Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an update.
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TLDR
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.About:
This article is published in FEBS Letters.The article was published on 2013-06-27 and is currently open access. It has received 124 citations till now. The article focuses on the topics: Heat shock protein & Interactome.read more
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A first line of stress defense: small heat shock proteins and their function in protein homeostasis.
TL;DR: Small heat shock proteins (sHsps) are virtually ubiquitous molecular chaperones that can prevent the irreversible aggregation of denaturing proteins and have evolved independently in metazoans, plants and fungi.
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Insect Heat Shock Proteins During Stress and Diapause
Allison M. King,Thomas H. MacRae +1 more
TL;DR: Heat shock proteins are synthesized constitutively in insects and induced by stressors such as heat, cold, crowding, and anoxia, and undergo differential regulation without the general disruption of protein production in diapause.
Journal ArticleDOI
Small heat shock proteins: Role in cellular functions and pathology.
TL;DR: A "dynamic partitioning hypothesis" is proposed for the promiscuous interactions and pleotropic functions exhibited by sHsps, which exhibit a robust anti-apoptotic property, involving several stages of mitochondrial-mediated, extrinsic apoptotic as well as pro-survival pathways.
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Gene Expression Is Circular: Factors for mRNA Degradation Also Foster mRNA Synthesis
Gal Haimovich,Daniel A. Medina,Sebastien Causse,Manuel Garber,Gonzalo Millán-Zambrano,Oren Barkai,Sebastián Chávez,José E. Pérez-Ortín,Xavier Darzacq,Mordechai Choder +9 more
TL;DR: It is demonstrated that most yeast mRNAs are degraded by the cytoplasmic 5'-to-3' pathway (the "decaysome"), as proposed previously, and the level of these m RNAs is highly robust to perturbations in this major pathway because defects in various decaysome components lead to transcription downregulation.
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Small heat shock proteins: Simplicity meets complexity.
TL;DR: New roles and new cofactors, as well as variations in structure and regulation of sHsps, have emerged, and current evidence suggests that smaller oligomers are more active chaperones.
References
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A human protein-protein interaction network : a resource for annotating the proteome
Ulrich Stelzl,Uwe Worm,Maciej Lalowski,Christian Haenig,Felix H. Brembeck,Heike Goehler,Martin Stroedicke,Martina Zenkner,Anke Schoenherr,Susanne Koeppen,Jan Timm,Sascha Mintzlaff,Claudia Abraham,Nicole Bock,Silvia Kietzmann,Astrid Goedde,Engin Toksöz,Anja Droege,Sylvia Krobitsch,Bernhard Korn,Walter Birchmeier,Hans Lehrach,Erich E. Wanker +22 more
TL;DR: A large, highly connected network of interacting pairs of human proteins was identified, characterizing ANP32A and CRMP1 as modulators of Wnt signaling and two novel Axin-1 interactions were validated experimentally.
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Alpha-crystallin can function as a molecular chaperone
TL;DR: It is shown that alpha-crystallin refracts light and protects proteins from aggregation in the transparent eye lens and that in nonlens cells alpha-Crystallin may have other functions in addition to its capacity to suppress aggregation of proteins.
Book
The Biology of heat shock proteins and molecular chaperones.
TL;DR: McClintock et al. as mentioned in this paper described the role of heat shock proteins as proteases or unfolded polypeptide-binding proteins in the regulation of the heat shock response in eukaryotic organisms.
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Small heat shock proteins are molecular chaperones
TL;DR: It is shown that all sHsps investigated act as molecular chaperones in these folding reactions and at stoichiometric amounts they maximally prevent the aggregation of citrate synthase and alpha-glucosidase under heat shock conditions and stabilize the proteins.
Journal ArticleDOI
A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy.
Patrick Vicart,Patrick Vicart,Anne Caron,Pascale Guicheney,Zhenlin Li,Zhenlin Li,Marie-Christine Prévost,Armelle Faure,Danielle Chateau,Françoise Chapon,Fernando M.S. Tomé,Jean-Marie Dupret,Denise Paulin,Denise Paulin,Michel Fardeau +14 more
TL;DR: These results are the first to identify a defect in a molecular chaperone as a cause for an inherited human muscle disorder, and an R120G missense mutation in CRYAB that co-segregates with the disease phenotype in this family.