93. doi: 10.1078/S0171-9335(04)70031-X.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Actins / metabolism
  • Adaptor Proteins, Signal Transducing*
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Caco-2 Cells
  • Cloning, Molecular
  • Cytoskeletal Proteins
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Fluorescent Antibody Technique
  • Gene Library
  • Glycoproteins
  • Humans
  • In Situ Hybridization
  • LIM Domain Proteins
  • Metalloproteins / metabolism*
  • Mice
  • Microfilament Proteins
  • Molecular Sequence Data
  • Plasmids
  • Precipitin Tests
  • Proteasome Endopeptidase Complex
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein Tyrosine Phosphatase, Non-Receptor Type 13
  • Protein Tyrosine Phosphatases / chemistry
  • Protein Tyrosine Phosphatases / metabolism*
  • RNA, Messenger / metabolism
  • Sequence Homology, Amino Acid
  • Tissue Distribution
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*
  • Transfection
  • Two-Hybrid System Techniques
  • Zyxin

Substances

  • Actins
  • Adaptor Proteins, Signal Transducing
  • Cytoskeletal Proteins
  • DNA-Binding Proteins
  • Glycoproteins
  • LIM Domain Proteins
  • Metalloproteins
  • Microfilament Proteins
  • PDLIM4 protein, human
  • PSMC5 protein, human
  • Pdlim4 protein, mouse
  • RNA, Messenger
  • Transcription Factors
  • ZYX protein, human
  • Zyx protein, mouse
  • Zyxin
  • PTPN13 protein, human
  • Protein Tyrosine Phosphatase, Non-Receptor Type 13
  • Protein Tyrosine Phosphatases
  • Ptpn13 protein, mouse
  • Proteasome Endopeptidase Complex
  • ATPases Associated with Diverse Cellular Activities