P120 catenin: An essential regulator of cadherin stability, adhesion-induced signaling, and cancer progression

Antonis Kourtidis, Siu P. Ngok, Panos Z. Anastasiadis

Research output: Chapter in Book/Report/Conference proceedingChapter

93 Scopus citations


p120 catenin is the best studied member of a subfamily of proteins that associate with the cadherin juxtamembrane domain to suppress cadherin endocytosis. p120 also recruits the minus ends of microtubules to the cadherin complex, leading to junction maturation. In addition, p120 regulates the activity of Rho family GTPases through multiple interactions with Rho GEFs, GAPs, Rho GTPases, and their effectors. Nuclear signaling is affected by the interaction of p120 with Kaiso, a transcription factor regulating Wnt-responsive genes as well as transcriptionally repressing methylated promoters. Multiple alternatively spliced p120 isoforms and complex phosphorylation events affect these p120 functions. In cancer, reduced p120 expression correlates with reduced E-cadherin function and with tumor progression. In contrast, in tumor cells that have lost E-cadherin expression, p120 promotes cell invasion and anchorage-independent growth. Furthermore, p120 is required for Src-induced oncogenic transformation and provides a potential target for future therapeutic interventions.

Original languageEnglish (US)
Title of host publicationThe Molecular Biology of Cadherins
PublisherElsevier B.V.
Number of pages24
ISBN (Print)9780123943118
StatePublished - 2013

Publication series

NameProgress in Molecular Biology and Translational Science
ISSN (Print)1877-1173


  • Cell-cell junctions
  • E-Cadherin
  • EMT
  • Endocytosis
  • Kaiso
  • Microtubules
  • RTK
  • Rac1
  • RhoA
  • Src

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology


Dive into the research topics of 'P120 catenin: An essential regulator of cadherin stability, adhesion-induced signaling, and cancer progression'. Together they form a unique fingerprint.

Cite this