The pH sensibility of actin-bundling LIM proteins is governed by the acidic properties of their C-terminal domain

Danièle Moes, Céline Hoffmann, Monika Dieterle, Flora Moreau, Katrin Neumann, Jessica Papuga, Angela Tavares Furtado, André Steinmetz, Clément Thomas*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)

Abstract

Actin-bundling Arabidopsis LIM proteins are subdivided into two subfamilies differing in their pH sensitivity. Widely-expressed WLIMs are active under low and high physiologically-relevant pH conditions, whereas pollen-enriched PLIMs are inactivated by pH values above 6.8. By a domain swapping approach we identified the C-terminal (Ct) domain of PLIMs as the domain responsible for pH responsiveness. Remarkably, this domain conferred pH sensitivity to LIM proteins, when provided "in trans" (i.e., as a single, independent, peptide), indicating that it operates through the interaction with another domain. An acidic 6xc-Myc peptide functionally mimicked the Ct domain of PLIMs and efficiently inhibited LIM actin bundling activity under high pH conditions. Together, our data suggest a model where PLIMs are regulated by an intermolecular interaction between their acidic Ct domain and another, yet unidentified, domain.

Original languageEnglish
Pages (from-to)2312-2319
Number of pages8
JournalFEBS Letters
Volume589
Issue number18
DOIs
Publication statusPublished - 12 Aug 2015

Keywords

  • Actin-bundling
  • Cytoskeleton
  • LIM domain
  • c-Myc
  • pH responsiveness

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