Literature DB >> 23684648

Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an update.

André-Patrick Arrigo1.   

Abstract

Small heat shock proteins (sHsps) regulate a large number of fundamental cellular processes and are involved in many pathological diseases. They share complex oligomerization and phosphorylation properties allowing them to interact and modulate the activity of many client proteins. Here, the up-to date protein interactome of the ten human sHsps is presented as an illustration of their multiple cellular functions. In addition of forming homo-oligomers, some of these proteins interact whith each other and form hetero-oligomeric complexes that could bear new protein targets recognition abilities. Here, novel informations are presented on how the formation of HspB1/HspB5 complex can stimulate the activity of the oxidoresistance promoting enzyme glucose 6-phosphate dehydrogenase through its interaction with newly formed highly phosphorylated HspB1 homo-oligomers.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2013        PMID: 23684648     DOI: 10.1016/j.febslet.2013.05.011

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  50 in total

1.  Regulation of small heat-shock proteins by hetero-oligomer formation.

Authors:  Evgeny V Mymrikov; Mareike Riedl; Carsten Peters; Sevil Weinkauf; Martin Haslbeck; Johannes Buchner
Journal:  J Biol Chem       Date:  2019-11-25       Impact factor: 5.157

Review 2.  Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell.

Authors:  André-Patrick Arrigo
Journal:  Cell Stress Chaperones       Date:  2017-01-31       Impact factor: 3.667

3.  Structure and properties of chimeric small heat shock proteins containing yellow fluorescent protein attached to their C-terminal ends.

Authors:  Petr N Datskevich; Nikolai B Gusev
Journal:  Cell Stress Chaperones       Date:  2013-11-27       Impact factor: 3.667

Review 4.  A first line of stress defense: small heat shock proteins and their function in protein homeostasis.

Authors:  Martin Haslbeck; Elizabeth Vierling
Journal:  J Mol Biol       Date:  2015-02-10       Impact factor: 5.469

5.  Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1.

Authors:  Michelle Heirbaut; Frederik Lermyte; Esther M Martin; Steven Beelen; Frank Sobott; Sergei V Strelkov; Stephen D Weeks
Journal:  J Biol Chem       Date:  2017-05-09       Impact factor: 5.157

Review 6.  Small heat shock proteins: Simplicity meets complexity.

Authors:  Martin Haslbeck; Sevil Weinkauf; Johannes Buchner
Journal:  J Biol Chem       Date:  2018-10-31       Impact factor: 5.157

7.  It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate.

Authors:  Indu Santhanagopalan; Matteo T Degiacomi; Dale A Shepherd; Georg K A Hochberg; Justin L P Benesch; Elizabeth Vierling
Journal:  J Biol Chem       Date:  2018-10-22       Impact factor: 5.157

Review 8.  The BAG3-dependent and -independent roles of cardiac small heat shock proteins.

Authors:  Xi Fang; Julius Bogomolovas; Christa Trexler; Ju Chen
Journal:  JCI Insight       Date:  2019-02-21

9.  Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1.

Authors:  Anna S Chalova; Maria V Sudnitsyna; Pavel I Semenyuk; Victor N Orlov; Nikolai B Gusev
Journal:  Cell Stress Chaperones       Date:  2014-06-05       Impact factor: 3.667

Review 10.  Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells.

Authors:  Christine Slingsby; Graeme J Wistow
Journal:  Prog Biophys Mol Biol       Date:  2014-02-28       Impact factor: 3.667

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