Results 241 to 250 of about 55,033 (326)

CD9‐association with PIP2 areas is regulated by a CD9 salt bridge

open access: yesFEBS Open Bio, EarlyView.
The tetraspanin CD9 has an intracellular salt bridge. If CD9 opens, open‐CD9 moves from PIP2‐rich areas to regions populated by its interaction partner EWI‐2. Hence, the state of the salt bridge regulates the distribution of CD9 and by this CD9‐EWI‐2 complex formation.
Yahya Homsi   +2 more
wiley   +1 more source

Characterization of WAC interactions with R2TP and TTT chaperone complexes linking glucose and glutamine availability to mTORC1 activity

open access: yesFEBS Open Bio, EarlyView.
TTT and R2TP chaperone complexes are required for the assembly and activation of mTORC1. WAC directly interacts with components of TTT, R2TP, and mTORC1, and these interactions are affected by the availability of glucose and glutamine, correlating with changes in mTORC1 activity.
Sofía Cabezudo   +11 more
wiley   +1 more source

Two‐way inhibition of PAX5 transcriptional activity by PAX5::CBFA2T3

open access: yesFEBS Open Bio, EarlyView.
PAX5::CBFA2T3 (PAX5‐C) is a fusion protein of the B‐cell transcription factor, PAX5, and is found in B‐cell ALL. We propose a putative model of two‐way inhibition of PAX5 transcriptional activity by PAX5‐C. There are two ways of repression by PAX5‐C: DNA‐binding‐dependent way and HDAC‐dependent way, with either being sufficient for the repression. HDAC
Reina Ueno   +12 more
wiley   +1 more source

The cochaperone BAG3 promotes the stabilization of p53 under heat stress conditions

open access: yesFEBS Open Bio, EarlyView.
Under heat stress, BAG3 translocates to the nucleus and forms a complex with Hsp70 and p53, thereby promoting p53 stabilization and enhancing its transcriptional activity. These findings suggest that BAG3 functions as a cochaperone that supports p53‐mediated stress responses in cooperation with Hsp70.
Ngoc Nguyen Thi Minh   +2 more
wiley   +1 more source

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