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 wi...

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Bibliographic Details
Published in:FEBS letters 2001-02, Vol.489 (2), p.233-236
Main Authors: Shenolikar, Shirish, Minkoff, Charles M., Steplock, Deborah A., Evangelista, Christine, Liu, Min-Zhi, Weinman, Edward J.
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Biosensing Techniques
Cell Line
Dimerization
Na +/H + exchanger-3
Okadaic acid
Peptide Fragments - metabolism
Phosphoproteins - chemistry
Phosphoproteins - genetics
Phosphoproteins - metabolism
Phosphorylation
Protein Binding
Protein oligomerization
Protein phosphorylation
Protein Structure, Tertiary
PSD-95/Disc large/ZO-1 domain
Rabbits
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Sodium-Hydrogen Exchangers
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(01)02109-3