Integrin signalling adaptors: not only figurants in the cancer story

Nat Rev Cancer. 2010 Dec;10(12):858-70. doi: 10.1038/nrc2967. Epub 2010 Nov 24.

Abstract

Current evidence highlights the ability of adaptor (or scaffold) proteins to create signalling platforms that drive cellular transformation upon integrin-dependent adhesion and growth factor receptor activation. The understanding of the biological effects that are regulated by these adaptors in tumours might be crucial for the identification of new targets and the development of innovative therapeutic strategies for human cancer. In this Review we discuss the relevance of adaptor proteins in signalling that originates from integrin-mediated cell-extracellular matrix (ECM) adhesion and growth factor stimulation in the context of cell transformation and tumour progression. We specifically underline the contribution of p130 Crk-associated substrate (p130CAS; also known as BCAR1), neural precursor cell expressed, developmentally down-regulated 9 (NEDD9; also known as HEF1), CRK and the integrin-linked kinase (ILK)-pinch-parvin (IPP) complex to cancer, along with the more recently identified p140 Cas-associated protein (p140CAP; also known as SRCIN1).

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing / physiology*
  • Adaptor Proteins, Vesicular Transport / physiology
  • Animals
  • Apoptosis
  • Cell Movement
  • Humans
  • Integrins / physiology*
  • Neoplasm Invasiveness
  • Neoplasms / etiology*
  • Phosphoproteins / physiology
  • Protein-Serine-Threonine Kinases / physiology
  • Proto-Oncogene Proteins c-crk / physiology
  • Receptor, ErbB-2 / physiology
  • Transforming Growth Factor beta / physiology

Substances

  • Adaptor Proteins, Signal Transducing
  • Adaptor Proteins, Vesicular Transport
  • CRK protein, human
  • Integrins
  • NEDD9 protein, human
  • Phosphoproteins
  • Proto-Oncogene Proteins c-crk
  • SNIP protein, human
  • Transforming Growth Factor beta
  • integrin-linked kinase
  • ERBB2 protein, human
  • Receptor, ErbB-2
  • Protein-Serine-Threonine Kinases