A novel interface between the N-terminal and coiled-coil domain of STAT1 functions in an auto-inhibitory manner.

ABSTRACT:

Background

STAT1 is an intracellular signaling molecule that is crucially involved in the regulation of the innate immune system by activation of defense mechanisms against microbial pathogens. Phosphorylation-dependent activation of the STAT1 transcription factor is associated with a conversion from an antiparallel to parallel dimer configuration, which after nuclear import binds to DNA. However, not much is known about the specific intermolecular interactions that stabilize unphosphorylated, antiparallel STAT1 complexes prior to activation.

Results

In this study, we identified a previously unknown interdimeric interaction site, which is involved in the termination of STAT1 signaling. Introduction of the glutamic acid-to-alanine point mutation E169A in the coiled-coil domai

SUBMITTER: Remling L 

PROVIDER: S-EPMC10331961 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature