AURORA A interacts with DICER and SETD2 to promote S-phase progression

ABSTRACT: The oncogenic kinase AURORA A is essential for mitotic progression, and its catalytic inhibition arrests cells at the G2/M-transition. Unexpectedly, degradation of AURORA A by PROTACs (proteolysis targeting chimeras) induces profound S-phase defects, revealing a non-catalytic scaffolding function of AURORA A. To dissect this function, we profile the AURORA A S-phase interactome and identify multiple RNA-binding proteins not characterized as AURORA A substrates. Among these, the ribonuclease DICER directly associates with AURORA A to form an abundant nuclear complex. RNA degradation shifts AURORA A, DICER, and additional RNA-binding proteins from heavy to light gradient fractions, implicating RNA-dependent complex function. In contrast, PROTAC-mediated depletion of AURORA A alters the gradi

SUBMITTER: Juliane Müller 

PROVIDER: S-SCDT-10_1038-S44319-026-00850-0 | biostudies-other |

REPOSITORIES: biostudies-other