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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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

da Silva, Kelly P. [1] ; Borges, Julio C. [1]
Número total de Autores: 2
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Inst Chem Sao Carlos, IQSC, BR-13560970 Sao Carlos, SP - Brazil
Número total de Afiliações: 1
Tipo de documento: Artigo Científico
Fonte: PROTEIN AND PEPTIDE LETTERS; v. 18, n. 2, p. 132-142, FEB 2011.
Citações Web of Science: 24

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)

Processo FAPESP: 08/09025-8 - Estudo da chaperone molecular Hsp90 e sua co-chaperone p23 de Plasmodium Falciparum e Leishmania braziliensis
Beneficiário:Kelly Pereira da Silva
Linha de fomento: Bolsas no Brasil - Doutorado
Processo FAPESP: 07/05001-4 - Estudos dos sistemas chaperones moleculares HSP70 e HSP90 de parasitas
Beneficiário:Julio Cesar Borges
Linha de fomento: Auxílio à Pesquisa - Apoio a Jovens Pesquisadores