Spatiotemporal regulation of the ubiquitinated cargo-binding activity of Rabex-5 in the endocytic pathway.

ABSTRACT:

Background

The regulatory mechanism underlying the interaction of the Rabex-5 MIU domain with ubiquitinated cargos remains unclear.

Results

Rabex-5 guanine nucleotide exchange factor (GEF) mutants affected interactions of ubiquitinated cargos.

Conclusion

GDP/GTP exchange in the GEF domain controls the MIU domain interactions with the ubiquitinated cargos.

Significance

Rabex-5 GEF activity acts as an intramolecular switch for spatiotemporal trafficking of the ubiquitinated cargos. Ubiquitin (Ub)-dependent endocytosis of membrane proteins requires precise molecular recognition of ubiquitinated cargo by Ub-binding proteins (UBPs). Many UBPs are often themselves monoubiquitinated, a mechanism referred to as coupled monoubiquitination, which prevents them from bindi

SUBMITTER: Aikawa Y 

PROVIDER: S-EPMC3504772 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature