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

Author

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

Subjects
Evolution, Hsp70 cycle, JDP, HSP70 Heat-Shock Proteins, Molecular Chaperones, Poland, HSP40 Heat-Shock Proteins
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

9. Role for ribosome-associated complex and stress-seventy subfamily B (RAC-Ssb) in integral membrane protein translation

Author

Acosta-Sampson, Ligia, Döring, Kristina, Lin, Yuping, Yu, Vivian Y, Bukau, Bernd, Kramer, Günter, and Cate, Jamie HD

Subjects
Biochemistry and Cell Biology, Biological Sciences, Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, Codon, Cytoplasm, Fungal Proteins, Membrane Proteins, Neurospora crassa, Oxidative Stress, Protein Biosynthesis, Proteostasis, RNA, Messenger, Ribosomes, Saccharomyces cerevisiae, Unfolded Protein Response, chaperone, membrane protein, protein synthesis, translation control, unfolded protein response, stress-seventy subfamily B, major facilitator superfamily, ribosome associated complex, Chemical Sciences, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Chemical sciences
Abstract

Targeting of most integral membrane proteins to the endoplasmic reticulum is controlled by the signal recognition particle, which recognizes a hydrophobic signal sequence near the protein N terminus. Proper folding of these proteins is monitored by the unfolded protein response and involves protein degradation pathways to ensure quality control. Here, we identify a new pathway for quality control of major facilitator superfamily transporters that occurs before the first transmembrane helix, the signal sequence recognized by the signal recognition particle, is made by the ribosome. Increased rates of translation elongation of the N-terminal sequence of these integral membrane proteins can divert the nascent protein chains to the ribosome-associated complex and stress-seventy subfamily B chaperones. We also show that quality control of integral membrane proteins by ribosome-associated complex-stress-seventy subfamily B couples translation rate to the unfolded protein response, which has implications for understanding mechanisms underlying human disease and protein production in biotechnology.

Published
2017

18. HSP40 proteins use class-specific regulation to drive HSP70 functional diversity

Author

Faust, Ofrah, Abayev-Avraham, Meital, Wentink, Anne S., Maurer, Michael, Nillegoda, Nadinath B., London, Nir, and Bukau, Bernd

Subjects
Health aspects, Heat shock proteins -- Health aspects
Abstract

Author(s): Ofrah Faust [sup.1] , Meital Abayev-Avraham [sup.1] , Anne S. Wentink [sup.2] , Michael Maurer [sup.1] [sup.2] , Nadinath B. Nillegoda [sup.2] [sup.3] , Nir London [sup.4] , Bernd [...], The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular chaperones, which perform numerous cellular functions that affect almost all aspects of the protein life cycle from synthesis to degradation.sup.1-3. Achieving this broad spectrum of functions requires precise regulation of HSP70 activity. Proteins of the HSP40 family, also known as J-domain proteins (JDPs), have a key role in this process by preselecting substrates for transfer to their HSP70 partners and by stimulating the ATP hydrolysis of HSP70, leading to stable substrate binding.sup.3,4. In humans, JDPs constitute a large and diverse family with more than 40 different members.sup.2, which vary in their substrate selectivity and in the nature and number of their client-binding domains.sup.5. Here we show that JDPs can also differ fundamentally in their interactions with HSP70 chaperones. Using nuclear magnetic resonance spectroscopy.sup.6,7 we find that the major class B JDPs are regulated by an autoinhibitory mechanism that is not present in other classes. Although in all JDPs the interaction of the characteristic J-domain is responsible for the activation of HSP70, in DNAJB1 the HSP70-binding sites in this domain are intrinsically blocked by an adjacent glycine-phenylalanine rich region--an inhibition that can be released upon the interaction of a second site on DNAJB1 with the HSP70 C-terminal tail. This regulation, which controls substrate targeting to HSP70, is essential for the disaggregation of amyloid fibres by HSP70-DNAJB1, illustrating why no other class of JDPs can substitute for class B in this function. Moreover, this regulatory layer, which governs the functional specificities of JDP co-chaperones and their interactions with HSP70s, could be key to the wide range of cellular functions of HSP70. The binding and activation of HSP70 by class B J-domain proteins is subject to an autoinhibitory regulatory mechanism that controls substrate targeting to HSP70 and is required for the disaggregation of amyloid fibres.

