Related Experiment Video
Updated: May 28, 2026

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
Published on: June 30, 2019
A negatively charged domain of LAT mediates its interaction with the active form of Lck
Panagiotis S Kabouridis1, David A Isenberg, Elizabeth C Jury
1William Harvey Research Institute , Barts and The London School of Medicine and Dentistry, Queen Mary University of London, Charterhouse Square, London, UK. p.s.kabouridis@qmul.ac.uk
Abstract:
We have shown previously that in T cells, LAT co-immunoprecipitates with the active but not the inactive-'closed' form of Lck, and that this interaction impacts negatively on Lck activity. Here we confirm that activation of T cells induced a transient LAT/Lck association within 4 min after stimulation, returning to basal levels by 30 min. Interestingly, autoimmune T cells isolated from patients with systemic lupus erythematosus, which contain a larger pool of active Lck and LAT, exhibited increased LAT/Lck association compared to healthy controls. To identify the domain of LAT responsible for its interaction with active Lck, a series of LAT truncation mutants were constructed and tested in co-immunoprecipitation experiments. We found that the segment comprising residues 112-126 of human LAT is required for its interaction with Lck. This domain is rich in negatively charged amino acids and is conserved among different species. Therefore, in addition to the conserved tyrosines, the 112-126 domain identified here could be important for certain functions of LAT in T cells.
More Related Videos
15:05Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
Published on: May 20, 2020
07:33Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction
Published on: April 26, 2011
Related Concept Videos
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Mechanisms of Membrane Domain Formation
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Membrane Domains
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Mechanism of Lamellipodia Formation
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...