Genetic ablation of the c-Cbl ubiquitin ligase domain results in increased energy expenditure and improved insulin action

Diabetes. 2006 Dec;55(12):3411-7. doi: 10.2337/db06-0955.

Abstract

Casitas b-lineage lymphoma (c-Cbl) is a multiadaptor protein with E3-ubiquitin ligase activity residing within its RING finger domain. We have previously reported that c-Cbl-deficient mice exhibit elevated energy expenditure, reduced adiposity, and improved insulin action. In this study, we examined mice expressing c-Cbl protein with a loss-of-function mutation within the RING finger domain (c-Cbl(A/-) mice). Compared with control animals, c-Cbl(A/-) mice display a phenotype that includes reduced adiposity, despite greater food intake; reduced circulating insulin, leptin, and triglyceride levels; and improved glucose tolerance. c-Cbl(A/-) mice also display elevated oxygen consumption (13%) and are protected against high-fat diet-induced obesity and insulin resistance. Unlike c-Cbl(A/-) mice, mice expressing a mutant c-Cbl with the phosphatidylinositol (PI) 3-kinase binding domain ablated (c-Cbl(F/F) mice) exhibited an insulin sensitivity, body composition, and energy expenditure similar to that of wild-type animals. These results indicate that c-Cbl ubiquitin ligase activity, but not c-Cbl-dependent activation of PI 3-kinase, plays a key role in the regulation of whole-body energy metabolism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipose Tissue / anatomy & histology*
  • Animals
  • Blood Glucose / metabolism
  • Calorimetry, Indirect
  • DNA Primers
  • Energy Metabolism*
  • Gene Deletion*
  • Glucose Tolerance Test
  • Insulin / physiology*
  • Kinetics
  • Mice
  • Mice, Knockout
  • Phosphatidylinositol 3-Kinases / metabolism
  • Polymerase Chain Reaction
  • Proto-Oncogene Proteins c-cbl / deficiency*
  • Thinness / genetics

Substances

  • Blood Glucose
  • DNA Primers
  • Insulin
  • Proto-Oncogene Proteins c-cbl
  • Phosphatidylinositol 3-Kinases
  • Cbl protein, mouse