Phosphorylation of a pdz domain extension modulates binding affinity and interdomain interactions in postsynaptic density-95 (psd-95) protein, a membrane-associated guanylate kinase (maguk)*

HIGHLIGHTS

• who: Jun Zhang from the effects of such additional segments can be dynamically modulated by phosphorylation, building upon previous work that showed that the external segments can regulate PDZ functionIn many multidomain proteins, the role of interdomain linkers is not well understood. By mimicking phosphorylation at Tyr, and in the linker of the PDZ3-linker-, construct from PSD-95, progressive increases in mobility in , due to linker phosphorylation were detected. This suggests that the linker plays a key role in supradomain assembly. We propose that linkers in MAGUKs and in other PDZ proteins can adopt varying degrees . . .
  

   

  

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