AIM1 is an actin-binding protein that suppresses cell migration and micrometastatic dissemination

Nat Commun. 2017 Jul 26;8(1):142. doi: 10.1038/s41467-017-00084-8.


A defining hallmark of primary and metastatic cancers is the migration and invasion of malignant cells. These invasive properties involve altered dynamics of the cytoskeleton and one of its major structural components β-actin. Here we identify AIM1 (absent in melanoma 1) as an actin-binding protein that suppresses pro-invasive properties in benign prostate epithelium. Depletion of AIM1 in prostate epithelial cells increases cytoskeletal remodeling, intracellular traction forces, cell migration and invasion, and anchorage-independent growth. In addition, decreased AIM1 expression results in increased metastatic dissemination in vivo. AIM1 strongly associates with the actin cytoskeleton in prostate epithelial cells in normal tissues, but not in prostate cancers. In addition to a mislocalization of AIM1 from the actin cytoskeleton in invasive cancers, advanced prostate cancers often harbor AIM1 deletion and reduced expression. These findings implicate AIM1 as a key suppressor of invasive phenotypes that becomes dysregulated in primary and metastatic prostate cancer.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / metabolism
  • Actins / genetics
  • Actins / metabolism*
  • Animals
  • Cell Line
  • Cell Line, Tumor
  • Cell Movement*
  • Crystallins / genetics
  • Crystallins / metabolism*
  • HEK293 Cells
  • Humans
  • Male
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mice
  • Microscopy, Electron, Transmission
  • Microscopy, Fluorescence
  • Neoplasm Invasiveness
  • Neoplasm Micrometastasis
  • Prostatic Neoplasms / genetics
  • Prostatic Neoplasms / metabolism*
  • Prostatic Neoplasms / ultrastructure
  • Protein Binding
  • RNA Interference
  • Transplantation, Heterologous


  • Actins
  • CRYBG1 protein, human
  • Crystallins
  • Membrane Proteins