Beyond the RING: CBL proteins as multivalent adapters

Oncogene. 2001 Oct 1;20(44):6382-402. doi: 10.1038/sj.onc.1204781.

Abstract

Following discovery of c-Cbl, a cellular form of the transforming retroviral protein v-Cbl, multiple Cbl-related proteins have been identified in vertebrate and invertebrate organisms. c-Cbl and its homologues are capable of interacting with numerous proteins involved in cell signaling, including various molecular adapters and protein tyrosine kinases. It appears that Cbl proteins play several functional roles, acting both as multivalent adapters and inhibitors of various protein tyrosine kinases. The latter function is linked, to a substantial extent, to the E3 ubiquitin-ligase activity of Cbl proteins. Experimental evidence for these functions, interrelations between them, and their biological significance are addressed in this review, with the main accent placed on the adapter functions of Cbl proteins.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Humans
  • Phosphorylation
  • Protein Binding
  • Protein Structure, Tertiary
  • Proto-Oncogene Proteins / chemistry*
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins / physiology*
  • Proto-Oncogene Proteins c-cbl
  • Serine / metabolism
  • Signal Transduction
  • Threonine / metabolism
  • Tissue Distribution
  • Ubiquitin-Protein Ligases*

Substances

  • Proto-Oncogene Proteins
  • Threonine
  • Serine
  • Proto-Oncogene Proteins c-cbl
  • Ubiquitin-Protein Ligases
  • CBL protein, human