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Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1
Open accessAbstract
Small heat-shock proteins (sHSPs) are a conserved group of molecular chaperones with important roles in cellular proteostasis. Although sHSPs are characterized by their small monomeric weight, they typically assemble into large polydisperse oligomers that vary in both size and shape but are principally composed of dimeric building blocks. These assemblies can include different sHSP orthologues, creating additional complexity that may affect chaperone activity. However, the structural and functional properties of such hetero-oligomers are poorly understood. We became interested in hetero-oligomer formation between human heat-shock protein family B (small) member 1 (HSPB1) and HSPB6, which are both highly expressed in skeletal muscle. When mixed in vitro , these two sHSPs form a polydisperse oligomer array composed solely of heterodimers, suggesting preferential association that is determined at the monomer level. Previously, we have shown that the sHSP N-terminal domains (NTDs), which have a high degree of intrinsic disorder, are essential for the biased formation. Here we employed iterative deletion mapping to elucidate how the NTD of HSPB6 influences its preferential association with HSPB1 and show that this region has multiple roles in this process. First, the highly conserved motif RLFDQ X FG is necessary for subunit exchange among oligomers. Second, a site ˜20 residues downstream of this motif determines the size of the resultant hetero-oligomers. Third, a region unique to HSPB6 dictates the preferential formation of heterodimers. In conclusion, the disordered NTD of HSPB6 helps regulate the size and stability of hetero-oligomeric complexes, indicating that terminal sHSP regions define the assembly properties of these proteins.
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MUSCLE: multiple sequence alignment with high accuracy and high throughput
Edgar, R. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh340 · Cited by 44,662
Protein production by auto-induction in high-density shaking cultures
Studier, F. W. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.01.016 · Cited by 5,949
PRIMUS: a Windows PC-based system for small-angle scattering data analysis
Konarev, P. V., Волков, В. В., Sokolova, A. V., Koch, M. H. J., & Svergun, D. I. (2003) · Journal of Applied Crystallography · doi:10.1107/s0021889803012779 · Cited by 2,850
New developments in the ATSAS program package for small-angle scattering data analysis
Petoukhov, M. V., Franke, D., Shkumatov, A. V., Tria, G., Kikhney, A., Gajda, M. J., Gorba, C., Mertens, H. D. T., Konarev, P. V., & Svergun, D. I. (2012) · Journal of Applied Crystallography · doi:10.1107/s0021889812007662 · Cited by 1,907
Molecular Chaperone Functions in Protein Folding and Proteostasis
Kim, Y., Hipp, M. S., Bracher, A., Hayer-Hartl, M. K., & Hartl, F. U. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-092442 · Cited by 1,540
Some like it hot: the structure and function of small heat-shock proteins
Haslbeck, M., Franzmann, T. M., Weinfurtner, D., & Büchner, J. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb993 · Cited by 858
A First Line of Stress Defense: Small Heat Shock Proteins and Their Function in Protein Homeostasis
Haslbeck, M., & Vierling, E. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.02.002 · Cited by 633
DOG 1.0: illustrator of protein domain structures
Ren, J., Wen, L.-P., Gao, X., Jin, C.-J., Xue, Y., & Yao, X.-B. (2009) · Cell Research · doi:10.1038/cr.2009.6 · Cited by 614
Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions
Basha, E., O’Neill, H. A., & Vierling, E. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.11.005 · Cited by 540
Protein‐Based Nanomedicine Platforms for Drug Delivery
MaHam, A., Tang, Z., Wu, H., Wang, J., & Lin, Y. (2009) · Small · doi:10.1002/smll.200801602 · Cited by 522
ATSAS 2.1 – towards automated and web-supported small-angle scattering data analysis
Petoukhov, M. V., Konarev, P. V., Kikhney, A., & Svergun, D. I. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807002853 · Cited by 452
Large Potentials of Small Heat Shock Proteins
Mymrikov, E. V., Seit‐Nebi, A. S., & Gusev, N. B. (2011) · Physiological Reviews · doi:10.1152/physrev.00023.2010 · Cited by 409
GeneSilico protein structure prediction meta-server
Kurowski, M. A. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg557 · Cited by 407
The small heat shock proteins and their role in human disease
Sun, Y., & MacRae, T. H. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04708.x · Cited by 322
Frog2: Efficient 3D conformation ensemble generator for small compounds
Miteva, M. A., Guyon, F., & Tufféry, P. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq325 · Cited by 297
Sugiyama, Y., Suzuki, A., Kishikawa, M., 阿久津, 里., Hirose, T., Waye, M. M. Y., Tsui, S. K., Yoshida, S., & Ohno, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1095 · Cited by 296
sHsps and their role in the chaperone network
