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USP13 binds NEDD4. 29 / 29
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"NEDD4 undergoes K29-linked auto-ubiquitination at K1279 and serves as a scaffold for recruiting USP13 to form a NEDD4-USP13 deubiquitination complex, which subsequently cleaves the K48-linked poly-ubiquitin chains from PIK3C3 at K419, thus stabilizing PIK3C3 to promote autophagy. the ubiquitination of USP13; however, NEDD4 appears to be its own substrate for ubiquitination, and the catalytic activity of NEDD4 is required for its auto-ubiquitination."
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"Since knockdown of VPS34 did not affect the association between NEDD4-1 and USP13 ( Figure 4 D), we hypothesized that NEDD4-1 may first bind to USP13 to form an NEDD4-1-USP13 complex."
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"In addition, KO of BECN1 could not affect the interaction of NEDD4-1 with USP13 or VPS34, indicating that the NEDD4-1-USP13 complex binds to VPS34 in a Beclin-1-independent manner ( Figure S4 E)."
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"Immunoblot analysis showed that NEDD4-1 interacted with USP13 at 1 h post-EBSS incubation, while the apparent interaction between NEDD4-1-USP13 and VPS34 could be detected at a later time point (at 2 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"These results suggest that the formation of NEDD4-1-USP13 complex is an essential prerequisite for VPS34 deubiquitination."
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"We observed that NEDD4 interacts with USP13 upon autophagy induction, whereas NEDD4USP13 interacts with PIK3C3 at a later time point, indicating that NEDD4 might recruit USP13 to form a NEDD4 and USP13 complex."
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"Vps34, a unique member of the class III phosphoinositide 3-kinase, is an autophagy-associated protein that controls autophagosome generation, and its ubiquitination is downregulated by the NEDD4-USP13 complex."
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"NEDD4-1 recruits USP13 to form a NEDD4-USP13 complex, thereby increasing the interaction between USP13 and Vps34 and inhibiting K48-linked ubiquitination of Vps34 on K419."
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"USP13 could not affect the ubiquitination and protein stability of the VPS34 K419R mutant ( Figure 4 K), further confirming that the NEDD4-1-USP13 complex mainly cleaves K48-linked poly-ubiquitin chai[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Subsequently, the NEDD4-USP13 axis cleaves the K48-linked poly-ubiquitin chains on PIK3C3 at K419 and promotes autophagy through suppressing the proteasomal degradation of PIK3C3."
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"NEDD4 undergoes K29-linked auto-ubiquitination at K1279, which in turn serves as a scaffold for recruiting the deubiquitinating enzyme USP13 to form a NEDD4-USP13 deubiquitination complex."
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"Our findings provide insight into the mechanisms underpinning VPS34 deubiquitination mediated by the NEDD4-1-USP13 axis, thus promoting the stabilization of VPS34 and contributing to autophagosome for[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We observed that NEDD4 interacts with USP13 upon autophagy induction, whereas NEDD4USP13 interacts with PIK3C3 at a later time point, indicating that NEDD4 might recruit USP13 to form a NEDD4-USP13 complex (Figure 1)."
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"Similarly, auto-ubiquitination of NEDD4-1 enables it to act as a scaffolding protein to recruit USP13 to form the NEDD4-1-USP13 deubiquitination complex."
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"These results suggest that USP13 is indispensable for the NEDD4-1-regulated removal of K48-linked poly-ubiquitin chains on VPS34.Since knockdown of VPS34 did not affect the association between NEDD4-1[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In addition, KO of BECN1 could not affect the interaction of NEDD4-1 with USP13 or VPS34, indicating that the NEDD4-1-USP13 complex binds to VPS34 in a Beclin-1-independent manner ( Figure S4 E)."
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"These results suggest that the auto-ubiquitination of NEDD4-1 at K1279 is indispensable for NEDD4-USP13 complex formation, thus mediating the deubiquitination and stabilization of VPS34."
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"Interestingly, although knockdown of PIK3C3 does not affect the association between NEDD4 and USP13, the association between USP13 and PIK3C3 is completely abrogated in NEDD4 deficient cells."
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"These results suggest that the formation of NEDD4-1-USP13 complex is an essential prerequisite for VPS34 deubiquitination.To determine whether USP13 stabilizes VPS34 in a catalytic activity-dependent [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Furthermore, we have discovered that NEDD4-1 undergoes K29-linked auto-polyubiquitination at K1279 and functions as a platform to recruit USP13 to form an NEDD4-1-USP13 deubiquitination complex."
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"The formation of the NEDD4-1-USP13 complex plays a critical role in cleaving the K48-linked ubiquitin chains of VPS34 and then stabilizing VPS34, thus promoting the formation of autophagosomes."
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"These results suggest that the auto-ubiquitination of NEDD4-1 at K1279 is indispensable for NEDD4-USP13 complex formation, thus mediating the deubiquitination and stabilization of VPS34.Ubiquitination[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Our results suggested that K48-linked ubiquitination is a signal for VPS34 degradation and that NEDD4-1-USP13 complex reverses this process."
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"The formation of the NEDD4-1-USP13 complex plays a critical role in cleaving the K48-linked ubiquitin chains of VPS34 and then stabilizing VPS34, thus promoting the formation of autophagosomes."
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"NEDD4-1-USP13 axis promoted autophagy flux at the basal level, and the enhancement was largely increased at the early time of autophagy-induced conditions (0.5–4 h)."
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"Our results suggested that K48-linked ubiquitination is a signal for VPS34 degradation and that NEDD4-1-USP13 complex reverses this process.Previous studies indicated that several ubiquitin ligases an[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The NEDD4-1-USP13 axis suppresses the proteasomal degradation of VPS34 and promotes autophagic flux."
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"Vps34, a unique member of the class III phosphoinositide 3-kinase, is an autophagy-associated protein that controls autophagosome generation, and its ubiquitination is downregulated by the NEDD4-USP13 complex."
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"NEDD4-1 recruits USP13 to form a NEDD4-USP13 complex, thereby increasing the interaction between USP13 and Vps34 and inhibiting K48-linked ubiquitination of Vps34 on K419."
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