IndraLab

Statements


| 2 18

sparser
"OTUB1 binds to ubiquitin-charged E2 enzymes and positions the donor ubiquitin at its proximal site, thereby providing partial protection to the vulnerable thioester linkage through a helix situated in its N-terminal region."

sparser
"Thus, we sought to know whether SET7-mediated methylation of OTUB1 can affect OTUB1 binding to the E2 enzyme, UBC13."

sparser
"Remarkably, the binding of uncharged E2 enzymes to OTUB1 stimulates its DUB activity ( xref ) showing that catalytic and non-catalytic functions can be intertwined."

sparser
"In addition, binding of E2 enzymes to OTUB1 can also promote OTUB1 deubiquitinase activity dependent on the ratio of ubiquitin (Ub)–charged E2 (E2-Ub) to uncharged E2 enzyme and levels of free Ub ( xref )."

sparser
"Mass spectrometry-proteomic studies have revealed that OTUB1 interacts with six other E2 enzymes in cells: UBE2D1 (UbcH5a), UBE2D2 (UbcH5b), UBE2D3 (UbcH5c), UBE2E1 (UbcH6), UBE2E2 (UbcH8), and UBE2E3 (UbcH9 or UbcM2) xref , xref ."

sparser
"An in vitro study showed that binding of an uncharged E2 enzyme to OTUB1 can stimulate cleavage of polyubiquitin by stabilizing N-terminal ubiquitin-binding helix to fold which then comprises the proximal ubiquitin-binding site xref ."

sparser
"OTUB1 D88 binds E2 enzymes and suppresses Ub-conjugating activity ( xref )."

sparser
"In order to verify that the OTUB1 C91S mutation did not affect binding to E2 enzymes, we measured binding of a subset of E2s (UBE2D1 and UBE2D3) to wild-type OTUB1 and found no significant difference in K d values ( xref )."

sparser
"OTUB1 stabilizes E2s UBE2E1 by inhibiting its auto-ubiquitination independent of the deubiquitinase activity, and the activity of OTUB1 in removing the K48 poly-ubiquitin chain can further be stimulated by OTUB1-E2s complex in turn xref ."

sparser
"For example, OTUB1 stabilizes E2s UBE2E1 by restraining its autoubiquitination independence of the deubiquitinase activity, and OTUB1 cleavage of k48 polyubiquitin function can further be stimulated b[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Mass spectrometry studies have revealed that OTUB1 can form complexes with several other E2s in cells, including UBE2E1 (UBCH6), UBE2E2 (UBCH8), and UBE2E3 (UBCH9), in addition to UBE2N (UBC13) and the UBCH5 (UBE2D1, -2, and -3) isoforms ( xref , xref )."

sparser
"We have demonstrated that OTUB1 binds to phospho-SMAD2/3 and E2 ubiquitin-conjugating enzymes, thereby inhibiting the polyubiquitylation of SMAD2/3 in vitro."

sparser
"The nonstandard manner of inhibiting ubiquitination involves the direct interaction of OTUB1 with E2 ubiquitin-conjugating enzymes to remove ubiquitin."

reach
"Herhaus et al. [25] have demonstrated that OTUB1 binded to phospho-Smad2/3 (p-Smad2/3) and E2 ubiquitin-conjugating enzymes, thereby enhancing the TGFβ-induced transcriptional responses by stabilizati[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"These observations reveal a novel role for OTUB1 binding to E2 ubiquitin-conjugating enzymes in regulating E2 stability within the cell."

sparser
"To reveal the underlying mechanism, the authors performed mass spectrometry analysis for OTUB1 immunoprecipitate and found Ubc13 (UBE2N), UBE2D and UBE2E E2s interact with OTUB1."

sparser
"Likewise, binding of uncharged E2s to OTUB1 stimulates OTUB1 cleavage of K48-linked substrates [ xref ]."

sparser
"Further characterization of this mechanism demonstrated that OTUB1 directly binds and consequently inhibits a related subclass of E2 enzymes that include UBC13, the only known E2 that cooperates with RNF168 during the DNA damage response xref , xref ."

sparser
"Substitution of the active site cysteine with serine (C91S) inactivates OTUB1 ( xref ), whereas a T134R substitution abrogates OTUB1 binding to E2 ubiquitin-conjugating enzymes ( xref , xref ), thereby disrupting the ability of OTUB1 to prevent ubiquitin transfer."

reach
"OTUB1 binds to UBC13 (UBE2N), an E2 ubiquitin-conjugating enzyme for RNF168, and restricts its interaction with RNF168, suppressing the DSB responses by inhibiting RNF168-induced polyubiquitylation independently of its catalytic activity [64]."