Ser⁷¹ Phosphorylation Inhibits Actin-Binding of Profilin-1 and Its Apoptosis-Sensitizing Activity.

ABSTRACT: The essential actin-binding factor profilin-1 (Pfn1) is a non-classical tumor suppressor with the abilities toboth inhibit cellular proliferation and augment chemotherapy-induced apoptosis. Besides actin, Pfn1 interacts with proteins harboring the poly-L-proline (PLP) motifs. Our recent work demonstrated that both nuclear localization and PLP-binding are required for tumor growth inhibition by Pfn1, and this is at least partially due to Pfn1 association with the PLP-containing ENL protein in the Super Elongation Complex (SEC) and the transcriptional inhibition of pro-cancer genes. In this paper, by identifying a phosphorylation event of Pfn1 at Ser⁷¹ capable of inhibiting its actin-binding and nuclear export, we provide in vitro and in vivo evidence that chemothera

SUBMITTER: Wang F 

PROVIDER: S-EPMC8255618 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature