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ISSN: 2329-6798

Modern Chemistry & Applications
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Research Article

Structural Investigation of HSP70-HSP90 and HSP90-TDF Interactions

Urmi Roy, Alisa G Woods, Izabela Sokolowska and Costel C Darie*
Department of Chemistry and Biomolecular Science, Clarkson University, USA
Corresponding Author : Costel C Darie
Biochemistry & Proteomics Group
Structural Biology & Molecular Modeling Unit
Department of Chemistry & Biomolecular Science
Clarkson University, 8 Clarkson Avenue
Potsdam, NY, 13699-5810, USA
Tel: 315-268-7763
Fax: 315-268-6610
E-mail: [email protected]
Received March 20, 2014; Accepted May 27, 2014; Published May 30, 2014
Citation: Roy U, Woods AG, Sokolowska I, Darie CC (2014) Structural Investigation of HSP70-HSP90 and HSP90-TDF Interactions. Mod Chem appl 2:126. doi:10.4172/2329-6798.1000126
Copyright: © 2014 Roy U, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

Tumor Differentiation Factor (TDF) is a pituitary protein, which is secreted into the blood stream and targets breast and prostate. The end effect of TDF on these tissues is differentiation of breast and prostate cells. However, it is not yet clear how TDF induces cell differentiation. Studies in our laboratory determined that the potential TDF receptor candidates are: HSPA8, a member of the 70 kDa heat shock protein family and HSP90 protein. Our previous studies also indicated that TDF may have an inducible receptor, composed of both HSP70 and HSP90, and that TDF signaling depends on the interaction of these proteins. Here we provide additional insights about the proposed interaction between HSP70 and HSP90 and about the HSP90-TDF interaction.

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