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

Coordinated activation of Hsp70 chaperones.

Science (New York, N.Y.) - 2 Jan 2004

Steel Gregor J, Fullerton Donna M, Tyson John R, Stirling Colin J

Abstract excerpt

Hsp70s are a ubiquitous family of molecular chaperones involved in many cellular processes. Two Hsp70s, Lhs1p and Kar2p, are required for protein biogenesis in the yeast endoplasmic reticulum. Here, we found that Lhs1p and Kar2p specifically interacted to couple, and coordinately regulate, their respective activities. Lhs1p stimulated Kar2p by providing a specific nucleotide exchange activity, whereas Kar2p...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Adenosine Triphosphate
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanine Nucleotide Exchange Factors

Share to Heat-Shock Proteins

Share to HSP70 Heat-Shock Proteins

Share to Molecular Chaperones

Share to Protein Folding

Source

Identifiers

PMID: 14704430
DOI: 10.1126/science.1092287

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Coordinated activation of Hsp70 chaperones.PMID 14704430Read ↗

Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct.Semantic proximity Read ↗

Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.Semantic proximity Read ↗

Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Semantic proximity Read ↗

Role of the HSP70 Co-Chaperone SIL1 in Health and Disease.Semantic proximity Read ↗

Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p.Semantic proximity Read ↗

The Role of Non-Canonical Hsp70s (Hsp110/Grp170) in CancerSemantic proximity Read ↗

With or Without You: Co-chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein TriageSemantic proximity Read ↗

The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb.Semantic proximity Read ↗

The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel.Semantic proximity Read ↗

Inhibition of heat tolerance and nuclear import of Gts1p by Ssa1p and Ssa2p.Semantic proximity Read ↗

Functional and physical interaction between yeast Hsp90 and Hsp70.Semantic proximity Read ↗

Tuning the Hsp70 Chaperone Cycle: Emerging Roles of GrpE-Like NEFs in Proteostasis and Organelle FunctionSemantic proximity Read ↗

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