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

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

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...

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Bibliographic Details
Main Authors: Yoichiro Harada, Chihiro Sato, Ken Kitajima
Format: Article
Language:English
Published: MDPI AG 2015-05-01
Series:Biomolecules
Subjects:
high molecular-weight complex
Hsp70
oligomerization
sulfatide
Online Access:http://www.mdpi.com/2218-273X/5/2/958

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