Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates.

The Journal of biological chemistry - 17 Mar 2006

Stirling Peter C, Cuéllar Jorge, Alfaro Gabriel A, El Khadali Fatima, Beh Christopher T, Valpuesta José M, Melki Ronald, Leroux Michel R

Abstract excerpt

Many ATP-dependent molecular chaperones, including Hsp70, Hsp90, and the chaperonins GroEL/Hsp60, require cofactor proteins to regulate their ATPase activities and thus folding functions in vivo. One conspicuous exception has been the eukaryotic chaperonin CCT, for which no regulator of its ATPase activity, other than non-native substrate proteins, is known. We identify the evolutionarily conserved PhLP3...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Chaperonins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoskeleton

Share to Image Processing, Computer-Assisted

Share to Microscopy, Electron

Share to Microtubules

Share to Testis

Share to Tubulin

Source

Identifiers

PMID: 16415341
DOI: 10.1074/jbc.M513235200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates.PMID 16415341Read ↗

Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progression.Semantic proximity Read ↗

A two-step mechanism for the folding of actin by the yeast cytosolic chaperonin.Semantic proximity Read ↗

Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunit.Semantic proximity Read ↗

Equivalent mutations in the eight subunits of the chaperonin CCT produce dramatically different cellular and gene expression phenotypes.Semantic proximity Read ↗

Analysis of mutationally altered forms of the Cct6 subunit of the chaperonin from Saccharomyces cerevisiae.Semantic proximity Read ↗

Defects in Protein Folding Machinery Affect Cell Wall Integrity and Reduce Ethanol Tolerance in S. cerevisiae.Semantic proximity Read ↗

Chaperone Requirements for De Novo Folding of <i>Saccharomyces cerevisiae</i> SeptinsSemantic proximity Read ↗

Cryptic out-of-frame translational initiation of TBCE rescues tubulin formation in compound heterozygous HRD.Semantic proximity Read ↗

Interaction of p53 with the CCT complex promotes protein folding and wild-type p53 activity.Semantic proximity Read ↗

Disease-causing mutations in the G protein β5 β-propeller disrupt its chaperonin-mediated folding trajectorySemantic proximity Read ↗

Overexpressed ribosomal proteins suppress defective chaperonins in Saccharomyces cerevisiae.Semantic proximity Read ↗

A chaperonin subunit with unique structures is essential for folding of a specific substrate.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.