Recombinant Human PFD6 protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PFD6 also known as Prefoldin Subunit 6 is a component of the prefoldin complex. It has a molecular mass of approximately 15 kDa. PFD6 is expressed in various tissues including the heart liver and skeletal muscle. Mechanically PFD6 works as a molecular chaperone binding to newly synthesized polypeptides. It helps stabilize these nascent chains preventing premature folding and facilitating their transport to other complexes like the cytosolic chaperonin-containing TCP-1.

Biological function summary

PFD6 as part of the prefoldin complex assists in the correct folding of proteins necessary for cell function. The prefoldin complex acts as an assembly platform. It specifically interacts with cytoskeletal proteins such as actin and tubulin. This interaction is significant for maintaining cellular structure and dynamics. PFD6 therefore supports numerous cellular processes dependent on microtubule and actin filament formation.

Pathways

PFD6 participates in cellular maintenance processes. It plays a role in the protein folding and stabilization pathways working together with the cytosolic chaperonin CCT/TRiC complex. This interaction ensures that proteins involved in cell division and signaling like tubulins and actins are correctly folded. Additionally PFD6 connects to pathways involving cell motility and organization through stable support to the cytoskeleton.

PFD6 has links to certain neurodegenerative diseases and cancer. Aberrations in protein folding mechanisms can lead to accumulation of misfolded proteins contributing to neurodegenerative diseases like Alzheimer's. In cancer abnormal expression of PFD6 might affect cell structure and division due to its interactions with cytoskeletal elements like actin and tubulin. Research continues to explore how PFD6-related pathways influence these diseases highlighting potential therapeutic targets.