Structure, properties, and functions of the human small heat-shock protein HSP22 (HspB8, H11, E2IG1)

A critical review

Anton Shemetov, Alim S. Seit-Nebi, Nikolai B. Gusev

Research output: Contribution to journalShort survey

48 Citations (Scopus)

Abstract

The recently described human HSP22 belongs to the superfamily of small heat-shock proteins containing a conservative α-crystallin domain. HSP22 seems to be involved in regulation of cell proliferation, cardiac hypertrophy, apoptosis, and carcinogenesis, and expression of point mutants of HSP22 correlates with development of different neuromuscular diseases. Therefore, an investigation of the structure and properties of HSP22 is desirable for understanding its multiple functions. HSP22 seems to belong to the group of so-called intrinsically disordered proteins and possesses a highly flexible structure. HSP22 tends to form small-molecular-mass oligomers and interacts with biological membranes and many different proteins, among them glycolytic enzymes and different protein kinases. HSP22 possesses chaperonelike activity and prevents aggregation of denatured proteins both in vitro and in vivo. Depending on the cell type and its expression, HSP22 might have either pro- or anti-apoptotic effects. Chaperonelike activity seems to be important for anti-apoptotic effects, whereas interaction with and regulation of certain protein kinases might be important for the pro-apoptotic effects of HSP22. Expression of K141N or K141E mutants of HSP22 correlates with development of distal hereditary motor neuropathy and/or Charcot-Marie-Tooth disease. These mutations destabilize the structure of HSP22, affect its interaction with other small heat-shock proteins, and decrease its chaperonelike activity. HSP22 decreases or prevents aggregation of Huntingtin fragments and amyloid-β peptide 1-40 of the Dutch type. Thus, HSP22 seems to play an important role in the nervous system, and further investigations are needed to understand the molecular mechanisms of its functioning.

Original languageEnglish (US)
Pages (from-to)264-269
Number of pages6
JournalJournal of Neuroscience Research
Volume86
Issue number2
DOIs
StatePublished - Feb 1 2008
Externally publishedYes

Fingerprint

Small Heat-Shock Proteins
Protein Kinases
Intrinsically Disordered Proteins
Charcot-Marie-Tooth Disease
Neuromuscular Diseases
Crystallins
Peptide Fragments
Cardiomegaly
Amyloid
Nervous System
Carcinogenesis
Proteins
Cell Proliferation
Apoptosis
Mutation
Membranes
Enzymes
In Vitro Techniques

Keywords

  • Congenital diseases
  • Phosphorylation
  • Small heat-shock proteins

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience

Cite this

Structure, properties, and functions of the human small heat-shock protein HSP22 (HspB8, H11, E2IG1) : A critical review. / Shemetov, Anton; Seit-Nebi, Alim S.; Gusev, Nikolai B.

In: Journal of Neuroscience Research, Vol. 86, No. 2, 01.02.2008, p. 264-269.

Research output: Contribution to journalShort survey

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