IndraLab

Statements

USP14 binds CXCR4. 17 / 19
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"CXCL12, a CXCR4 agonist, induces a time-dependent association of USP14 with CXCR4, or its C terminus, that is not mimicked by USP2A, USP4, or USP7, other members of the deubiquitination catalytic family."
19106094
sparser
"This study verified that CXCL12 incubation of HEK293 cells stably expressing the receptor and transiently expressing HA-USP14 leads to a time-dependent association of USP14 with CXCR4 ( xref )."
19106094
reach
"Of further interest was our finding that USP14 interaction with CXCR4 is relatively selective, compared with other members of the USP family, including USP2a, USP4, and USP7, which were evaluated using the same experimental strategy (XREF_FIG)."
19106094
sparser
"We were curious whether CXCL12 activation of CXCR4 might lead to redistribution of USP14 to CXCR4-containing membrane compartments, consistent with the ligand- and time-dependent association of USP14 with CXCR4 noted in xref ."
19106094
sparser
"A proteomics study revealed that the steady state level of USP14 was increased upon CXCL12 stimulation of target cells ( xref ), and preliminary studies revealed that ligand stimulation led to enhanced association of USP14 with the CXCR4."
19106094
sparser
"These data are consistent with the interpretation that not only does USP14 associate with CXCR4 in a ligand-modulated fashion (as in xref ), but also that USP14 recognizes this receptor as a substrate for deubiquitination."
19106094
reach
"The physical interaction of CXCR4 and USP14 is paralleled by USP14 catalyzed deubiquitination of the receptor; knockdown of endogenous USP14 by RNA interference (RNAi) blocks CXCR4 deubiquitination, whereas overexpression of USP14 promotes CXCR4 deubiquitination."
19106094
reach
"In summary, our findings demonstrate that CXCL12 activation of the CXCR4 leads to a dynamic ubiquitination and deubiquitination cycle and that USP14 preferentially interacts with and deubiquitinates CXCR4."
19106094
sparser
"CXCL12 Activation Leads to a Time-dependent Association of USP14 with CXCR4 —A previous series of experiments revealed the possibility that USP14 was a CXCR4-interacting protein ( xref )."
19106094
sparser
"USP14 interaction with CXCR4 is not mimicked by other deubiquitinating enzymes of the USP family evaluated, including USP2a, USP4, and USP7 ( xref )."
19106094
sparser
"The physical interaction of CXCR4 and USP14 is paralleled by USP14-catalyzed deubiquitination of the receptor; knockdown of endogenous USP14 by RNA interference (RNAi) blocks CXCR4 deubiquitination, whereas overexpression of USP14 promotes CXCR4 deubiquitination."
19106094
sparser
"The finding, however, that the C terminus of CXCR4 can directly interact with USP14 provides additional confirmation of a direct interaction between this enzyme and CXCR4."
19106094
biogrid
No evidence text available
19106094
sparser
"Of further interest was our finding that USP14 interaction with CXCR4 is relatively selective, compared with other members of the USP family, including USP2a, USP4, and USP7, which were evaluated using the same experimental strategy ( xref )."
19106094
biogrid
No evidence text available
19106094
sparser
"As a result to stimulation with the CXCL12 CXCR4 agonist, CXCR4 was found to be colocalized and interacting with USP14."
35069211
reach
"USP14 interaction with CXCR4 is not mimicked by other deubiquitinating enzymes of the USP family evaluated, including USP2a, USP4, and USP7 (XREF_FIG)."
19106094