Two newly identified assembly factors for the ribosome-associated iron-sulfur protein Rli1 reveal a general mechanism for how the cytosolic iron-sulfur protein assembly (CIA) machinery recruits apoproteins.

Mammalian cellular iron homeostasis and the maturation of the cytosolic iron sulfur cluster proteins are dependent on the mitochondrial protein import machinery.

A new role is identified for GLI1 in modulating the inflammatory response of macrophages and the overaction of osteoclasts in collagen-induced arthritis by collaboratively regulating DNMT1 and DNMT3a.

Cell biological, biochemical and structural studies reveal the mechanistic roles of two new mitochondrial iron-sulfur protein assembly factors, explaining the patho-biochemical defects of affected patients.

PTPN22 function is regulated by reactive oxygen species, and redox regulation of PTPN22 impacts T-cell-dependent autoimmune inflammation.

Iron content in neural stem cells controlled by glial ferritin is critical for self-renewal and proliferation of neural stem cells.