Search

Your search keyword '"Liberek, Krzysztof"' showing total 11 results
Start Over Author "Liberek, Krzysztof" Database OAIster
11 results on '"Liberek, Krzysztof"'

1. J-domain proteins:From molecular mechanisms to diseases

Author

Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias P., Adupa, Vasista, Andréasson, Claes, Blatch, Gregory L., Braun, Janice E.A., Brodsky, Jeffrey L., Bukau, Bernd, Chapple, J. Paul, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin M., Hines, Justin K., Ishikawa, Koji, Joachimiak, Lukasz A., Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos H.I., Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, Kampinga, Harm H., Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias P., Adupa, Vasista, Andréasson, Claes, Blatch, Gregory L., Braun, Janice E.A., Brodsky, Jeffrey L., Bukau, Bernd, Chapple, J. Paul, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin M., Hines, Justin K., Ishikawa, Koji, Joachimiak, Lukasz A., Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos H.I., Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, and Kampinga, Harm H.

Abstract

J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.

Published
2024

2. J-domain proteins: From molecular mechanisms to diseases.

Author

Marszalek, Jaroslaw, Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias, Adupa, Vasista, Andréasson, Claes, Blatch, Gregory, Braun, Janice, Brodsky, Jeffrey, Bukau, Bernd, Chapple, J, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin, Hines, Justin, Ishikawa, Koji, Joachimiak, Lukasz, Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos, Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, Kampinga, Harm, Marszalek, Jaroslaw, Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias, Adupa, Vasista, Andréasson, Claes, Blatch, Gregory, Braun, Janice, Brodsky, Jeffrey, Bukau, Bernd, Chapple, J, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin, Hines, Justin, Ishikawa, Koji, Joachimiak, Lukasz, Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos, Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, and Kampinga, Harm

Abstract

J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.

Published
2024

3. J-domain proteins : From molecular mechanisms to diseases

Author

Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias P., Adupa, Vasista, Andréasson, Claes, Blatch, Gregory L., Braun, Janice E. A., Brodsky, Jeffrey L., Bukau, Bernd, Chapple, J. Paul, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin M., Hines, Justin K., Ishikawa, Koji, Joachimiak, Lukasz A., Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos H. I., Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, Kampinga, Harm H., Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias P., Adupa, Vasista, Andréasson, Claes, Blatch, Gregory L., Braun, Janice E. A., Brodsky, Jeffrey L., Bukau, Bernd, Chapple, J. Paul, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin M., Hines, Justin K., Ishikawa, Koji, Joachimiak, Lukasz A., Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos H. I., Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, and Kampinga, Harm H.

Abstract

J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.

Published
2024
Full Text
View/download PDF

4. J-domain proteins:From molecular mechanisms to diseases

Author

Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias P., Adupa, Vasista, Andréasson, Claes, Blatch, Gregory L., Braun, Janice E.A., Brodsky, Jeffrey L., Bukau, Bernd, Chapple, J. Paul, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin M., Hines, Justin K., Ishikawa, Koji, Joachimiak, Lukasz A., Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos H.I., Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, Kampinga, Harm H., Marszalek, Jaroslaw, De Los Rios, Paolo, Cyr, Douglas, Mayer, Matthias P., Adupa, Vasista, Andréasson, Claes, Blatch, Gregory L., Braun, Janice E.A., Brodsky, Jeffrey L., Bukau, Bernd, Chapple, J. Paul, Conz, Charlotte, Dementin, Sébastien, Genevaux, Pierre, Genest, Olivier, Goloubinoff, Pierre, Gestwicki, Jason, Hammond, Colin M., Hines, Justin K., Ishikawa, Koji, Joachimiak, Lukasz A., Kirstein, Janine, Liberek, Krzysztof, Mokranjac, Dejana, Nillegoda, Nadinath, Ramos, Carlos H.I., Rebeaud, Mathieu, Ron, David, Rospert, Sabine, Sahi, Chandan, Shalgi, Reut, Tomiczek, Bartlomiej, Ushioda, Ryo, Ustyantseva, Elizaveta, Ye, Yihong, Zylicz, Maciej, and Kampinga, Harm H.

Abstract

J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.

Published
2024

5. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H, Kampinga, Harm H, Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E, Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E, Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P, Nagata, Kazuhiro, Nillegoda, Nadinath B, Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratłomiej, Ushioda, Ryo, Young, Jason C, Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A, Marszalek, Jaroslaw, Kampinga, Harm H, Kampinga, Harm H, Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E, Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E, Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P, Nagata, Kazuhiro, Nillegoda, Nadinath B, Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratłomiej, Ushioda, Ryo, Young, Jason C, Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A, and Marszalek, Jaroslaw

Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

Published
2019

6. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratlomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., Marszalek, Jaroslaw, Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratlomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., and Marszalek, Jaroslaw

Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

Published
2019
Full Text
View/download PDF

7. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratłomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., Marszalek, Jaroslaw, Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratłomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., and Marszalek, Jaroslaw

Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

Published
2019
Full Text
View/download PDF

8. Function, evolution, and structure of J-domain proteins

Author

Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratłomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., Marszalek, Jaroslaw, Kampinga, Harm H., Andreasson, Claes, Barducci, Alessandro, Cheetham, Michael E., Cyr, Douglas, Emanuelsson, Cecilia, Genevaux, Pierre, Gestwicki, Jason E., Goloubinoff, Pierre, Huerta-Cepas, Jaime, Kirstein, Janine, Liberek, Krzysztof, Mayer, Matthias P., Nagata, Kazuhiro, Nillegoda, Nadinath B., Pulido, Pablo, Ramos, Carlos, De los Rios, Paolo, Rospert, Sabine, Rosenzweig, Rina, Sahi, Chandan, Taipale, Mikko, Tomiczek, Bratłomiej, Ushioda, Ryo, Young, Jason C., Zimmermann, Richard, Zylicz, Alicja, Zylicz, Maciej, Craig, Elizabeth A., and Marszalek, Jaroslaw

Abstract

Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.

Published
2019
Full Text
View/download PDF

9. Small heat shock proteins: multifaceted proteins with important implications for life

Author

Carra, Serena, Alberti, Simon, Benesch, Justin, Boelens, Wilbert C, Buchner, Johannes, Carver, John A, Cecconi, Ciro, Ecroyd, Heath, Gusev, Nikolai, Hightower, Lawrence, Klevit, Rachel, Lee, Hyun, Liberek, Krzysztof, Lockwood, Brent, Poletti, Angelo, Timmerman, Vincent, Toth, Melinda, Vierling, Elizabeth, Wu, Tangchun, Tanguay, Robert, Carra, Serena, Alberti, Simon, Benesch, Justin, Boelens, Wilbert C, Buchner, Johannes, Carver, John A, Cecconi, Ciro, Ecroyd, Heath, Gusev, Nikolai, Hightower, Lawrence, Klevit, Rachel, Lee, Hyun, Liberek, Krzysztof, Lockwood, Brent, Poletti, Angelo, Timmerman, Vincent, Toth, Melinda, Vierling, Elizabeth, Wu, Tangchun, and Tanguay, Robert

Abstract

Small Heat Shock Proteins (sHSPs) evolved early in the history of life; they are present in archaea, bacteria, and eukaryota. sHSPs belong to the superfamily of molecular chaperones: they are components of the cellular protein quality control machinery and are thought to act as the first line of defense against conditions that endanger the cellular proteome. In plants, sHSPs protect cells against abiotic stresses, providing innovative targets for sustainable agricultural production. In humans, sHSPs (also known as HSPBs) are associated with the development of several neurological diseases. Thus, manipulation of sHSP expression may represent an attractive therapeutic strategy for disease treatment. Experimental evidence demonstrates that enhancing the chaperone function of sHSPs protects against age-related protein conformation diseases, which are characterized by protein aggregation. Moreover, sHSPs can promote longevity and healthy aging in vivo. In addition, sHSPs have been implicated in the prognosis of several types of cancer. Here, sHSP upregulation, by enhancing cellular health, could promote cancer development; on the other hand, their downregulation, by sensitizing cells to external stressors and chemotherapeutics, may have beneficial outcomes. The complexity and diversity of sHSP function and properties and the need to identify their specific clients, as well as their implication in human disease, have been discussed by many of the world's experts in the sHSP field during a dedicated workshop in Québec City, Canada, on 26-29 August 2018.

Published
2019

10. The growing world of small heat shock proteins: from structure to functions

Author

Carra, Serena, Alberti, Simon, Arrigo, Patrick, Benesch, Justin, Benjamin, Ivor, Boelens, Wilbert C, Bartelt-Kirbach, Britta, Brundel, Bianca, Buchner, Johannes, Bukau, Bernd, Carver, John A, Ecroyd, Heath, Emanuelsson, Cecilia, Finet, Stephanie, Golenhofen, Nikola, Goloubinoff, Pierre, Gusev, Nikolai, Haslbeck, Martin, Hightower, Lawrence, Kampinga, Harm, Klevit, Rachel, Liberek, Krzysztof, Mchaourab, Hassane, McMenimen, Kathryn, Poletti, Angelo, Quinlan, Roy, Strelkov, Sergei, Toth, Melinda, Vierling, Elizabeth, Tanguay, Robert, Carra, Serena, Alberti, Simon, Arrigo, Patrick, Benesch, Justin, Benjamin, Ivor, Boelens, Wilbert C, Bartelt-Kirbach, Britta, Brundel, Bianca, Buchner, Johannes, Bukau, Bernd, Carver, John A, Ecroyd, Heath, Emanuelsson, Cecilia, Finet, Stephanie, Golenhofen, Nikola, Goloubinoff, Pierre, Gusev, Nikolai, Haslbeck, Martin, Hightower, Lawrence, Kampinga, Harm, Klevit, Rachel, Liberek, Krzysztof, Mchaourab, Hassane, McMenimen, Kathryn, Poletti, Angelo, Quinlan, Roy, Strelkov, Sergei, Toth, Melinda, Vierling, Elizabeth, and Tanguay, Robert

