Disease relevance of USP6NL

• RN-tre is ubiquitously expressed and maps to 10p13, a region known to be involved in translocations in various leukemias [1].

High impact information on USP6NL

• Through its src homology-3 domain, Eps8 interacts with RN-tre [2].
• We show that RN-tre is a Rab5 GTPase-activating protein, whose activity is regulated by the EGFR [2].
• Overexpression of RN-tre blocks the internalization of both proteins, consistent with its function as a negative regulator of Rab5 and endocytosis [3].
• Finally, comparison of the structure and biological activities of RN-tre and of the tre oncogene product, provided insight into the mechanism of oncogenic activation of tre [4].
• RN-tre identifies a family of tre-related proteins displaying a novel potential protein binding domain [1].

Biological context of USP6NL

• A role for RN-tre in cell proliferation was suggested by the finding that a C-terminal truncated mutant was able to confer proliferative advantage and reduced serum-requirement to NIH3T3 fibroblasts [4].

Other interactions of USP6NL

• Furthermore, RN-tre diverts Eps8 from its Rac-activating function, resulting in the attenuation of Rac signalling [2].

References