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Heat shock factors (HSFs) are essential for survival in a stressful environment. HSFs mediate the heat shock response by binding heat shock elements present in heat shock protein (HSP) genes, thereby mediating their transcription. They are also important regulators of development, lifespan and disease.
The endosomal sorting complex required for transport (ESCRT) machinery catalyses membrane budding in the endolysosomal pathway, which differs from other budding events in that it is directed away from the cytosol. Recent studies have elucidated a mechanism whereby ESCRT-I and ESCRT-II stabilize the bud neck and ESCRT-III mediates neck cleavage.
Despite decades of research, the extent to which human progerias resemble accelerated ageing is still unclear and highly debated. Understanding this connection will require the ongoing characterization of genetic pathways that influence the ageing process in model systems and investigations into molecular pathways that define the pathogenesis of human progerias.
Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in modulating polypeptide folding, degradation and translocation across membranes, and protein–protein interactions. This functional diversity is driven by their interaction with J proteins — a diverse class of cofactors.
The molecular composition of the cellular lipidome is complex and still poorly understood. The exact mechanisms of how compositional complexity affects cell homeostasis and its regulation are also unclear. The emerging field of lipidomics is developing sensitive mass spectrometry technologies for the quantitative characterization of the lipidome.
