Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
We show that the mitochondrial fission proteins MiD49 and MiD51 are activated by fatty acyl-coenzyme A (FA-CoA). FA-CoA binds in a previously identified pocket located within MiDs, inducing their oligomerization and ability to activate the dynamin DRP1, ultimately promoting mitochondrial fission. Activated MiDs synergize with mitochondrial fission factor (MFF) in stimulating DRP1 activity, leading us to hypothesize that MiDs act upstream of MFF during mitochondrial fission.
Contractile activity of both the epithelium and underlying mesenchyme are required for epithelial deformation and cell fate acquisition during early mouse hair follicle development. Subsequently, localized basement membrane remodelling facilitates the release of tension-generated pressure to promote cell divisions, tissue fluidification and downgrowth of the developing hair follicle.
The chemoresistant and immunoevasive characteristics of leukaemia stem cells (LSCs) impede the treatment efficacy for acute myeloid leukaemia (AML). We find that inhibiting the tyrosine phosphatase SHP-1 effectively alters the metabolic state of LSCs, making them more susceptible to chemotherapy and immune surveillance in AML.
The generation of clathrin-coated vesicles during endocytosis requires the co-ordinated recruitment of dozens of proteins to the plasma membrane. We discovered that the plant TPLATE (or TSET) complex (TPC) undergoes biomolecular condensation through interactions with plasma membrane phospholipids and, via weak multivalent interactions, recruits clathrin and other endocytic proteins to facilitate the efficient progression of endocytosis.