IndraLab

Statements

USP8 translocates to the membrane. 13 / 13
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"Nevertheless, our findings demonstrate that optimal Usp8 tyrosine phosphorylation requires an intact Usp8 MIT domain, which is consistent with the proposed role of the MIT domain in recruitment of Usp[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"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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"The MIT domain in Usp8 was first identified by Row and coworkers, who showed that the MIT domain interacts with Escrt-III CHMP proteins and is necessary for the recruitment of Usp8 to endosomal membra[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"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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"These findings are consistent with the model that Usp8 is tyrosine phosphorylated upon MIT-dependent recruitment of Usp8 to endosomal membranes [17,21] ."
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"These findings are consistent with the model that Usp8 is tyrosine phosphorylated upon MIT dependent recruitment of Usp8 to endosomal membranes [17,21]."
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"Interestingly, removal of the MIT domain does not completely abolish Usp8 tyrosine phosphorylation, suggesting that Usp8 might be recruited to endosomal membranes also via alternative mechanisms (e.g.[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"5 and 6 ), suggesting that Usp8 might also be recruited to endosomal membranes through alternative mechanisms."
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"Nevertheless, our findings demonstrate that optimal Usp8 tyrosine phosphorylation requires an intact Usp8 MIT domain, which is consistent with the proposed role of the MIT domain in recruitment of Usp[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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sparser
"Interestingly, removal of the MIT domain does not completely abolish Usp8 tyrosine phosphorylation, suggesting that Usp8 might be recruited to endosomal membranes also via alternative mechanisms (e.g.[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Even though the MIT domain is essential for tyrosine phosphorylation of the truncated Usp8 construct 1-504, removal of the MIT domain does not completely abolish tyrosine phosphorylation of Usp8 WT (F[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Taken together, our results do not support the model that Usp8 is tyrosine phosphorylated within the MIT domain but rather support the hypothesis that the MIT domain is required to recruit Usp8 to the[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Our finding that the MIT domain of Usp8 is essential for optimal Usp8 tyrosine phosphorylation ( Fig. 6 ) is consistent with the model that Usp8 is tyrosine phosphorylated upon MIT-dependent recruitme[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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