Genetic and cell biological analyses reveal a new role of Drp1 in postsynaptic endocytosis during brain development beyond mitochondrial division GTPase.
Tyrosine phosphorylation of the intracellular domain of LRP1 serves as a molecular switch to regulate cellular cholesterol homeostasis through nuclear hormone receptor-mediated regulation of the cellular cholesterol exporter ABCA1.
In oligodendrocyte progenitor cells, lipid metabolism and peroxisome biogenesis are regulated by the low-density lipoprotein related-receptor-1, and if disrupted, impair proper white matter development and adult repair.
Dhh1, Pat1, and Lsm1 target subsets of cellular mRNAs for decapping via interactions of these regulatory proteins with the C-terminal domain of Dcp2, the catalytic component of the decapping enzyme.
Intersectin counterparts in yeast recruit WASP and WIP to endocytic sites to establish a robust multivalent SH3 domain-PRM interaction network which gives actin assembly onset a switch-like behavior in vivo.
Mechanically stimulating mitochondria causes them to divide via the recruitment of the mitochondrial fission machinery to the mechanically strained site, showing that intracellular organelles can be mechanoresponsive.
Two GAP proteins bound to mitochondria regulate the enyzme Rab7, and thereby the expansion of the isolation membrane during mitophagy, downstream of PINK1 and Parkin, two proteins that are mutated in familial Parkinson's disease.
The dual role of Drosophila Mitofusin in steroid hormone production and cholesterol ester storage, which is evolutionary conserved by the combined expression of the two mammalian Mitofusins, ensures proper synaptic development.