Filamin A interacting protein 1-like as a therapeutic target in cancer

Mijung Kwon, Steven K. Libutti

Research output: Contribution to journalReview articlepeer-review

14 Scopus citations


Introduction: Filamin A interacting protein 1-like (FILIP1L) is a novel tumor suppressor-like protein that has its expression downregulated in various cancers through promoter hypermethylation. When overexpressed, FILIP1L inhibits cancer cell invasion and metastasis through the inhibition of canonical WNT signaling. Areas covered: This review gives an overview of the structure and isoforms, gene expression and cellular location of FILIP1L, and how FILIP1L inhibits cancer invasion and metastasis. Furthermore, the review discusses the potential mechanism by which FILIP1L inhibits cancer metastasis through inhibiting canonical WNT signaling and thus blocking downstream β-catenin transcriptional targets. Expert opinion: By inhibiting β-catenin, the key transcriptional factor of the canonical WNT signaling pathway, FILIP1L could block various downstream pathways that are regulated by β-catenin transcriptional targets. FILIP1L could therefore have great potential as a novel cancer therapeutic target. However, in order to fulfill its therapeutic potential, its precise mechanism of action of antimetastatic activity has to be identified. In addition, the physiological role of FILIP1L and its relationship with other isoforms needs to be characterized.

Original languageEnglish (US)
Pages (from-to)1435-1447
Number of pages13
JournalExpert Opinion on Therapeutic Targets
Issue number12
StatePublished - Dec 1 2014


  • Epithelial-to-mesenchymal transition
  • Filamin A interacting protein 1-like
  • Invasion
  • MMP
  • Metastasis
  • Ovarian cancer
  • Pancreatic cancer
  • WNT signaling
  • β-catenin degradation

ASJC Scopus subject areas

  • Molecular Medicine
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry


Dive into the research topics of 'Filamin A interacting protein 1-like as a therapeutic target in cancer'. Together they form a unique fingerprint.

Cite this