A novel isoform of tensin-1 promotes actin filament assembly for efficient erythroblast enucleation.

ABSTRACT:

Abstract

Mammalian red blood cells are generated via a terminal erythroid differentiation pathway culminating in cell polarization and enucleation. Actin filament (F-actin) polymerization is critical for enucleation, but the underlying molecular regulatory mechanisms remain poorly understood. We used publicly available RNA sequencing and proteomic data sets to mine for actin-regulatory factors differentially expressed during human erythroid differentiation and discovered that a focal adhesion (FA) protein, tensin-1 (TNS1), dramatically increases in expression late in differentiation. Remarkably, we found that differentiating human CD34+ cells express a novel truncated form of TNS1 (erythroid TNS1 [eTNS1]; Mr ∼125 kDa) missing the N-terminal half of the protein containing the actin-

SUBMITTER: Ghosh A 

PROVIDER: S-EPMC12753235 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature