PIM1 accelerates prostate cancer cell motility by phosphorylating actin capping proteins.

ABSTRACT:

Background

The PIM family kinases promote cancer cell survival and motility as well as metastatic growth in various types of cancer. We have previously identified several PIM substrates, which support cancer cell migration and invasiveness. However, none of them are known to regulate cellular movements by directly interacting with the actin cytoskeleton. Here we have studied the phosphorylation-dependent effects of PIM1 on actin capping proteins, which bind as heterodimers to the fast-growing actin filament ends and stabilize them.

Methods

Based on a phosphoproteomics screen for novel PIM substrates, we have used kinase assays and fluorescence-based imaging techniques to validate actin capping proteins as PIM1 substrates and interaction partners. We have analysed the functio

SUBMITTER: Santio NM 

PROVIDER: S-EPMC7414696 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature