Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2047452 | FEBS Letters | 2015 | 8 Pages |
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.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Danièle Moes, Céline Hoffmann, Monika Dieterle, Flora Moreau, Katrin Neumann, Jessica Papuga, Angela Tavares Furtado, André Steinmetz, Clément Thomas,