IndraLab

Statements

OTUD5 binds VDAC2. 8 / 8
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"Because VDAC2 mainly interacts with OTUD5 via the N-terminal stretch, we hypothesized that OTUD5 likely modulates the ubiquitination of lysine residues (s) in the N-terminal stretch of VDAC2."
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"OTUD5 directly interacts with VDAC2 in an OTU domain-dependent manner and sustains VDAC2 stability by cleaving K48-linked polyubiquitin chains from VDAC2 K23 and K31."
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"Immunofluorescence staining assays using confocal microscopy were then performed in HEK-293T cells, and a distinct interaction between OTUD5 and VDAC2 was detected (Figure 10A)."
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"Moreover, the direct interaction between OTUD5 and VDAC2 was confirmed using glutathione S-transferase precipitation assays (Figure 10C)."
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"OTUD5 Interacts With VDAC2 and Cleaves the K48-linked Polyubiquitin Chains From VDAC2."
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"Immunofluorescence staining assays using confocal microscopy were then performed in HEK-293T cells, and a distinct interaction between OTUD5 and VDAC2 was detected ( xref A )."
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"Moreover, the direct interaction between OTUD5 and VDAC2 was confirmed using glutathione S-transferase precipitation assays ( xref C )."
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"Collectively, these data indicate that OTUD5 directly interacts with VDAC2 in an OTU domain-dependent manner."
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