14-3-3 protein interactions

A complex of MAST1 and 14-3-3 regulates Tau phosphorylation in the developing cortex

This study identifies MAST1 and 14-3-3 as regulators of Tau phosphorylation in the developing cortex through interactions and phosphorylation events.

Liquid-liquid phase separation and amyloid aggregation in the 14-3-3 protein family

This study investigates the phase separation and amyloid aggregation properties of 14-3-3 protein isoforms, finding that some forms can accelerate α-synuclein aggregation and form heterotypical droplets with α-synuclein.

Analysis of the Modulation of RAF Signaling by 14-3-3 Proteins

The paper develops a mathematical model of RAF activation modulated by 14-3-3 proteins, showing that weak binding stabilized by avidity explains experimental observations of RAF activation upon 14-3-3 overexpression.

The Holdup Multiplex, an assay for high-throughput measurement of protein-ligand affinity constants using a mass-spectrometry readout

The paper introduces a high-throughput mass-spectrometry-based assay to measure protein-ligand affinity constants, demonstrating its application to 14-3-3 isoforms and phosphopeptides.

Multi-dimensional demarcation of phylogenetic groups of plant 14-3-3 isoforms using biochemical signatures

This study identifies biochemical signatures that categorize plant 14-3-3 isoforms into epsilon and non-epsilon groups, revealing key amino acid positions responsible for phylogenetic demarcation.

Negative Charges, Not Necessary Phosphorylation, are Required for Ligand Recognition by 14-3-3 Proteins

This study shows that negative charges, not phosphorylation, are required for 14-3-3ε binding, with at least one negative charge needed and two for high affinity.

PermaPhosSer: autonomous synthesis of functional, permanently phosphorylated proteins

The paper develops a system to autonomously produce phosphorylated proteins in E. coli, demonstrating that non-hydrolyzable phosphoserine mimics phosphoserine function in three biological contexts.