IndraLab

Statements

USP8 is phosphorylated on tyrosine. 15 / 15
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rlimsp
"Here, we demonstrate, in the context of a chimeric EGFR-ErbB2 receptor, that (i) EGF induces pY1091 Cbl binding site-dependent K63-polyubiquitination of EGFR-ErbB2, (ii) Cbl is tyrosine phosphorylated upon stimulation of EGFR-ErbB2 wt and Y1091F mutant receptor, (iii) EGF-induced activation of EGFR-ErbB2 induces Usp8 tyrosine phosphorylation, and (iv) ubiquitination of the EGFR-ErbB2 wt and Y1091F mutant is enhanced upon coexpression of catalytically inactive Usp8-C748A in the presence and absence of EGF."
21044682
rlimsp
"We also show that enhanced endosomal recycling of the EGFR induced by TGFα stimulation is associated with decreased Usp8 tyrosine phosphorylation."
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rlimsp
"In the present study we show that overexpression of constitutively active SRC enhances constitutive and ligand-induced Usp8 tyrosine phosphorylation."
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rlimsp
"However, mutation of three MIT domain tyrosine residues did not abolish Usp8 tyrosine phosphorylation."
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rlimsp
"Our findings are most consistent with the model that MIT domain-dependent recruitment of Usp8 to endosomal membranes is important for low stoichiometry SRC-mediated tyrosine phosphorylation of multiple Usp8 tyrosines."
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sparser
"However, since the tyrosine phosphorylation in the 1–504 construct was decreased compared to Usp8 WT, it is likely that more than a single tyrosine residue of Usp8 is phosphorylated."
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sparser
"To identify the Usp8 tyrosine residues that are phosphorylated upon EGF-stimulation of EGFR, we first addressed the question which part of Usp8 is essential for binding to the EGFR and for subsequent [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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rlimsp
"We previously demonstrated that Usp8 is tyrosine phosphorylated in an EGFR- and SRC-kinase dependent manner."
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sparser
"In contrast, TCHP is deubiquitinated by USP8 after EGFR-mediated phosphorylation of USP8 at tyrosine residues 717 and 810 [ xref ]."
| PMC
sparser
"Using Usp8 deletion constructs, our results demonstrate that Usp8 is efficiently tyrosine phosphorylated on at least one tyrosine residue in the N-terminal 504 amino acids of Usp8, as detected by immu[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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rlimsp
"We further show that Usp8 tyrosine phosphorylation upon stimulation of EGFR-ErbB2 is (a) independent of Y1091, (b) dependent on Src- and EGFR-ErbB2-kinase activity, (c) enhanced upon coexpression of Usp8-C748A, and (d) partly dependent on the Microtubule Interacting and Transport (MIT) domain of Usp8."
21044682
rlimsp
"We therefore hypothesize that tyrosine phosphorylation of Usp8 could regulate the function of Usp8."
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sparser
"Phosphorylation of USP8 at additional Ser and Tyr residues has been reported to regulate its function although the exact outcomes are not yet defined [ xref ]."
32512887
sparser
"Nevertheless, our results support the model that the Usp8 MIT domain is important for endosomal recruitment and allows low stoichiometry SRC family kinase-mediated Usp8 tyrosine phosphorylation of mul[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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sparser
"To address the question of the functional significance of Usp8 tyrosine phosphorylation, it is crucial to elucidate the regulation of Usp8 tyrosine phosphorylation and to identify the Usp8 tyrosine re[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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