IndraLab

Statements


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sparser
"To elucidate if USP22 was directly binding PALB2 WD40 we performed in-vitro pulldown experiments using MBP-PALB2 WD40 as the bait along with His-USP22 ( xref )."

sparser
"To evaluate USP22-PALB2 binding in cells an IP was performed with FLAG-PALB2 in H1299 lung adenocarcinoma cells in which endogenous USP22 was successfully pulled down ( xref )."

sparser
"USP22 directly interacts with PALB2 to promote DNA homologous recombination repair and inhibit the killing effect of cisplatin on cancer cells."

sparser
"USP22 DUB Domain Interacts with PALB2 WD40 Domain."

sparser
"Our in-silico analysis showed an interaction between the C-terminal DUB domain of USP22 and the C-terminal WD40 domain of PALB2 that has been previously crystallized ( xref , PDB: 2W18) xref ."

sparser
"PALB2 WD40 Domain Directly Binds USP22 and stimulates its Catalytic Activity."

sparser
"Using our in-silico model of PALB2-USP22 binding ( xref ) we predicted several residues on the PALB2 WD40 domain that looked critical for this interaction; S951, N953 (upper panel), R942 (middle panel), and H913 (lower panel)."

sparser
"We identified a direct interaction between the C-terminal WD40 domain of PALB2 and the DUB domain of USP22 and that this interaction was necessary and sufficient to activate USP22 catalytic DUB activity in-vitro ."

reach
"To assay for this we used the U2OS cell line and overexpressed either FLAG-H2B or FLAG-H2B and analyzed recruitment of GFP-USP22, Rad51, PALB2, and BRCA2 after induction of mCherry-LacI-FOKI (Figure 2d,e)."

sparser
"Understanding the interaction of USP22-PALB2 and indeed the interaction of other DUBs with WD40 domain containing proteins could present a new way to target DUBs for cancer therapies."

sparser
"Furthermore, the lysine residues on PALB2 that USP22 could be potentially deubiquitinating have not been mapped by this study or others and is an excellent future direction for further study on the USP22-PALB2 interaction."

sparser
"USP22 directly interacts with PALB2 through the latter's C-terminal WD40 domain to promote DNA homologous recombination repair [ 78 ]."

reach
"Given that USP22 KD causes moderate increase in global H2Bk120ub and the data show both USP22 and H2BK120ub are clearly important for recruitment of USP22, Rad51, PALB2, and BRCA2 to sites of DSBs, this suggests the modulation and fine tuning of H2Bk120ub is important."

reach
"Although this shows USP22 can bind both PALB2 and SAGA it does not delineate whether these are two separate populations or whether USP22 can interact with all of these components including PALB2 at the same time."

reach
"PALB2 WD40 Domain Directly Binds USP22 and stimulates its Catalytic Activity."

reach
"Consistent with our LacO array recruitment experiment, (Figure 4b) mCherry-PALB2 could not pull-down FLAG-USP22 while mCherry-PALB2 robustly bound FLAG-USP22 ."

reach
"To elucidate if USP22 was directly binding PALB2 we performed in-vitro pulldown experiments using MBP-PALB2 as the bait along with His-USP22 (Figure 4d)."

reach
"Upon addition of MBP-PALB2 , USP22 enzymatic activity was robustly activated (Figure 4e) showing that PALB2 directly binds USP22 and stimulates its catalytic activity."

sparser
"USP22 directly interacts with PALB2 via the C-terminal WD40 domain to promote DNA homologous recombination repair ( xref )."