scholarly journals Caught in the middle: the role of Bag3 in disease

2009 ◽  
Vol 425 (1) ◽  
pp. e1-e3 ◽  
Author(s):  
Andrea K. McCollum ◽  
Giovanna Casagrande ◽  
Elise C. Kohn
Keyword(s):  
Heat Shock ◽  
Muscular Dystrophy ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Small Heat Shock Protein ◽  
Cag Repeats ◽  
Binding Partner ◽  
Biochemical Journal ◽  
Exon 1

Bag3 is a Bag family co-chaperone that regulates the ATPase activity of Hsp70 (heat-shock protein 70) chaperones. Recent studies have demonstrated that Bag3 can initiate macroautophagy in co-operation with small heat-shock protein HspB8. In this issue of the Biochemical Journal, Fuchs and co-workers have discovered the IPV motif in Bag3 that is necessary for binding to HspB8. The authors have also identified HspB6 as a new binding partner for Bag3 and characterized further the binding of both HspB8 and HspB6 in Bag3-mediated clearance of aggregated polyglutamine-containing protein Htt43Q (huntingtin exon 1 fragment with 43 CAG repeats). It is clear from recent identification of a Bag3 mutation that causes a form of muscular dystrophy that the full function of Bag3 in disease is not clear. We will apply the findings of Fuchs et al. in this issue to reconcile the phenotypes of Bag3 homologue knockouts with the emerging role of Bag3 in autophagy.

Protective role of myocardial heat shock protein 70 in burn trauma: Another brick in the wall?

2004 ◽  
Vol 32 (6) ◽  
pp. 1425-1426 ◽  
Author(s):  
Martin Westphal ◽  
Perenlei Enkhbaatar ◽  
Daniel L. Traber
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Protective Role ◽  
Burn Trauma

scholarly journals Role of the Conserved SRLFDQFFG Region of α-Crystallin, a Small Heat Shock Protein

2003 ◽  
Vol 278 (51) ◽  
pp. 51159-51166 ◽  
Author(s):  
Saloni Yatin Pasta ◽  
Bakthisaran Raman ◽  
Tangirala Ramakrishna ◽  
Ch. Mohan Rao
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein

The Role of Heat Shock Protein 70 in Infection and Immunity

2015 ◽  
pp. 95-117
Author(s):  
Jose Rey-Ladino ◽  
Abiola Senok ◽  
Abdullah Sarkar ◽  
Ahlam Al Shedoukhy
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70

The role of heat shock protein 70 in the thermoresistance of prostate cancer cell line spheroids

FEBS Letters ◽  
2004 ◽  
Vol 561 (1-3) ◽  
pp. 144-148 ◽  
Author(s):  
Samideh Khoei ◽  
Bahram Goliaei ◽  
Ali Neshasteh-Riz ◽  
Abdolkhalegh Deizadji
Keyword(s):  
Prostate Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cell Line ◽  
Cancer Cell ◽  
Heat Shock Protein 70 ◽  
Prostate Cancer Cell ◽  
Cancer Cell Line ◽  
Prostate Cancer Cell Line

Protective role of Mycobacterium leprae small heat-shock protein in heterologous hosts, Escherichia coli and Mycobacterium smegmatis, grown under stress

2013 ◽  
Vol 62 (7) ◽  
pp. 959-967 ◽  
Author(s):  
Jayapal Jeya Maheshwari ◽  
Kuppamuthu Dharmalingam
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mycobacterium Smegmatis ◽  
Small Heat Shock Protein ◽  
Mycobacterium Leprae ◽  
Protective Role ◽  
Low Oxygen

The aim of this study is to examine the in vivo role of a small heat-shock protein (sHsp18) from Mycobacterium leprae in the survival of heterologous recombinant hosts carrying the gene encoding this protein under different environmental conditions that are normally encountered by M. leprae during its infection of the human host. Using an Escherichia coli system where shsp18 expression is controlled by its native promoter, we show that expression of shsp18 is induced under low oxygen tension, nutrient depletion and oxidative stress, all of which reflect the natural internal environment of the granulomas where the pathogen resides for long periods. We demonstrate the in vivo chaperone activity of sHsp18 through its ability to confer survival advantage to recombinant E. coli at heat-shock temperatures. Additional evidence for the protective role of sHsp18 was obtained when Mycobacterium smegmatis harbouring a copy of shsp18 was found to multiply better in human macrophages. Furthermore, the autokinase activity of sHsp18 protein demonstrated for what is believed to be the first time in this study implies that some of the functions of sHsp18 might be controlled by the phosphorylation state of this protein. Results from this study suggest that shsp18 might be one of the factors that facilitate the survival and persistence of M. leprae under stress and autophosphorylation of sHsp18 protein could be a mechanism used by this protein to sense changes in the external environment.

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