Unconventional secretion mediated by direct protein self-translocation across the plasma membranes of mammalian cells

In recent years, a surprisingly complex picture emerged about endoplasmic reticulum (ER)/Golgi-independent secretory pathways, and several routes have been discovered that differ with regard to their molecular mechanisms and machineries. Fibroblast growth factor 2 (FGF2) is secreted by a pathway of unconventional protein secretion (UPS) that is based on direct self-translocation across the plasma membrane. Building on previous research, a component of this process has been identified to be glypican-1 (GPC1), a GPI-anchored heparan sulfate proteoglycan located on cell surfaces. These findings not only shed light on the molecular mechanism underlying this process but also reveal an intimate relationship between FGF2 and GPC1 that might be of critical relevance for the prominent roles they both have in tumor progression and metastasis.

Automated summary

In recent years, research has revealed a complex picture of endoplasmic reticulum (ER)/Golgi-independent secretory pathways, including the discovery of several routes with different molecular mechanisms and machineries. Fibroblast growth factor 2 (FGF2) has been found to be secreted through an unconventional protein secretion (UPS) pathway that involves direct translocation across the plasma membrane. This process has been shown to involve glypican-1 (GPC1), a GPI-anchored heparan sulfate proteoglycan located on cell surfaces. These findings not only provide insight into the molecular mechanism of this process but also highlight the important relationship between FGF2 and GPC1 in tumor progression and metastasis.