Prefoldin, a jellyfish-like molecular chaperone: functional cooperation with a group II chaperonin and beyond
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Prefoldin is a hexameric molecular chaperone found in the cytosol of archaea and eukaryotes. Its hexameric complex is built from two related classes of subunits and has the appearance of a jellyfish: its body consists of a double beta-barrel assembly with six long tentacle-like coiled coils protruding from it. Using the tentacles, prefoldin captures an unfolded protein substrate and transfers it to a group II chaperonin. The prefoldin-group II chaperonin system is thought to be important for the folding of newly synthesized proteins and for their maintenance, or proteostasis, in the cytosol. Based on structural information of archaeal prefoldins, the mechanisms of substrate recognition and prefoldin-chaperonin cooperation have been investigated. In contrast, the role and mechanism of eukaryotic PFDs remain unknown. Recent studies have shown that prefoldin plays an important role in proteostasis and is involved in various diseases. In this paper, we review a series of studies on the molecular mechanisms of archaeal prefoldins and introduce recent findings about eukaryotic prefoldin.
KeywordsMolecular chaperone Prefoldin Chaperonin
This work partly supported by grants-in-aids for scientific research (JP16H04572, JP16H00753 and JP15J08261) from the Ministry of Education, Science, Sports, and Culture of Japan and the World Class Professor Program (No. 168.A10/D2/KP/2017) from Ministry of Research, Technology and Higher Education of the Republic of Indonesia.
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Conflict of interest
Muhamad Sahlan declares that he has no conflict of interest. Tamotsu Zako declares that he has no conflict of interest. Masafumi Yohda declares that he has no conflict of interest.
This article does not contain any studies with human participants or animals performed by any of the authors.
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