N-terminal PDZ domain is required for NHERF dimerization.
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.
Shenolikar
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S
Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA. sheno001@mc.duke.edu
Minkoff
C M
CM
Steplock
D A
DA
Evangelista
C
C
Liu
M
M
Weinman
E J
EJ
D000818:Animals; D001665:Binding Sites; D015374:Biosensing Techniques; D002460:Cell Line; D019281:Dimerization; D010446:Peptide Fragments / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011817:Rabbits; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017923:Sodium-Hydrogen Exchangers
D010446:Peptide Fragments; D010750:Phosphoproteins; D011994:Recombinant Proteins; D017923:Sodium-Hydrogen Exchangers; C093376:sodium-hydrogen exchanger regulatory factor