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Vol. 9, Issue 3, 671-683, March 1998
Department of Cell Biology and Histology, Institute of Cellular
Signaling, University of Nijmegen, the Netherlands
The specificity of protein-protein interactions in cellular
signaling cascades is dependent on the sequence and intramolecular location of distinct amino acid motifs. We used the two-hybrid interaction trap to identify proteins that can associate with the PDZ
motif-rich segment in the protein tyrosine phosphatase PTP-BL. A
specific interaction was found with the Lin-11, Isl-1, Mec-3 (LIM)
domain containing protein RIL. More detailed analysis demonstrated that
the binding specificity resides in the second and fourth PDZ motif of
PTP-BL and the LIM domain in RIL. Immunohistochemistry on various mouse
tissues revealed a submembranous colocalization of PTP-BL and RIL in
epithelial cells. Remarkably, there is also an N-terminal PDZ motif in
RIL itself that can bind to the RIL-LIM domain. We demonstrate here
that the RIL-LIM domain can be phosphorylated on tyrosine in vitro and
in vivo and can be dephosphorylated in vitro by the PTPase domain of
PTP-BL. Our data point to the presence of a double PDZ-binding
interface on the RIL-LIM domain and suggest tyrosine phosphorylation as
a regulatory mechanism for LIM-PDZ associations in the assembly of
multiprotein complexes. These findings are in line with an important
role of PDZ-mediated interactions in the shaping and organization of
submembranous microenvironments of polarized cells.
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