David Chakravorty
@davechakravorty.bsky.social
Associate Research Professor studying heterotrimeric G proteins (mostly but not exclusively of the plant variety) at Penn State University
Reposted by David Chakravorty
The blue-light receptor CRY1 serves as a switch to balance photosynthesis and plant defense www.cell.com/cell-host-mi...
The blue-light receptor CRY1 serves as a switch to balance photosynthesis and plant defense
Previously, photoreceptors were regarded as a switch for growth control. Hao et al. found that CRY1 acts as dual-control switch to regulate the growth-defense trade-off. LURP1 re-localizes to the plasma membrane upon N-terminal palmitoylation in a calcium- and blue-light-dependent manner after flg22 elicitation to activate immune receptors and promote immunity.
www.cell.com
December 27, 2024 at 11:48 PM
The blue-light receptor CRY1 serves as a switch to balance photosynthesis and plant defense www.cell.com/cell-host-mi...
Reposted by David Chakravorty
The Arabidopsis blue-light photoreceptor CRY2 is active in darkness to inhibit root growth
www.cell.com/cell/fulltex...
#plantscience
www.cell.com/cell/fulltex...
#plantscience
The Arabidopsis blue-light photoreceptor CRY2 is active in darkness to inhibit root growth
CRY2 interacts with the cell-division-promoting factors FL1 and FL3 to inhibit primary-root
elongation in darkness, while blue light relieves this inhibition.
www.cell.com
November 16, 2024 at 7:57 AM
The Arabidopsis blue-light photoreceptor CRY2 is active in darkness to inhibit root growth
www.cell.com/cell/fulltex...
#plantscience
www.cell.com/cell/fulltex...
#plantscience
Reposted by David Chakravorty
"Changes in intracellular loop conformation alone can significantly affect G-protein binding and signaling... without first affecting the transmembrane helices... [suggesting] one could design allosteric ligands that act via this non-canonical activation mechanism at... important GPCR drug targets."
A non-canonical mechanism of GPCR activation - Nature Communications
Ligands that activate GPCRs generally do so by stabilizing a particular conformation of the transmembrane helices. Here, the authors reveal a distinct activation mechanism where a ligand instead stabi...
www.nature.com
November 19, 2024 at 6:06 PM
"Changes in intracellular loop conformation alone can significantly affect G-protein binding and signaling... without first affecting the transmembrane helices... [suggesting] one could design allosteric ligands that act via this non-canonical activation mechanism at... important GPCR drug targets."