IndraLab

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USP12 translocates from the nucleus to the cytoplasm. 6 / 6
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sparser
"After stimulating the TCR with an anti-CD3 antibody, phosphorylation of the USP12 cytoplasmic pool could be induced, allowing USP12 to translocate from the nucleus to the cytoplasm and acted directly on the substrate proteins LAT and Trat1 to stabilize the TCR complex on the T cell surface during signaling."

sparser
"However, in TCR signaling, the translocation manner was quite different that USP12 translocated from the nucleus to the cytoplasm to deubiquitinate LAT and Trat1 proteins [ 20 ]."

sparser
"A recent report showed that in TCR signaling, USP12 translocates from the nucleus to the cytoplasm, where USP12 deubiquitinates and stabilizes LAT and Trat1 and prevents their lysosome-dependent degradation in T cells."

sparser
"It has been reported that in TCR signaling, USP12 translocates from the nucleus to the cytoplasm to deubiquitinate LAT and Trat1 proteins [ xref ]."

sparser
"Together with the recent finding that USP12 can be exported from the nucleus to the cytoplasm by CRM1 ( Jahan et al., 2016 ), our results raised the possibility that the USP12/WDR20 complex may underg[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"However, in the TCR-related studies, anti-CD3 stimulation of the TCR translocated USP12 from the nucleus to the cytoplasm to act on the substrate proteins LAT and Trat1 to stabilize the TCR."