Abstract：
:The E3 ubiquitin ligase HUWE1, deregulated in carcinoma, has been implicated in tumor formation. Here, we uncover a role for HUWE1 in cell migration and invasion through degrading the RAC activator TIAM1, implying an additional function in malignant progression. In MDCKII cells in response to HGF, HUWE1 catalyzes TIAM1 ubiquitylation and degradation predominantly at cell-cell adhesions, facilitating junction disassembly, migration, and invasion. Depleting HUWE1 or mutating the TIAM1 ubiquitylation site prevents TIAM1 degradation, antagonizing scattering, and invasion. Moreover, simultaneous depletion of TIAM1 restores migration and invasion in HUWE1-depleted cells. Significantly, we show that HUWE1 stimulates human lung cancer cell invasion through regulating TIAM1 stability. Finally, we demonstrate that HUWE1 and TIAM1 protein levels are inversely correlated in human lung carcinomas. Thus, we elucidate a critical role for HUWE1 in regulating epithelial cell-cell adhesion and provide additional evidence that ubiquitylation contributes to spatiotemporal control of RAC.
journal_name
Cell Repjournal_title
Cell reportsauthors
Vaughan L,Tan CT,Chapman A,Nonaka D,Mack NA,Smith D,Booton R,Hurlstone AF,Malliri Adoi
10.1016/j.celrep.2014.12.012subject
Has Abstractpub_date
2015-01-06 00:00:00pages
88-102issue
1issn
2211-1247pii
S2211-1247(14)01041-9journal_volume
10pub_type
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