Amazing stability of the arginine-phosphate electrostatic interaction

Amina S. Woods, Sergi Ferré

Research output: Contribution to journalArticlepeer-review

176 Scopus citations


Electrostatic interactions between a basic epitope containing adjacent arginine residues and an acidic epitope containing a phosphorylated serine are involved in receptor heteromerization. In the present study, we demonstrate that this arginine-phosphate electrostatic interaction possesses a "covalent-like" stability. Hence, these bonds can withstand fragmentation by mass spectrometric collision-induced dissociation at energies similar to those that fragment covalent bonds and they demonstrate an extremely low dissociation constant by plasmon resonance. The present work also highlights the importance of phosphorylation-dephosphorylation events in the modulation of this electrostatic attraction. Phosphorylation of the acidic epitope, a casein kinase one consensus site, makes it available to interact with the basic epitope. On the other hand, phosphorylation of serine and/or threonine residues adjacent to the basic epitope, a protein kinase A consensus site, slows down the attraction between the epitopes. Although analyzed here in the frame of receptor heteromerization, the arginine-phosphate electrostatic interaction most likely represents a general mechanism in protein-protein interactions.

Original languageEnglish (US)
Pages (from-to)1397-1402
Number of pages6
JournalJournal of Proteome Research
Issue number4
StatePublished - Jul 2005
Externally publishedYes


  • CK1
  • Electrostatic interaction
  • Phosphorylation
  • PKA
  • Receptor heteromers

ASJC Scopus subject areas

  • Genetics
  • Biotechnology
  • Biochemistry


Dive into the research topics of 'Amazing stability of the arginine-phosphate electrostatic interaction'. Together they form a unique fingerprint.

Cite this