IndraLab

Statements

HACE1 ubiquitinates RAC1 on K147. 7 / 7
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"The overexpression of HACE1 enhanced Rac1 polyubiquitination compared with control cells, whereas the overexpression of catalytically inactive HACE1 (C876S) showed no change in levels of Rac1 polyubiquitination (XREF_FIG) 16 Moreover, to verify that HACE1 ubiquitylation of Rac1 occurs at lysine 147 (citation), we ectopically expressed HA tagged wild-type Rac1 as well as a K147R mutant."
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"GTP-bound Rac1 is ubiquitylated by Hace1 at lysine (K)-147 (ref. xref )."
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"Thus, the decrease in levels of activated Rac1 in HACE1 overexpressing MCF7 cells is due to the proteosomal degradation of polyubiquitination of Rac1 at lysine 147 by HACE1."
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"As a substrate of Hace1, Rho GTPase Rac1 can be ubiquitylated at lysine 147 by HACE1."
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"Castillo-Lluva et al. further showed that HACE1 catalyzes polyubiquitination of Rac1 at lysine 147 following its activation by a migration stimulus, such as hepatocyte growth factor (HGF), resulting in Rac1 degradation by the proteasome."
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"Ubiquitination of Rac1 at Lys147 by the E3 ligase HACE1 (a tumor suppressor) is another described post-translational modification that is required for proteasomal degradation of the GTP-bound protein."
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"It is interesting to note that HACE1 ubiquitylates Rac1 on Lys147 XREF_BIBR, which is remote from the regions that are structurally sensitive to the bound nucleotide; furthermore, this residue is fully accessible in inactive Rac1 bound to RhoGDI XREF_BIBR."
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