| Title |
-
Rabring7 Degrades c-Myc through Complex Formation with MM-1
|
|---|
| Creator |
Iguchi-Ariga, Sanae M. M.
|
|---|
| Rights |
-
-
http://creativecommons.org/licenses/by/3.0/
|
|---|
| Subject |
|
|---|
| Description |
Other
-
We have reported that a novel c-Myc-binding protein, MM-1, repressed E-box-dependent transcription and transforming activities of c-Myc and that a mutation of A157R in MM-1, which is often observed in patients with leukemia or lymphoma, abrogated all of the repressive activities of MM-1 toward c-Myc, indicating that MM-1 is a novel tumor suppressor. MM-1 also binds to the ubiquitin-proteasome system, leading to degradation of c-Myc. In this study, we identified Rabring7, a Rab7-binding and RING finger-containing protein, as an MM-1-binding protein, and we found that Rabring7 mono-ubiquitinated MM-1 in the cytoplasm without degradation of MM-1. Rabring7 was also found to bind to c-Myc and to ubiquitinate c-Myc in a threonine 58-dependent manner. When c-Myc was co-transfected with MM-1 and Rabring7, c-Myc was degraded. Furthermore, it was found that c-Myc was stabilized in MM-1-knockdown cells even when Rabring7 was transfected and that Rabring7 was bound to and co-localized with MM-1 and c-Myc after MM-1 and Rabring7 had been translocated from the cytoplasm to the nucleus. These results suggest that Rabring7 stimulates c-Myc degradation via mono-ubiquitination of MM-1.
|
|---|
| Publisher | Public Library of Science
|
|---|
| Date | Issued 2012-07-23
|
|---|
| Language | eng |
|---|
| NIItype | journal article |
|---|
| Versiontype | VoR |
|---|
| Identifier | URI http://hdl.handle.net/2115/50059
|
|---|
| Relation |
-
isIdenticalTo
DOI
https://doi.org/10.1371/journal.pone.0041891
|
|---|
| Journal | |
|---|
| File |
|
|---|
| Oaidate | 2017-10-15T15:00:00Z |
|---|
