 GLUE Domain | |
|
Class:Phospholipid binding
| |
|
Structure:
| |
|
Domain binding and function:
The GLUE (GRAM-like ubiquitin-binding in EAP45) domain structure has a typical PH domain architecture with two curved β sheets forming a barrel-like structure and one long α helix. Although the GLUE domain structurally resembles a split PH domain, the phosphoinositide pocket is clearly different that of the PH domain. The major components of the ESCRT complex consists of proteins recruited at different stages of the vesicular transport pathway. The GLUE domain plays a critical role in its ability to bind PtdIns3p and translocate Vps36 to endosomes. The affinity of the GLUE domain to bind PtdIns3p-containing vesicles is approximately 0.1μM. Mutations within the GLUE domain inhibit lipid binding and result in defects in the sorting of ubiquitinated cargo. Furthermore, the GLUE domain of Vps36 contains two integral NSF domains that recognize ubiquitin.
| |
|
Examples of Proteins:
| GLUE proteins |
|
Binding Partner |
| Vps36 |  |
PtsIns3P, PtdIns4P, PtdIns(3,4)P2, PtdIns(3,5) P2
|
|
|
|
| |
|
Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
| |
|
