Molecular characterization of rat cvHsp/HspB7 in vitro and its dynamic molecular architecture

Yang, Zehong; Wang, Yao; Lu, Yongzhi; Wang, Chao

doi:10.3892/mmr.2010.382

Cited by 3 publications

(1 citation statement)

References 25 publications

(26 reference statements)

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“…Therefore, hspb12 may play a supporting role in KV cilia function (Figure 8A), which is primarily revealed when hspb7 is reduced. Hspb7 forms homo-multimers with up to 12 subunits (Yang et al, 2011), and it interacts with at least one other sHsp, Hspb8 (Sun et al, 2004). Hspb7-Hspb12 binding has not been studied because mammals lack hspb12 , but they are plausible binding partners due to the homology of the α-crystallin domains.…”

Section: Discussionmentioning

confidence: 99%

Small heat shock proteins are necessary for heart migration and laterality determination in zebrafish

Lahvic

Marin

et al. 2013

Developmental Biology

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Small heat shock proteins (sHsps) regulate cellular functions not only under stress, but also during normal development, when they are expressed in organ-specific patterns. Here we demonstrate that two small heat shock proteins expressed in embryonic zebrafish heart, hspb7 and hspb12, have roles in the development of left-right asymmetry. In zebrafish, laterality is determined by the motility of cilia in Kupffer’s vesicle (KV), where hspb7 is expressed; knockdown of hspb7 causes laterality defects by disrupting the motility of these cilia. In embryos with reduced hspb7, the axonemes of KV cilia have a 9+0 structure, while control embyros have a predominately 9+2 structure. Reduction of either hspb7 or hspb12 alters the expression pattern of genes that propagate the signals that establish left-right asymmetry: the nodal-related gene southpaw (spaw) in the lateral plate mesoderm, and its downstream targets pitx2, lefty1 and lefty2. Partial depletion of hspb7 causes concordant heart, brain and visceral laterality defects, indicating that loss of KV cilia motility leads causes coordinated but randomized laterality. Reducing hspb12 leads to similar alterations in the expression of downstream laterality genes, but at a lower penetrance. Simultaneous reduction of hspb7 and hspb12 randomizes heart, brain and visceral laterality, suggesting that these two genes have partially redundant functions in the establishment of left-right asymmetry. In addition, both hspb7 and hspb12 are expressed in the precardiac mesoderm and in the yolk syncytial layer, which supports the migration and fusion of mesodermal cardiac precursors. In embryos in which the reduction of hspb7 or hspb12 was limited to the yolk, migration defects predominated, suggesting that the yolk expression of these genes rather than heart expression is responsible for the migration defects.

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Section: Discussionmentioning

confidence: 99%

Small heat shock proteins are necessary for heart migration and laterality determination in zebrafish

Lahvic

Marin

et al. 2013

Developmental Biology

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Cardio-Vascular Heat Shock Protein (cvHsp, HspB7), an Unusual Representative of Small Heat Shock Protein Family

Muranova

Shatov

Bukach

et al. 2021

Biochemistry Moscow

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Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases

Tedesco

Cristofani

Ferrari

et al. 2022

Front. Mol. Biosci.

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The family of the human small Heat Shock Proteins (HSPBs) consists of ten members of chaperones (HSPB1-HSPB10), characterized by a low molecular weight and capable of dimerization and oligomerization forming large homo- or hetero-complexes. All HSPBs possess a highly conserved centrally located α-crystallin domain and poorly conserved N- and C-terminal domains. The main feature of HSPBs is to exert cytoprotective functions by preserving proteostasis, assuring the structural maintenance of the cytoskeleton and acting in response to cellular stresses and apoptosis. HSPBs take part in cell homeostasis by acting as holdases, which is the ability to interact with a substrate preventing its aggregation. In addition, HSPBs cooperate in substrates refolding driven by other chaperones or, alternatively, promote substrate routing to degradation. Notably, while some HSPBs are ubiquitously expressed, others show peculiar tissue-specific expression. Cardiac muscle, skeletal muscle and neurons show high expression levels for a wide variety of HSPBs. Indeed, most of the mutations identified in HSPBs are associated to cardiomyopathies, myopathies, and motor neuropathies. Instead, mutations in HSPB4 and HSPB5, which are also expressed in lens, have been associated with cataract. Mutations of HSPBs family members encompass base substitutions, insertions, and deletions, resulting in single amino acid substitutions or in the generation of truncated or elongated proteins. This review will provide an updated overview of disease-related mutations in HSPBs focusing on the structural and biochemical effects of mutations and their functional consequences.

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Molecular characterization of rat cvHsp/HspB7 in vitro and its dynamic molecular architecture

Cited by 3 publications

References 25 publications

Small heat shock proteins are necessary for heart migration and laterality determination in zebrafish

Small heat shock proteins are necessary for heart migration and laterality determination in zebrafish

Cardio-Vascular Heat Shock Protein (cvHsp, HspB7), an Unusual Representative of Small Heat Shock Protein Family

Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases

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