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Structural and Biological Interaction of hsc-70 Protein with Phosphatidylserine in Endosomal Microautophagy.

J. Biol. Chem.. 2016-12; 
MorozovaKateryna,ClementCristina C,KaushikSusmita,StillerBarbara,AriasEsperanza,AhmadAtta,RauchJennifer N,ChatterjeeVictor,MelisChiara,ScharfBrian,GestwickiJason E,CuervoAna-Maria,ZuiderwegErik R P,SantambrogioL
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Mutagenesis Services The hsc-70 mutants (R533A, R535A, K573Q, K583Q, K589Q, K597Q, and K601Q) were generated using site-directed mutagenesis with the mouse wild-type hsc-70 cDNA as template (GenScript, Piscataway, NJ). Get A Quote

摘要

hsc-70 (HSPA8) is a cytosolic molecular chaperone, which plays a central role in cellular proteostasis, including quality control during protein refolding and regulation of protein degradation. hsc-70 is pivotal to the process of macroautophagy, chaperone-mediated autophagy, and endosomal microautophagy. The latter requires hsc-70 interaction with negatively charged phosphatidylserine (PS) at the endosomal limiting membrane. Herein, by combining plasmon resonance, NMR spectroscopy, and amino acid mutagenesis, we mapped the C terminus of the hsc-70 LID domain as the structural interface interacting with endosomal PS, and we estimated an hsc-70/PS equilibrium dissociation constant of 4.7 ± 0.1 ... More

关键词

70-kilodalton heat shock protein (Hsp70),autophagy,chaperone,endosome,phosphatidylse