IndraLab

Statements

MCL1 binds JOSD1. 17 / 20
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"As shown in Fig. xref , the interaction between JOSD1 and MCL-1 was strikingly disrupted in TRAF4-deficient cells, while other deubiquitinases were not affected."
36535926
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"Likewise, compared with CAL27R-sgCtrl cells, the depletion of TRAF4 destroyed the interaction between JOSD1 and MCL-1, which was further enhanced in the presence of radiation (Fig. xref )."
36535926
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"MCL1 WT and S159D mutant (which is a phosphomimetic mutant in the GSK3β phosphorylation site), but not MCL1 S159A mutant (which abolished phosphorylation by GSK-3), substantially decreased the interaction between JOSD1 and MCL-1 in the presence of IR in CAL27R cells (Fig. xref )."
36535926
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"TRAF4 promoted Akt K63-linked ubiquitination and activation to suppress GSK3β activity and MCL-1 S159 phosphorylation, facilitating the interaction between MCL-1 and JOSD1, which ultimately promoted the stability and expression of MCL-1 to confer resistance to radiotherapy in OSCC cells (Fig. 7G)."
36535926
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"These results suggest that the phosphorylation of MCL-1 S159 disrupts the interaction between JOSD1 and MCL-1, and eventually induces MCL-1 ubiquitination and degradation in TRAF4-knockout OSCC cells."
36535926
sparser
"These results indicate that depletion of TRAF4 sensitizes OSCC cells to radiotherapy, which depends on disrupting the interaction of JOSD1 with MCL-1 to promote MCL-1 ubiquitination and degradation."
36535926
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"Our results indicated that depletion of TRAF4 disrupted the interaction between MCL-1 and JOSD1, particularly under IR treatment."
36535926
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"TRAF4 promoted Akt K63-linked ubiquitination and activation to suppress GSK3β activity and MCL-1 S159 phosphorylation, facilitating the interaction between MCL-1 and JOSD1, which ultimately promoted the stability and expression of MCL-1 to confer resistance to radiotherapy in OSCC cells (Fig. xref )."
36535926
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"Further research showed that curcumol-induced Mcl-1 Ser159 phosphorylation is required to disrupt the interaction between deubiquitinase JOSD1 and Mcl-1 and eventually induce Mcl-1 ubiquitination and degradation."
36869017
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"Likewise, compared with CAL27R-sgCtrl cells, the depletion of TRAF4 destroyed the interaction between JOSD1 and MCL-1, which was further enhanced in the presence of radiation (Fig. 5B)."
36535926
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"TRAF4 knockout inhibited the phosphorylation of Akt and upregulated GSK3β activity, resulting in increased myeloid cell leukemia-1 (MCL-1) S159 phosphorylation, which disrupted the interaction of MCL-1 with Josephin domain containing 1 (JOSD1), and ultimately induced MCL-1 ubiquitination and degradation."
36535926
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"MCL-1 phosphorylation disrupts the interaction between JOSD1 and MCL-1 in TRAF4- deficient OSCC cells."
36535926
sparser
"Further research showed that curcumol-induced Mcl-1 Ser159 phosphorylation is required to disrupt the interaction between deubiquitinase JOSD1 and Mcl-1 and eventually induce Mcl-1 ubiquitination and degradation."
36869017
reach
"As shown in Fig. 5A, the interaction between JOSD1 and MCL-1 was strikingly disrupted in TRAF4-deficient cells, while other deubiquitinases were not affected."
36535926
reach
"These results suggest that the phosphorylation of MCL-1 S159 disrupts the interaction between JOSD1 and MCL-1, and eventually induces MCL-1 ubiquitination and degradation in TRAF4-knockout OSCC cells."
36535926
reach
"Our results indicated that depletion of TRAF4 disrupted the interaction between MCL-1 and JOSD1, particularly under IR treatment."
36535926
reach
"MCL1 WT and S159D mutant (which is a phosphomimetic mutant in the GSK3β phosphorylation site), but not MCL1 S159A mutant (which abolished phosphorylation by GSK-3), substantially decreased the interaction between JOSD1 and MCL-1 in the presence of IR in CAL27R cells (Fig. 5E)."
36535926