Abstract

Small heat shock proteins (sHSPs) are present in all kingdoms of life and play fundamental roles in cell biology. sHSPs are key components of the cellular protein quality control system, acting as the first line of defense against conditions that affect protein homeostasis and proteome stability, from bacteria to plants to humans. sHSPs have the ability to bind to a large subset of substrates and to maintain them in a state competent for refolding or clearance with the assistance of the HSP70 machinery. sHSPs participate in a number of biological processes, from the cell cycle, to cell differentiation, from adaptation to stressful conditions, to apoptosis, and, even, to the transformation of a cell into a malignant state. As a consequence, sHSP malfunction has been implicated in abnormal placental development and preterm deliveries, in the prognosis of several types of cancer, and in the development of neurological diseases. Moreover, mutations in the genes encoding several mammalian sHSPs result in neurological, muscular, or cardiac age-related diseases in humans. Loss of protein homeostasis due to protein aggregation is typical of many age-related neurodegenerative and neuromuscular diseases. In light of the role of sHSPs in the clearance of un/misfolded aggregation-prone substrates, pharmacological modulation of sHSP expression or function and rescue of defective sHSPs represent possible routes to alleviate or cure protein conformation diseases. Here, we report the latest news and views on sHSPs discussed by many of the world's experts in the sHSP field during a dedicated workshop organized in Italy (Bertinoro, CEUB, October 12-15, 2016).

Published
2017

11. The growing world of small heat shock proteins: from structure to functions

Author

Carra, Serena, Alberti, Simon, Arrigo, Patrick, Benesch, Justin, Benjamin, Ivor, Boelens, Wilbert C, Bartelt-Kirbach, Britta, Brundel, Bianca, Buchner, Johannes, Bukau, Bernd, Carver, John A, Ecroyd, Heath, Emanuelsson, Cecilia, Finet, Stephanie, Golenhofen, Nikola, Goloubinoff, Pierre, Gusev, Nikolai, Haslbeck, Martin, Hightower, Lawrence, Kampinga, Harm, Klevit, Rachel, Liberek, Krzysztof, Mchaourab, Hassane, McMenimen, Kathryn, Poletti, Angelo, Quinlan, Roy, Strelkov, Sergei, Toth, Melinda, Vierling, Elizabeth, Tanguay, Robert, Carra, Serena, Alberti, Simon, Arrigo, Patrick, Benesch, Justin, Benjamin, Ivor, Boelens, Wilbert C, Bartelt-Kirbach, Britta, Brundel, Bianca, Buchner, Johannes, Bukau, Bernd, Carver, John A, Ecroyd, Heath, Emanuelsson, Cecilia, Finet, Stephanie, Golenhofen, Nikola, Goloubinoff, Pierre, Gusev, Nikolai, Haslbeck, Martin, Hightower, Lawrence, Kampinga, Harm, Klevit, Rachel, Liberek, Krzysztof, Mchaourab, Hassane, McMenimen, Kathryn, Poletti, Angelo, Quinlan, Roy, Strelkov, Sergei, Toth, Melinda, Vierling, Elizabeth, and Tanguay, Robert

Abstract

Small heat shock proteins (sHSPs) are present in all kingdoms of life and play fundamental roles in cell biology. sHSPs are key components of the cellular protein quality control system, acting as the first line of defense against conditions that affect protein homeostasis and proteome stability, from bacteria to plants to humans. sHSPs have the ability to bind to a large subset of substrates and to maintain them in a state competent for refolding or clearance with the assistance of the HSP70 machinery. sHSPs participate in a number of biological processes, from the cell cycle, to cell differentiation, from adaptation to stressful conditions, to apoptosis, and, even, to the transformation of a cell into a malignant state. As a consequence, sHSP malfunction has been implicated in abnormal placental development and preterm deliveries, in the prognosis of several types of cancer, and in the development of neurological diseases. Moreover, mutations in the genes encoding several mammalian sHSPs result in neurological, muscular, or cardiac age-related diseases in humans. Loss of protein homeostasis due to protein aggregation is typical of many age-related neurodegenerative and neuromuscular diseases. In light of the role of sHSPs in the clearance of un/misfolded aggregation-prone substrates, pharmacological modulation of sHSP expression or function and rescue of defective sHSPs represent possible routes to alleviate or cure protein conformation diseases. Here, we report the latest news and views on sHSPs discussed by many of the world's experts in the sHSP field during a dedicated workshop organized in Italy (Bertinoro, CEUB, October 12-15, 2016).

Published
2017

Catalog

Books, media, physical & digital resources
See catalog results