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USP37 binds CDH1. 21 / 21
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"USP37 binds to APC/C adaptor protein CDH1 in G1/S and removes degradative polyUb from the APC substrate cyclin A. USP37-mediated deubiquitination and stabilization of cyclin A enable entry into the S phase."
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"USP37 binds to APC/C adaptor protein CDH1 in G1/S and removes degradative polyUb from the APC CDH1 substrate cyclin A. USP37-mediated deubiquitination and stabilization of cyclin A enable entry into the S phase."
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"In G1/S, Activated USP37 binds to Cdh1 and deubiquitinates cyclin A, which Promote S Phase Entry [XREF_BIBR]."
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"Here we show that USP37 binds the APC/C coactivator CDH1, but not CDC20."
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"They identified interactions between USP37 and CDH1, as well as APC/C subunits, implicating USP37 in the regulation of the G1/S transition and characterized the cell cycle regulation of USP37 (Figure 4C)."
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"Knockdown of CDH1 markedly reduced the interaction between USP37 and CDC27 ( Figure 1 F), suggesting that core APC/C components bind USP37 indirectly through CDH1."
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"A direct interaction between USP37 and CDH1 is likely because mixing of USP37 and CDH1 translated individually in rabbit reticulocyte lysates reproduced the interaction observed in cells ( Figure 1 G)[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"They identified interactions between USP37 and CDH1, as well as APC/C subunits, implicating USP37 in the regulation of the G1/S transition and characterized the cell cycle regulation of USP37 ( xref )."
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"Consistent with this degron being targeted by APC CDH1 , the KEN box-3 mutant USP37 interacted poorly with CDH1 ( Figure 5 F) and had a much longer half-life ( Figure 5 G)."
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"HBx acts as a chaperone of USP37 and shuttles it out of the nucleus, where the ubiquitin E3 ligase CDC20 homolog 1 (CDH1) and b-TrCP associate with USP37 (Zhou et al., 2003; von Mikecz, 2006; Saxena and Kumar, 2014)."
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"In human cells, the USP37 deubiquitinating enzyme forms a complex with human Cdh1 and selectively attenuates cyclin A ubiquitination, which allows CDK-cyclin A to initiate the transition into S phase."
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"In human cells, the USP37 deubiquitinating enzyme forms a complex with human Cdh1 and selectively attenuates cyclin A ubiquitination, which allows CDK-cyclin A to initiate the transition into S phase ( xref )."
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"Ubiquitin specific protease (USP) 44 has been described in checkpoint responsive regulation of the APC/C by stabilizing the APC-inhibitory MAD2 and CDC20 complex (Joo et al., 2007; Stegmeier et al., 2[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"A direct interaction between USP37 and CDH1 is likely because mixing of USP37 and CDH1 translated individually in rabbit reticulocyte lysates reproduced the interaction observed in cells."
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"Huang et al. characterized the USP37 interaction with CDH1 and CDC20 by tandem mass spectrometry and found that USP37 interacts with CDH1 but not CDC20."
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"Early work showed that USP37 binds the APC/C CDH1 E3 complex to regulate ubiquitylation of cyclin A, a substrate of APC/C CDH1 [ 28 ]."
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"Usp37 binds APC/C Cdh1 in G1 and deubiquitinates the APC/C substrate cyclin A [ xref ]."
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"Huang et al. characterized the USP37 interaction with CDH1 and CDC20 by tandem mass spectrometry and found that USP37 interacts with CDH1 but not CDC20."
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"USP37 binds to CDH1 and removes degradative polyubiquitin chains, leading to the early accumulation of cyclin A in the G1 phase and accelerated entry into the S phase ( xref )."
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"In G1/S, Activated USP37 binds to Cdh1 and deubiquitinates cyclin A, which Promote S Phase Entry [ xref ]."
27418942
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"USP37 binds to the substrate adaptor CDH1 and removes the polyubiquitin chain, which is the degradation signal, from cyclin A ( xref )."
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