Premium
N‐terminal PDZ domain is required for NHERF dimerization
Author(s) -
Shenolikar Shirish,
Minkoff Charles M.,
Steplock Deborah A.,
Evangelista Christine,
Liu Min-Zhi,
Weinman Edward J.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02109-3
Subject(s) - pdz domain , chemistry , recombinant dna , phosphorylation , microbiology and biotechnology , signal transduction , biophysics , biochemistry , biology , gene
NHERF, a 55 kDa PDZ‐containing protein, binds receptors and ion transporters to mediate signal transduction at the plasma membrane. Recombinant NHERF demonstrated an apparent size of 150 kDa on gel filtration, which could be reduced to approximately 55 kDa by protein denaturing agents, consistent with the formation of NHERF dimers. Biosensor studies established the time‐ and concentration‐dependent dimerization of NHERF. Overlays of recombinant NHERF fragments suggested that NHERF dimerization was principally mediated by the N‐terminal PDZ‐I domain. In PS120 cells, reversible protein phosphorylation modulated NHERF dimerization and suggested a role for NHERF dimers in hormonal signaling.