Coordinated activation of Hsp70 chaperones.
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 reciprocally activated the Lhs1p adenosine triphosphatase (ATPase). The two ATPase activities are coupled, and their coordinated regulation is essential for normal function in vivo.
Mesh Terms:
Adenosine Triphosphatases, Adenosine Triphosphate, Carrier Proteins, Endoplasmic Reticulum, Guanine Nucleotide Exchange Factors, HSP70 Heat-Shock Proteins, Heat-Shock Proteins, Membrane Transport Proteins, Molecular Chaperones, Mutation, Protein Binding, Protein Folding, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Adenosine Triphosphatases, Adenosine Triphosphate, Carrier Proteins, Endoplasmic Reticulum, Guanine Nucleotide Exchange Factors, HSP70 Heat-Shock Proteins, Heat-Shock Proteins, Membrane Transport Proteins, Molecular Chaperones, Mutation, Protein Binding, Protein Folding, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Science
Date: Jan. 02, 2004
PubMed ID: 14704430
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