Next Article in Journal
Roles of Prolyl Isomerases in RNA-Mediated Gene Expression
Next Article in Special Issue
Characterization of Receptor Binding Profiles of Influenza A Viruses Using An Ellipsometry-Based Label-Free Glycan Microarray Assay Platform
Previous Article in Journal
RNA-Mediated Regulation of HMGA1 Function
Previous Article in Special Issue
Overcoming Challenges and Opening New Opportunities in Glycoproteomics
Article Menu

Export Article

Open AccessArticle
Biomolecules 2015, 5(2), 958-973;

Sulfatide-Hsp70 Interaction Promotes Hsp70 Clustering and Stabilizes Binding to Unfolded Protein

The Laboratory of Animal Cell Function, Bioscience and Biotechnology Center, Nagoya University, Nagoya 464-8601, Japan
Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
Current address: Department of Systems Biology in Thromboregulation, Kagoshima University Graduate School of Medical and Dental Sciences, 8-35-1 Sakuragaoka, Kagoshima 890-8544, Japan.
Author to whom correspondence should be addressed.
Academic Editor: Hans Vliegenthart
Received: 26 February 2015 / Revised: 24 April 2015 / Accepted: 7 May 2015 / Published: 15 May 2015
(This article belongs to the Special Issue Challenges in Glycan, Glycoprotein and Proteoglycan Research)
Full-Text   |   PDF [2035 KB, uploaded 15 May 2015]   |  


The 70-kDa heat shock protein (Hsp70), one of the major stress-inducible molecular chaperones, is localized not only in the cytosol, but also in extracellular milieu in mammals. Hsp70 interacts with various cell surface glycolipids including sulfatide (3'-sulfogalactosphingolipid). However, the molecular mechanism, as well as the biological relevance, underlying the glycolipid-Hsp70 interaction is unknown. Here we report that sulfatide promotes Hsp70 oligomerization through the N-terminal ATPase domain, which stabilizes the binding of Hsp70 to unfolded protein in vitro. We find that the Hsp70 oligomer has apparent molecular masses ranging from 440 kDa to greater than 669 kDa. The C-terminal peptide-binding domain is dispensable for the sulfatide-induced oligomer formation. The oligomer formation is impaired in the presence of ATP, while the Hsp70 oligomer, once formed, is unable to bind to ATP. These results suggest that sulfatide locks Hsp70 in a high-affinity state to unfolded proteins by clustering the peptide-binding domain and blocking the binding to ATP that induces the dissociation of Hsp70 from protein substrates. View Full-Text
Keywords: high molecular-weight complex; Hsp70; oligomerization; sulfatide high molecular-weight complex; Hsp70; oligomerization; sulfatide

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Harada, Y.; Sato, C.; Kitajima, K. Sulfatide-Hsp70 Interaction Promotes Hsp70 Clustering and Stabilizes Binding to Unfolded Protein. Biomolecules 2015, 5, 958-973.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top