Haslbeck, M. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/pl00012492 · Cited by 293
The small heat-shock protein, αb-crystallin, has a variable quaternary structure
Haley, D. A., Horwitz, J., & Stewart, P. L. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1611 · Cited by 284
Crystal Structures of α-Crystallin Domain Dimers of αB-Crystallin and Hsp20
Bagnéris, C., Bateman, O. A., Naylor, C. E., Cronin, N., Boelens, W. C., Keep, N. H., & Slingsby, C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.07.069 · Cited by 277
Aquilina, J. A., Benesch, J. L. P., Bateman, O. A., Slingsby, C., & Robinson, C. V. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1932958100 · Cited by 243
Kato, K., Goto, S., Inaguma, Y., Hasegawa, K., Morishita, R., & Asano, T. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36606-1 · Cited by 221
Jehle, S., Vollmar, B. S., Bardiaux, B., Dove, K. K., Rajagopal, P., Gonen, T., Oschkinat, H., & Klevit, R. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014656108 · Cited by 210
The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity
Hochberg, G. K. A., Ecroyd, H. W., Liu, C., Cox, D., Cascio, D., Sawaya, M. R., Collier, M. P., Stroud, J. C., Carver, J. A., Baldwin, A. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322673111 · Cited by 206
Subunit Exchange of Multimeric Protein Complexes
Sobott, F., Benesch, J. L. P., Vierling, E., & Robinson, C. V. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206060200 · Cited by 199
Self-citationα-Crystallin. The isolation and characterization of distinct macromolecular fractions
Spector, A., Li, L., Augusteyn, R. C., Schneider, A., & Freund, T. (1971) · Biochemical Journal · doi:10.1042/bj1240337 · Cited by 171
Basha, E., Lee, G. J., Breci, L. A., Hausrath, A. C., Buan, N. R., Giese, K. C., & Vierling, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310684200 · Cited by 167
Phosphorylation of αB-Crystallin Alters Chaperone Function through Loss of Dimeric Substructure
Aquilina, J. A., Benesch, J. L. P., Ding, L., Yaron, O., Horwitz, J., & Robinson, C. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403348200 · Cited by 156
α‐crystallin: a review of its structure and function
Augusteyn, R. C. (2004) · Clinical and Experimental Optometry · doi:10.1111/j.1444-0938.2004.tb03095.x · Cited by 153
The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins
Mymrikov, E. V., Daake, M., Richter, B., Haslbeck, M., & Büchner, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.760413 · Cited by 152
Ligation independent cloning vectors for expression of SUMO fusions
Weeks, S. D., Drinker, M. S., & Loll, P. J. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2006.12.006 · Cited by 141
Self-citationArrigo, A. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.05.011 · Cited by 138
Binding determinants of the small heat shock protein, αB‐crystallin: recognition of the ‘IxI’ motif
Delbecq, S. P., Jehle, S., & Klevit, R. E. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.318 · Cited by 122
Sluchanko, N. N., Beelen, S., Kulikova, A. A., Weeks, S. D., Antson, A. A., Gusev, N. B., & Strelkov, S. V. (2017) · Structure · doi:10.1016/j.str.2016.12.005 · Cited by 120
Self-citationSome properties of human small heat shock protein Hsp20 (HspB6)
Bukach, O. V., Seit‐Nebi, A. S., Marston, S. B., & Gusev, N. B. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03928.x · Cited by 118
Baranova, E. V., Weeks, S. D., Beelen, S., Bukach, O. V., Gusev, N. B., & Strelkov, S. V. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.05.024 · Cited by 115
Self-citationThe Polydispersity of αB-Crystallin Is Rationalized by an Interconverting Polyhedral Architecture
Baldwin, A. J., Lioe, H., Hilton, G. R., Baker, L. A., Rubinstein, J. L., Kay, L. E., & Benesch, J. L. P. (2011) · Structure · doi:10.1016/j.str.2011.09.015 · Cited by 110
Intermolecular Exchange and Stabilization of Recombinant Human αA- and αB-Crystallin
Sun, T., & Liang, J. J. ‐. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.286 · Cited by 104
Heterooligomeric complexes of human small heat shock proteins
Mymrikov, E. V., Seit‐Nebi, A. S., & Gusev, N. B. (2011) · Cell Stress and Chaperones · doi:10.1007/s12192-011-0296-0 · Cited by 95
Detection and Architecture of Small Heat Shock Protein Monomers
Poulain, P., Gelly, J., & Flatters, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009990 · Cited by 95
Basha, E., Jones, C., Wysocki, V. H., & Vierling, E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.074088 · Cited by 92
Chaperone Activity and Homo- and Hetero-oligomer Formation of Bacterial Small Heat Shock Proteins
Studer, S., & Narberhaus, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004701200 · Cited by 87
A Library of Protein Cage Architectures as Nanomaterials
Flenniken, M. L., Uchida, M., Liepold, L. O., Kang, S., Young, M., & Douglas, T. (2009) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-69379-6_4 · Cited by 86
Role of the Conserved SRLFDQFFG Region of α-Crystallin, a Small Heat Shock Protein
