Heike Arlt

TL;DR: It is proposed that proteolytic and chaperone-like activities in the YTA10-12 complex mediate assembly and degradation processes of membrane protein complexes and thereby exert key functions in the maintenance of membrane integrity.

TL;DR: These findings establish a central role of molecular chaperone proteins in the degradation of misfolded proteins by PIM1 protease and demonstrate a functional interrelation between components of the folding machinery and the proteolytic system within mitochondria.

TL;DR: An overlapping substrate specificity of the subunits of the m‐AAA protease is revealed and this results explain the impaired assembly of respiratory chain complexes by defects in expression of intron‐containing genes in mitochondria lacking m‐ AAA protease.

TL;DR: Evidence is provided that a binding site for the cellular transcription factor CREB can also act as a target for IE86 transactivation, showing that at least one specific member of the ATF/CREB family of transcription factors is involved in mediating transactivation by the HCMV IE86 protein.

TL;DR: This study discovered that loss of GLS function in triple-negative breast cancer (TNBC) cell lines with a deregulated glutaminolysis pathway led to profound tumor growth inhibition in vitro and in vivo and found that GLS inhibition synergizes with mTOR inhibition, which introduces the possibility of a novel therapeutic strategy for TNBC.