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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The Molecular Chaperone Hsp70 Family Members Function by a Bidirectional Heterotrophic Allosteric Mechanism

Author(s):
da Silva, Kelly P. [1] ; Borges, Julio C. [1]
Total Authors: 2
Affiliation:
[1] Univ Sao Paulo, Inst Chem Sao Carlos, IQSC, BR-13560970 Sao Carlos, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: PROTEIN AND PEPTIDE LETTERS; v. 18, n. 2, p. 132-142, FEB 2011.
Web of Science Citations: 24
Abstract

The Hsp70 family is one of the most important and conserved molecular chaperone families. It is well documented that Hsp70 family members assist many cellular processes involving protein quality control, as follows: protein folding, transport through membranes, protein degradation, escape from aggregation, intracellular signaling, among several others. The Hsp70 proteins act as a cellular pivot capable of receiving and distributing substrates among the other molecular chaperone families. Despite the high identity of the Hsp70 proteins, there are several homologue Hsp70 members that do not have the same role in the cell, which allow them to develop and participate in such large number of activities. The Hsp70 proteins are composed of two main domains: one that binds ATP and hydrolyses it to ADP and another which directly interacts with substrates. These domains present bidirectional heterotrophic allosteric regulation allowing a fine regulated cycle of substrate binding and release. The general mechanism of the Hsp70s cycle is under the control of ATP hydrolysis that modulates the low (ATP-bound state) and high (ADP-bound state) affinity states of Hsp70 for substrates. An important feature of the Hsp70s cycle is that they have several co-chaperones that modulate their cycle and that can also interact and select substrates. Here, we review some known details of the bidirectional heterotrophic allosteric mechanism and other important features for Hsp70s regulating cycle and function. (AU)

FAPESP's process: 08/09025-8 - Study of the molecular chaperone Hsp90 and its co-chaperone p23 from Plasmodium falciparum and Leishmania braziliensis
Grantee:Kelly Pereira da Silva
Support type: Scholarships in Brazil - Doctorate