Prefoldin, a jellyfish-like molecular chaperone: functional cooperation with a group II chaperonin and beyond

Muhamad Sahlan, Tamotsu Zako, Masafumi Yohda

Research output: Contribution to journalReview articlepeer-review

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)339-345
Number of pages7
JournalBiophysical Reviews
Volume10
Issue number2
DOIs
Publication statusPublished - 1 Apr 2018

Keywords

  • Chaperonin
  • Molecular chaperone
  • Prefoldin

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