Pasta, S. Y., Raman, B., Ramakrishna, T., & Rao, C. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307523200 · Cited by 82
Aquilina, J. A., Shrestha, S., Morris, A. M., & Ecroyd, H. W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.443812 · Cited by 78
Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20)
Bukach, O. V., Glukhova, A., Seit‐Nebi, A. S., & Gusev, N. B. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.11.010 · Cited by 76
C-terminal interactions mediate the quaternary dynamics of αB-crystallin
Hilton, G. R., Hochberg, G. K. A., Laganowsky, A. D., McGinnigle, S. I., Baldwin, A. J., & Benesch, J. L. P. (2013) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2011.0405 · Cited by 74
Insights into the domains required for dimerization and assembly of human αB crystallin
Ghosh, J. G., & Clark, J. I. (2005) · Protein Science · doi:10.1110/ps.041152805 · Cited by 72
A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein Oligomers
Delbecq, S. P., Rosenbaum, J. C., & Klevit, R. E. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00490 · Cited by 71
Lermyte, F., Williams, J. P., Brown, J. M., Martin, E. M., & Sobott, F. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1124-z · Cited by 71
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den Engelsman, J., Boros, S., Dankers, P. Y. W., Kamps, B., Egberts, W. V., Böde, C., Lane, L. A., Aquilina, J. A., Benesch, J. L. P., Robinson, C. V., et al. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.08.052 · Cited by 54
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Tanguay, R. M., & Hightower, L. E. (2015) · Heat shock proteins · doi:10.1007/978-3-319-16077-1 · Cited by 40
Srinivas, P. N. B. S., Reddy, P. Y., & Reddy, G. B. (2008) · Biochemical Journal · doi:10.1042/bj20080544 · Cited by 39
Dissecting the Functional Role of the N-Terminal Domain of the Human Small Heat Shock Protein HSPB6
Heirbaut, M., Beelen, S., Strelkov, S. V., & Weeks, S. D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105892 · Cited by 36
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Clauwaert, J., Ellerton, H. D., Koretz, J. F., Thomson, K., & Augusteyn, R. C. (1989) · Current Eye Research · doi:10.3109/02713688908996387 · Cited by 23
Heirbaut, M., Lermyte, F., Martin, E. M., Beelen, S., Verschueren, T., Sobott, F., Strelkov, S. V., & Weeks, S. D. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.10.002 · Cited by 23
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Heirbaut, M., Strelkov, S. V., & Weeks, S. D. (2015) · Heat shock proteins · doi:10.1007/978-3-319-16077-1_8 · Cited by 7
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Sluzala, Z. B., Hamati, A., & Fort, P. E. (2025) · Cells · doi:10.3390/cells14020127 · Cited by 16
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Jovcevski, B., Aquilina, J. A., Benesch, J. L. P., & Ecroyd, H. W. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-018-0889-y · Cited by 9
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Almutairi, B. O., Almutairi, M. H., Alrefaei, A. F., Alkahtani, S. H., & Alarifi, S. A. (2023) · Medicina · doi:10.3390/medicina59050996 · Cited by 6
Gliniewicz, E. F., Chambers, K. M., Leon, E. R. D., Sibai, D., Campbell, H. C., & McMenimen, K. A. (2019) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25662 · Cited by 4
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Metadata
- Authors
- Heirbaut, M., Lermyte, F., Martin, E. M., Beelen, S., Sobott, F., Strelkov, S. V., & Weeks, S. D.
- Affiliations
- KU Leuven (BE)
- University of Antwerp (BE)
- University of Leeds (GB)
- Corresponding author
- Strelkov, Sergei V.
- Weeks, Stephen D.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 292
- Issue
- 24
- Pages
- 9944-9957
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC5473246
- OpenAlex
- W2613815235
- Cited by
- 28
- References
- 61
- Citations by year
- 2026: 2 · 2025: 3 · 2023: 5 · 2022: 2 · 2021: 2 · 2020: 7 · 2019: 3 · 2018: 4
- FWCI
- 1.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (submittedVersion)
- Lirias (submittedVersion, other-oa)
- Funders
- Fonds Wetenschappelijk Onderzoek (G093615N, WO03315N, 11L4115N)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- small heat shock proteins, HSPB6, HSPB1, hetero-oligomerization, N-terminal domain, intrinsically disordered regions, heterodimer, molecular chaperones, oligomer assembly, subunit exchange, oligomer size, skeletal muscle, proteostasis
- MeSH terms
- Cross-Linking Reagents, Heat-Shock Proteins, Humans, Models, Molecular, Nitrogen Isotopes, Peptide Fragments, Protein Conformation, Recombinant Fusion Proteins, Recombinant Proteins, Sulfhydryl Reagents, Mutagenesis, Site-Directed, Conserved Sequence, Gene Deletion, Point Mutation, Molecular Chaperones, Dimerization, Amino Acid Substitution, Amino Acid Motifs, HSP20 Heat-Shock Proteins, Scattering, Small Angle, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Stability, HSP27 Heat-Shock Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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