A novel isoform of Tensin1 promotes actin filament assembly for efficient erythroblast enucleation.

ABSTRACT: Mammalian red blood cells are generated via a terminal erythroid differentiation pathway culminating in cell polarization and enucleation. Actin filament polymerization is critical for enucleation, but the molecular regulatory mechanisms remain poorly understood. We utilized publicly available RNA-seq and proteomics datasets to mine for actin-binding proteins and actin-nucleation factors differentially expressed during human erythroid differentiation and discovered that a focal adhesion protein-Tensin-1-dramatically increases in expression late in differentiation. Remarkably, we found that differentiating human CD34+ cells express a novel truncated form of Tensin-1 (eTNS1; M_r ~125 kDa) missing the N-terminal half of the protein, due to an internal mRNA translation start site res

SUBMITTER: Ghosh A 

PROVIDER: S-EPMC11702514 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature