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The pH sensibility of actin‐bundling LIM proteins is governed by the acidic properties of their C‐terminal domain
Author(s) -
Moes Danièle,
Hoffmann Céline,
Dieterle Monika,
Moreau Flora,
Neumann Katrin,
Papuga Jessica,
Furtado Angela Tavares,
Steinmetz André,
Thomas Clément
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.07.033
Subject(s) - domain (mathematical analysis) , actin , chemistry , biophysics , terminal (telecommunication) , peptide , biochemistry , microbiology and biotechnology , biology , computer science , mathematical analysis , telecommunications , mathematics
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.