Coronin 1 trimerization is essential to protect pathogenic mycobacteria within macrophages from lysosomal delivery. Issue 21 (12th September 2014)

• Record Type: Journal Article
• Authors: BoseDasgupta, Somdeb; Pieters, Jean
• Is Part Of: FEBS letters. Volume 588:Issue 21(2014)
• Page Start: 3898
• Page End: 3905
• Publication Date: 2014-09-12
• Subjects: Coronin 1 -- Coiled coil -- Trimerization -- Pathogenic mycobacteria -- Macrophages; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2014.08.036
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Coronin 1 is a member of the evolutionarily conserved coronin protein family. Coronin proteins are characterized by the presence of a central WD repeat and a C‐terminal coiled coil that in coronin 1 is responsible for trimerization. Coronin 1 was identified as a host protein protecting intracellularly residing mycobacteria from degradation by activating the Ca 2+ /calcineurin pathway but whether or not trimerization is essential for this function remains unknown. We here show that trimerization is essential to promote mycobacterial survival within macrophages and activate calcineurin. Furthermore, macrophage activation that induces serine‐phosphorylation on coronin 1 resulted in coronin 1 monomerization. These results suggest that modulation of coronin 1 oligomerization is an effective way to determine the outcome of a mycobacterial infection in macrophages. Abstract : Trimerization of coronin 1 is required for mycobacterial survival in macrophages. Phosphorylation of coronin 1 by interferon‐γ results in monomerization. Activation of calcineurin requires a trimeric form of coronin 1.