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Characteristics of the interaction between Hsc70 and the transferrin receptor in exosomes released during reticulocyte maturation.

Authors: Geminard, C  Nault, F  Johnstone, RM  Vidal, M 
Citation: Geminard C, etal., J Biol Chem. 2001 Mar 30;276(13):9910-6. Epub 2000 Dec 22.
Pubmed: (View Article at PubMed) PMID:11133993
DOI: Full-text: DOI:10.1074/jbc.M009641200

The transferrin receptor (TfR) of reticulocytes is released in vesicular form (exosomes) during their maturation to erythrocytes. The heat shock cognate 70-kDa protein (Hsc70) has been demonstrated to interact with the cytosolic domain of the TfR and could thus trigger the receptor toward this secretion pathway. We investigated the characteristics of the interaction between Hsc70 and the TfR in exosomes with an in vitro binding assay using TfR immobilized on Sepharose beads and purified Hsc70. The results show that Hsc70 binds to exosomal TfR with characteristics expected of a chaperone/peptide interaction. We demonstrated that heat-denatured luciferase competed for in vitro binding, dependent on the nucleotide bound to Hsc70, and that this interaction activates the ATPase activity of Hsc70. Moreover, we used immunosuppressive agents that interact with Hsc70, thus decreasing Hsc70 binding to TfR in our in vitro binding assay and enabling us to assess the role of this interaction in vivo during reticulocyte maturation.

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RGD Object Information
RGD ID: 2326097
Created: 2010-06-23
Species: All species
Last Modified: 2010-06-23
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.