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Article

Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct.

The Journal of biological chemistry - 9 Jul 2010

Hale Sarah J, Lovell Simon C, de Keyzer Jeanine, Stirling Colin J

Abstract excerpt

Kar2p, an essential Hsp70 chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae, facilitates the transport and folding of nascent polypeptides within the endoplasmic reticulum lumen. The chaperone activity of Kar2p is regulated by its intrinsic ATPase activity that can be stimulated by two different nucleotide exchange factors, namely Sil1p and Lhs1p. Here, we demonstrate that the binding...

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Identifiers

PMID: 20430899
DOI: 10.1074/jbc.M110.111211
PMCID: PMC2898433

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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.

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Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct.PMID 20430899Read ↗

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