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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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Published in: | FEBS letters 2001-02, Vol.489 (2), p.233-236 |
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creator | Shenolikar, Shirish Minkoff, Charles M. Steplock, Deborah A. Evangelista, Christine Liu, Min-Zhi Weinman, Edward J. |
description | 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. |
doi_str_mv | 10.1016/S0014-5793(01)02109-3 |
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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 |
title | N-terminal PDZ domain is required for NHERF dimerization |
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