Published
2020
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19. 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

21. GPD1 Specifically Marks Dormant Glioma Stem Cells with a Distinct Metabolic Profile

Author

Rusu, Patricia, Shao, Chunxuan, Neuerburg, Anna, Acikgöz, Azer Aylin, Wu, Yonghe, Zou, Peng, Phapale, Prasad, Shankar, Tchirupura S., Döring, Kristina, Dettling, Steffen, Körkel-Qu, Huiqin, Bekki, Gözde, Costa, Barbara, Guo, Te, Friesen, Olga, Schlotter, Magdalena, Heikenwalder, Mathias, Tschaharganeh, Darjus F., Bukau, Bernd, Kramer, Günter, Angel, Peter, Herold-Mende, Christel, Radlwimmer, Bernhard, and Liu, Hai-Kun

Published
2019
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23. Processive extrusion of polypeptide loops by a Hsp100 disaggregase

Author

Avellaneda, Mario J., Franke, Kamila B., Sunderlikova, Vanda, Bukau, Bernd, Mogk, Axel, and Tans, Sander J.

Subjects
Physiological aspects, Polypeptides -- Physiological aspects, Heat shock proteins -- Physiological aspects
Abstract

Author(s): Mario J. Avellaneda [sup.1] , Kamila B. Franke [sup.2] , Vanda Sunderlikova [sup.1] , Bernd Bukau [sup.2] , Axel Mogk [sup.2] , Sander J. Tans [sup.1] [sup.3] Author Affiliations: [...], The ability to reverse protein aggregation is vital to cells.sup.1,2. Hsp100 disaggregases such as ClpB and Hsp104 are proposed to catalyse this reaction by translocating polypeptide loops through their central pore.sup.3,4. This model of disaggregation is appealing, as it could explain how polypeptides entangled within aggregates can be extracted and subsequently refolded with the assistance of Hsp70.sup.4,5. However, the model is also controversial, as the necessary motor activity has not been identified.sup.6-8 and recent findings indicate non-processive mechanisms such as entropic pulling or Brownian ratcheting.sup.9,10. How loop formation would be accomplished is also obscure. Indeed, cryo-electron microscopy studies consistently show single polypeptide strands in the Hsp100 pore.sup.11,12. Here, by following individual ClpB-substrate complexes in real time, we unambiguously demonstrate processive translocation of looped polypeptides. We integrate optical tweezers with fluorescent-particle tracking to show that ClpB translocates both arms of the loop simultaneously and switches to single-arm translocation when encountering obstacles. ClpB is notably powerful and rapid; it exerts forces of more than 50 pN at speeds of more than 500 residues per second in bursts of up to 28 residues. Remarkably, substrates refold while exiting the pore, analogous to co-translational folding. Our findings have implications for protein-processing phenomena including ubiquitin-mediated remodelling by Cdc48 (or its mammalian orthologue p97).sup.13 and degradation by the 26S proteasome.sup.14. A combination of optical tweezers and fluorescent-particle tracking is used to dissect the dynamics of the Hsp100 disaggregase ClpB, and show that the processive extrusion of polypeptide loops is the mechanistic basis of its activity.

Published
2020
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30. The growing world of small heat shock proteins: from structure to functions

Author

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

Published
2017

38. Binding Specificity of Escherichia coli Trigger Factor

Author

Patzelt, Holger, Rüdiger, Stefan, Brehmer, Dirk, Kramer, Günter, Vorderwülbecke, Sonja, Schaffitzel, Elke, Waitz, Andreas, Hesterkamp, Thomas, Dong, Liying, Schneider-Mergener, Jens, Bukau, Bernd, and Deuerling, Elke

Published
2001

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