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TitleA structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 1007, Year 2024
Publish dateFeb 2, 2024
AuthorsJunsun Park / Hyunmin Kim / Daniel Gestaut / Seyeon Lim / Kwadwo A Opoku-Nsiah / Alexander Leitner / Judith Frydman / Soung-Hun Roh /
PubMed AbstractProper cellular proteostasis, essential for viability, requires a network of chaperones and cochaperones. ATP-dependent chaperonin TRiC/CCT partners with cochaperones prefoldin (PFD) and phosducin- ...Proper cellular proteostasis, essential for viability, requires a network of chaperones and cochaperones. ATP-dependent chaperonin TRiC/CCT partners with cochaperones prefoldin (PFD) and phosducin-like proteins (PhLPs) to facilitate folding of essential eukaryotic proteins. Using cryoEM and biochemical analyses, we determine the ATP-driven cycle of TRiC-PFD-PhLP2A interaction. PhLP2A binds to open apo-TRiC through polyvalent domain-specific contacts with its chamber's equatorial and apical regions. PhLP2A N-terminal H3-domain binding to subunits CCT3/4 apical domains displace PFD from TRiC. ATP-induced TRiC closure rearranges the contacts of PhLP2A domains within the closed chamber. In the presence of substrate, actin and PhLP2A segregate into opposing chambers, each binding to positively charged inner surface residues from CCT1/3/6/8. Notably, actin induces a conformational change in PhLP2A, causing its N-terminal helices to extend across the inter-ring interface to directly contact a hydrophobic groove in actin. Our findings reveal an ATP-driven PhLP2A structural rearrangement cycle within the TRiC chamber to facilitate folding.
External linksNat Commun / PubMed:38307855 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 4.42 Å
Structure data

35122

8i1u

EMDB-35122, PDB-8i1u:
Human TRiC-PhLP2A complex in the closed state
Method: EM (single particle) / Resolution: 3.24 Å

35199

8i6j

EMDB-35199, PDB-8i6j:
The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state
Method: EM (single particle) / Resolution: 3.82 Å

35280

8i9q

EMDB-35280, PDB-8i9q:
The focused refinement of CCT4-PhLP2A from TRiC-PhLP2A complex in the open state
Method: EM (single particle) / Resolution: 4.22 Å

35284

8i9u

EMDB-35284, PDB-8i9u:
Human TRiC-PhLP2A complex in the open state
Method: EM (single particle) / Resolution: 3.1 Å

35335

8ib8

EMDB-35335, PDB-8ib8:
Human TRiC-PhLP2A-actin complex in the closed state
Method: EM (single particle) / Resolution: 4.42 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-AF3:
ALUMINUM FLUORIDE

Source
  • homo sapiens (human)
KeywordsCHAPERONE / chaperonin complex / cochaperone / chapronin complex

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