Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Recognition and ubiquitination of Notch by Itch, a hect-type E3 ubiquitin ligase.

http://www.ncbi.nlm.nih.gov/pubmed/10940313

Genetic studies identified Itch, which is a homologous to the E6-associated protein carboxyl terminus (Hect) domain-containing E3 ubiquitin-protein ligase that is disrupted in non-agouti lethal mice or Itchy mice. Itch-deficiency results in abnormal immune responses and constant itching in the skin. Here, Itch was shown to associate with Notch, a protein involved in cell fate decision in many mammalian cell types, including cells in the immune system. Itch binds to the N-terminal portion of the Notch intracellular domain via its WW domains and promotes ubiquitination of Notch through its Hect ubiquitin ligase domain. Thus, Itch may participate in the regulation of immune responses by modifying Notch-mediated signaling.

Pubmed ID: 10940313 RIS Download

Mesh terms: Animals | Humans | Jurkat Cells | Ligases | Membrane Proteins | Precipitin Tests | Protein Binding | Protein Structure, Tertiary | Pruritus | Receptors, Notch | Recombinant Fusion Proteins | Signal Transduction | Transfection | Ubiquitin-Protein Ligases | Ubiquitins

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NIDDK NIH HHS, Id: DK56558

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.