Direct Interaction Between Anthrax Toxin Receptor 1 and the Actin Cytoskeleton
Overview
Authors
Affiliations
The protective antigen component of anthrax toxin binds the I domain of the anthrax toxin receptors, ANTXR1 and ANTXR2, in a manner akin to how integrins bind their ligands. The I domains of integrins and ANTXR1 both have high- and low-affinity conformations, and the cytosolic tails of these receptors associate with the actin cytoskeleton. The association of ANTXR1 with the cytoskeleton correlates with weakened binding to PA, although a mechanistic explanation for this observation is lacking. Here, we identified a segment in the cytoplasmic tail of ANTXR1 required for its association with the cytoskeleton. We synthesized a 60-mer peptide based on this segment and demonstrated a direct interaction between the peptide and beta-actin, indicating that in contrast to integrins, ANTXR1 does not use an adaptor to bind the cytoskeleton. This peptide orders actin filaments into arrays, demonstrating an actin bundling activity that is novel for a membrane protein.
Przyklenk M, Karmacharya S, Bonasera D, Pasanen-Zentz A, Kmoch S, Paulsson M Sci Rep. 2024; 14(1):9321.
PMID: 38653789 PMC: 11039612. DOI: 10.1038/s41598-024-59901-y.
Thuault S, Mamelonet C, Salameh J, Ostacolo K, Chanez B, Salaun D Sci Rep. 2020; 10(1):6787.
PMID: 32321993 PMC: 7176661. DOI: 10.1038/s41598-020-63926-4.
Cheng B, Liu Y, Zhao Y, Li Q, Liu Y, Wang J Sci Rep. 2019; 9(1):12642.
PMID: 31477767 PMC: 6718418. DOI: 10.1038/s41598-019-49100-5.
Converging physiological roles of the anthrax toxin receptors.
Sergeeva O, van der Goot F F1000Res. 2019; 8.
PMID: 31448094 PMC: 6694455. DOI: 10.12688/f1000research.19423.1.
TEM8 functions as a receptor for uPA and mediates uPA-stimulated EGFR phosphorylation.
Zhang L, Shao Y, Gao L, Liu J, Xi Y, Xu Y Cell Commun Signal. 2018; 16(1):62.
PMID: 30241478 PMC: 6151050. DOI: 10.1186/s12964-018-0272-8.