Publications by authors named "Sigalit Sukenik"
Maintaining 26S proteasome activity under diverse physiological conditions is a fundamental requirement in order to maintain cellular proteostasis. Several quantitative and qualitative mechanisms have evolved to ensure that ubiquitin-proteasome system (UPS) substrates do not accumulate and lead to promiscuous protein-protein interactions that, in turn, lead to cellular malfunction. In this report, we demonstrate that Arsenite Inducible Regulatory Particle-Associate Protein (AIRAP), previously reported as a proteasomal adaptor required for maintaining proteasomal flux during arsenite exposure, can directly bind arsenite molecules.
View Article and Find Full Text PDFArticle Synopsis
- The assembly of signalosomes, crucial for T cell and mast cell signaling, requires the adaptor protein LAT, which interacts with cytosolic proteins from the Grb2 family.
- Research revealed that the protein Gads from the Grb2 family can dimerize via a specific SH2 domain interface, enhancing its binding to LAT molecules that are fully phosphorylated.
- Mutations that disrupt this dimerization reduce Gads' cooperativity and effectiveness in signaling, suggesting that proper Gads-LAT interaction boosts the cell's sensitivity to antigens by optimizing signalosome formation.