PFDN2 Human
Description
Product Specs
MGSSHHHHHH SSGLVPRGSH MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS.
Product Science Overview
The prefoldin complex is a heterohexameric structure composed of six subunits, including two alpha and four beta subunits. PFDN2 belongs to the beta subunit family . The complex has a unique jellyfish-like structure with tentacle-like extensions that capture unfolded protein substrates and transfer them to group II chaperonins for proper folding .
Prefoldin operates in an ATP-independent manner, which makes it particularly useful during cellular stress conditions where ATP levels might be compromised . This ATP-independent mechanism allows prefoldin to act as a holdase, stabilizing unfolded proteins and preventing their aggregation until they can be properly folded by chaperonins .
Prefoldin plays a crucial role in maintaining protein homeostasis, also known as proteostasis. It assists in the folding of approximately 10% of newly synthesized polypeptides downstream of the translation machinery . This includes cytoskeletal proteins such as actin and tubulin, which are essential for maintaining cell structure and function .
Recent studies have linked prefoldin to mitochondrial function. Specifically, PFDN2 has been shown to support mitochondrial morphology and the abundance of some respiratory chain complexes . It interacts with Tom70, a receptor for mitochondrial precursor proteins, suggesting a role in the quality control of proteins destined for the mitochondria .
Prefoldin and its subunits have been implicated in various diseases, particularly neurodegenerative disorders such as Alzheimer’s, Parkinson’s, and Huntington’s diseases . The complex’s ability to prevent protein aggregation is crucial in these conditions, where misfolded proteins form toxic aggregates that damage cells.
Additionally, abnormal expression of prefoldin subunits has been observed in different types of tumors. For instance, the c-Myc binding protein MM-1, a prefoldin subunit, can inhibit the activity of c-Myc, a protein involved in cell proliferation and tumor growth . This highlights the potential of prefoldin subunits as therapeutic targets in cancer treatment.
