IndraLab

Statements

DNM1L binds USP3. 7 / 7
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"These findings suggested that the USP3-DNM1L interaction mediated the function of GBC cells."
40197257
sparser
"Therefore, we speculated that G_DYNAMIN_2 might be an important domain for DNM1L to bind to USP3."
40197257
sparser
"Collectively, USP3 stabilizes DNM1L through deubiquitination, thereby remodeling mitochondrial dynamics and cellular metabolism, providing a theoretical basis and experimental foundation for precision therapies targeting the USP3–DNM1L axis in GBC ( xref )."
41301681
reach
"The immunoprecipitated samples was eluted using an elution buffer and subsequently analyzed via western blot assay.To verify the domains of DNM1L binds to USP3, various HA-tagged DNM1L deletion mutants (including HA-1–302 aa, HA-303–643 aa, and HA-644–736 aa) or HA-full constructs (HA-1–736 aa) and Flag-USP3 constructs were generated in the pcDNA3.1 vector."
40197257
reach
"USP3 physically interacted with and stabilized DNM1L."
40197257
sparser
"These findings suggest that the USP3–DNM1L axis drives the malignant phenotype of gallbladder cancer via the “mitochondrial dynamics-metabolic reprogramming-tumor progression” pathway, providing a theoretical basis for therapeutic strategies targeting mitochondrial metabolism."
41301681
sparser
"USP3 binds the GTPase domain (1–302 aa) of DNM1L and selectively cleaves K48-linked ubiquitin chains, prolonging DNM1L half-life and promoting its induction of excessive mitochondrial fission, ATP depletion, reactive oxygen species (ROS) accumulation, and mitochondrial DNA (mtDNA) loss."
41301681