IndraLab

Statements

USP13 binds Cohesin. 27 / 27
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"USP13 interacts with cohesin and regulates its ubiquitination in human cells."
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"As shown in xref D , the interaction between cohesin and USP13 was enhanced in cells arrested in the S phase when compared with asynchronous cycling cells, or cells arrested at other points in the cell cycle."
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"These data indicate that the interaction of USP13 with cohesin is cell cycle dependent—it is enhanced during DNA replication"
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"We next sought to determine which (if either) of these domains was required for the interaction of USP13 with cohesin."
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"These data demonstrate that the UBA1/2 domains are required for the interaction of USP13 with cohesin and that the ZnF domain is dispensable for the interaction of USP13 with cohesin."
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"We wondered whether ubiquitinated cohesin subunits were present primarily in the soluble fraction (where the USP13–cohesin complex resides), in the chromatin fraction, or both."
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"Mass spectrometry analysis revealed that USP13 could interact with Cohesin, and USP13 functioned as both ubiquitinase and deubiquitinase for Cohesin subunits."
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"USP13 and cohesin interact especially during DNA replication, and USP13 regulates the ubiquitination/deubiquitination of the interacting subunit of cohesion through its UBA1/2 domain ( xref )."
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"Interaction of endogenous USP13 with endogenous cohesin in cultured human cells."
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"To further confirm the interaction between USP13 and cohesin, endogenous cohesin was immunoprecipitated with SMC3 antibodies from whole cell lysates prepared from genetically unmodified HCT116 cells and Western blot performed with USP13 antibodies (and STAG2 antibodies as a positive control)."
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"Endogenous USP13 was also robustly coimmunoprecipitated by SMC3, confirming the interaction between USP13 and cohesin in genetically unmodified cells."
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"At this point we had demonstrated that endogenous USP13 bound to endogenous cohesin in the nucleus of human cells."
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"USP13 interacts with soluble cohesin complexes preferentially during DNA replication."
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"This experiment confirmed that USP13 interacts specifically with non–chromatin-bound cohesin complexes."
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"We next sought to determine whether the interaction between cohesin and USP13 was cell cycle dependent."
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"To test this, 293T cells were arrested at different points in the cell cycle and the interaction between cohesin and USP13 measured by performing USP13 Western blots on cohesin immunoprecipitates."
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"To test this, 293T cells were arrested at different points in the cell cycle and the interaction between cohesin and USP13 measured by performing USP13 Western blots on cohesin immunoprecipitates."
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"In this study we have focused on ubiquitination of the cohesin complex itself as a USP13-regulated target; however, it is likely that USP13-bound cohesin regulates the ubiquitination of other protein targets as well."
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"As shown in XREF_FIG D, the interaction between cohesin and USP13 was enhanced in cells arrested in the S phase when compared with asynchronous cycling cells, or cells arrested at other points in the cell cycle."
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"We wondered whether ubiquitinated cohesin subunits were present primarily in the soluble fraction (where the USP13 and cohesin complex resides), in the chromatin fraction, or both."
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"In this study we have focused on ubiquitination of the cohesin complex itself as a USP13 regulated target; however, it is likely that USP13 bound cohesin regulates the ubiquitination of other protein targets as well."
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"USP13 interacts with cohesin and regulates its ubiquitination in human cells."
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"In conclusion, here we demonstrate the existence of a robust, functionally and biochemically significant physical interaction between endogenous cohesin and endogenous USP13 in the soluble nuclear fraction of human cells."
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"To further confirm the interaction between USP13 and cohesin, endogenous cohesin was immunoprecipitated with SMC3 antibodies from whole cell lysates prepared from genetically unmodified HCT116cells and Western blot performed with USP13 antibodies (and STAG2 antibodies as a positive control)."
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"Endogenous USP13 was also robustly coimmunoprecipitated by SMC3, confirming the interaction between USP13 and cohesin in genetically unmodified cells."
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"At this point we had demonstrated that endogenous USP13 bound to endogenous cohesin in the nucleus of human cells."
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"We next sought to determine whether the interaction between cohesin and USP13 was cell cycle dependent."
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