IndraLab

Statements


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"The interaction between ubiquitin-specific peptidase 19 (USP19) and FUNDC1 was analyzed using co-immunoprecipitation."

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"Plasmids HA-USP19 and Flag-FUNDC1 were co-transfected into BEAS-2B cells to elucidate the interaction between USP19 and FUNDC1."

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"A previous study demonstrated that USP19 interacts with FUNDC1 and stabilizes FUNDC1 [17]."

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"In the present study, FUNDC1 protein levels were decreased by USP19 knockdown, indicating that USP19 may be involved in mitophagy by regulating FUNDC1 expression in CSE-treated BEAS-2B cells.The interaction between USP19 and FUNDC1 was confirmed using the co-IP assays."

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sparser
"USP19 may interact with FUNDC1, which regulates mitophagy in COPD."

sparser
"A previous study demonstrated that USP19 interacts with FUNDC1 and stabilizes FUNDC1 [ xref ]."

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"These results indicated that FUNDC1 interacts with USP19."

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"Collectively, these results showed that USP19 interacts with FUNDC1 and stabilizes FUNDC1 in BEAS-2B cells."

sparser
"The interaction between USP19 and FUNDC1 was confirmed using the co-IP assays."

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"In response to hypoxia, USP19 binds to and deubiquitinates FUNDC1 at ER-mitochondria contact sites, which facilitates Drp1 oligomerization and Drp1 GTP binding and hydrolysis activities, thereby promoting mitochondrial division."

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sparser
"Because previous studies have demonstrated that FUNDC1 translocates to the MAM in response to hypoxic stress and regulates mitochondrial dynamics similarly to USP19, they examined the interaction of USP19 with FUNDC1."

sparser
"In addition, USP19 (an ER-resident deubiquitinase) can bind FUNDC1 and deubiquitinate it at the MAMs leading to DRP1 oligomerization and promotion of mitochondrial division ( xref )."

sparser
"Interestingly, the authors found a direct interaction between USP19 and FUNDC1, and the interaction is dependent on the formation of the MAM structure, as their interactions were reduced in MFN2 KO cells."

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"Simultaneously, the deubiquitinating enzyme ubiquitin specific peptidase 19 (USP19), which is located in the endoplasmic reticulum, accumulates at the MAM and binds to the mitochondrial outer membrane protein FUNDC1, inducing its deubiquitination, promoting the oligomerization of dynamin-related protein 1 (DRP1), and resulting in mitochondrial fission (Zhang et al., 2022)."

sparser
"Furthermore, using immunoprecipitation coupled with pull-down assays, the investigation has confirmed that USP19 directly binds to FUNDC1, and that the interaction is strongly enhanced under hypoxic conditions ( xref ) ( xref )."

sparser
"The interaction between USP19 and its substrate FUNDC1 is also verified by co-immunoprecipitation assays and glutathione S- transferase (GST) affinity isolation assays ( xref )."

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"As hypoxia progresses, FUNDC1 may preferably bind to USP19, which deubiquitinates and stabilizes FUNDC1 at MERCSs, as a result, mitochondrial fission is initiated, and mitophagy is promoted to eliminate damage mitochondria ( xref ) ( xref )."