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Statements

PIK3C3 binds USP13. 20 / 20
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"Likewise, we observed that neither the NEDD4H1284A,C1286A nor the NEDD4K1279R mutant reduces the K48-linked ubiquitination of PIK3C3, or interacts with PIK3C3 and USP13."
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"Since previous reports indicated that the knockdown of USP10 led to a reduction in the level of USP13 ( Liu et al., 2011 ), we further examined the interaction between USP13 and VPS34, as well as the [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We found that USP13 could still interact with VPS34 and stabilize VPS34 in USP10 KO cells, indicating that USP10 is not required for USP13 to interact and stabilize VPS34 ( Figures S4 B and S4C)."
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"Consistently, knockdown of NEDD4-1 resulted in impaired interaction between VPS34 and USP13 ( Figure S4 D)."
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"As expected, KO of NEDD4-1 completely abrogated the interaction between USP13 and VPS34 ( Figure 4 E)."
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"To confirm whether USP13 could directly bind to VPS34, we performed in vitro His-pull-down assays and found that purified NEDD4-1 could directly promote the association between USP13 and VPS34 ( Figur[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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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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"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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"We found that NEDD4-1 markedly enhanced the association between VPS34 and USP13, but not USP10 ( Figures 4 A and S4 A)."
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"Since previous reports indicated that the knockdown of USP10 led to a reduction in the level of USP13 ( Liu et al., 2011 ), we further examined the interaction between USP13 and VPS34, as well as the [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We found that USP13 could still interact with VPS34 and stabilize VPS34 in USP10 KO cells, indicating that USP10 is not required for USP13 to interact and stabilize VPS34 ( Figures S4 B and S4C)."
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"Consistently, knockdown of NEDD4-1 resulted in impaired interaction between VPS34 and USP13 ( Figure S4 D)."
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"Moreover, we found that the NEDD4-1 K1279R mutant failed to interact with VPS34 and USP13 ( Figure 6 G), indicating that K1279 of NEDD4-1 is essential for its binding ability with USP13 and VPS34."
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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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"As expected, KO of NEDD4-1 completely abrogated the interaction between USP13 and VPS34 ( Figure 4 E)."
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"To confirm whether USP13 could directly bind to VPS34, we performed in vitro His-pull-down assays and found that purified NEDD4-1 could directly promote the association between USP13 and VPS34 ( Figur[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Interestingly, we found that Vps34 complexes interact with USP13 and the stabilities of USP10 and USP13 are coordinately regulated with that of Vps34 complexes."
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"Likewise, an in vitro His-affinity-isolation assay showed that purified NEDD4 directly enhances the association between USP13 and PIK3C3."
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"In addition, we found that a catalytically inactive mutant of NEDD4 (H1284A,C1286A), displays reduced accumulation of GFPLC3B puncta and fails to interact with PIK3C3 and USP13, suggesting the E3 ubiquitin ligase activity of NEDD4 is required for the association with PIK3C3 and USP13, which promotes the formation of autophagosomes."
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"We discovered that NEDD4 enhances the association between USP13 and PIK3C3, and NEDD4 fails to inhibit K48 linked ubiquitination of PIK3C3 in USP13 deficient cells."
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