Phosphorylation by cyclic AMP-dependent protein kinase inhibits chaperone-like activity of human HSP22 in vitro

Anton Shemetov, A. S. Seit-Nebi, O. V. Bukach, N. B. Gusev

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is effectively phosphorylated by cAMP-dependent protein kinase in vitro. Mutation S24D did not affect, whereas mutations S57D or S24,57D prevented phosphorylation of HSP22 by cAMP-dependent protein kinase thus indicating that Ser57 is the primary site of phosphorylation. Phosphorylation (or mutation) of Ser57 (or Ser24 and Ser57) resulted in changes of the local environment of tryptophan residues and increased HSP22 sus-ceptibility to chymotrypsinolysis. Mutations mimicking phosphorylation decreased dissociation of HSP22 oligomer at low concentration without affecting its quaternary structure at high protein concentration. Mutations S24D, S57D, and especially S24,57D were accompanied by decrease of chaperone-like activity of HSP22 if insulin and rhodanase were used as substrates. Thus, phosphorylation by cAMP-dependent protein kinase affects the structure and decreases chaperone-like activity of HSP22 in vitro.

Original languageEnglish (US)
Pages (from-to)200-208
Number of pages9
JournalBiochemistry (Moscow)
Volume73
Issue number2
DOIs
StatePublished - Feb 1 2008
Externally publishedYes

Fingerprint

Phosphorylation
Cyclic AMP-Dependent Protein Kinases
Human Activities
Mutation
Small Heat-Shock Proteins
Consensus Sequence
Molecular mass
Oligomers
Tryptophan
In Vitro Techniques
Insulin
Substrates
Proteins

Keywords

  • Chaperone-like activity
  • Phosphorylation
  • Small heat shock proteins
  • Structure

ASJC Scopus subject areas

  • Biochemistry

Cite this

Phosphorylation by cyclic AMP-dependent protein kinase inhibits chaperone-like activity of human HSP22 in vitro. / Shemetov, Anton; Seit-Nebi, A. S.; Bukach, O. V.; Gusev, N. B.

In: Biochemistry (Moscow), Vol. 73, No. 2, 01.02.2008, p. 200-208.

Research output: Contribution to journalArticle

@article{c2f8a2d0aebd4ba9b07804f1ae48cf1a,
title = "Phosphorylation by cyclic AMP-dependent protein kinase inhibits chaperone-like activity of human HSP22 in vitro",
abstract = "Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is effectively phosphorylated by cAMP-dependent protein kinase in vitro. Mutation S24D did not affect, whereas mutations S57D or S24,57D prevented phosphorylation of HSP22 by cAMP-dependent protein kinase thus indicating that Ser57 is the primary site of phosphorylation. Phosphorylation (or mutation) of Ser57 (or Ser24 and Ser57) resulted in changes of the local environment of tryptophan residues and increased HSP22 sus-ceptibility to chymotrypsinolysis. Mutations mimicking phosphorylation decreased dissociation of HSP22 oligomer at low concentration without affecting its quaternary structure at high protein concentration. Mutations S24D, S57D, and especially S24,57D were accompanied by decrease of chaperone-like activity of HSP22 if insulin and rhodanase were used as substrates. Thus, phosphorylation by cAMP-dependent protein kinase affects the structure and decreases chaperone-like activity of HSP22 in vitro.",
keywords = "Chaperone-like activity, Phosphorylation, Small heat shock proteins, Structure",
author = "Anton Shemetov and Seit-Nebi, {A. S.} and Bukach, {O. V.} and Gusev, {N. B.}",
year = "2008",
month = "2",
day = "1",
doi = "10.1007/s10541-008-2012-y",
language = "English (US)",
volume = "73",
pages = "200--208",
journal = "Biochemistry. Biokhimiia",
issn = "0006-2979",
publisher = "Maik Nauka-Interperiodica Publishing",
number = "2",

}

TY - JOUR

T1 - Phosphorylation by cyclic AMP-dependent protein kinase inhibits chaperone-like activity of human HSP22 in vitro

AU - Shemetov, Anton

AU - Seit-Nebi, A. S.

AU - Bukach, O. V.

AU - Gusev, N. B.

PY - 2008/2/1

Y1 - 2008/2/1

N2 - Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is effectively phosphorylated by cAMP-dependent protein kinase in vitro. Mutation S24D did not affect, whereas mutations S57D or S24,57D prevented phosphorylation of HSP22 by cAMP-dependent protein kinase thus indicating that Ser57 is the primary site of phosphorylation. Phosphorylation (or mutation) of Ser57 (or Ser24 and Ser57) resulted in changes of the local environment of tryptophan residues and increased HSP22 sus-ceptibility to chymotrypsinolysis. Mutations mimicking phosphorylation decreased dissociation of HSP22 oligomer at low concentration without affecting its quaternary structure at high protein concentration. Mutations S24D, S57D, and especially S24,57D were accompanied by decrease of chaperone-like activity of HSP22 if insulin and rhodanase were used as substrates. Thus, phosphorylation by cAMP-dependent protein kinase affects the structure and decreases chaperone-like activity of HSP22 in vitro.

AB - Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is effectively phosphorylated by cAMP-dependent protein kinase in vitro. Mutation S24D did not affect, whereas mutations S57D or S24,57D prevented phosphorylation of HSP22 by cAMP-dependent protein kinase thus indicating that Ser57 is the primary site of phosphorylation. Phosphorylation (or mutation) of Ser57 (or Ser24 and Ser57) resulted in changes of the local environment of tryptophan residues and increased HSP22 sus-ceptibility to chymotrypsinolysis. Mutations mimicking phosphorylation decreased dissociation of HSP22 oligomer at low concentration without affecting its quaternary structure at high protein concentration. Mutations S24D, S57D, and especially S24,57D were accompanied by decrease of chaperone-like activity of HSP22 if insulin and rhodanase were used as substrates. Thus, phosphorylation by cAMP-dependent protein kinase affects the structure and decreases chaperone-like activity of HSP22 in vitro.

KW - Chaperone-like activity

KW - Phosphorylation

KW - Small heat shock proteins

KW - Structure

UR - http://www.scopus.com/inward/record.url?scp=40649120772&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=40649120772&partnerID=8YFLogxK

U2 - 10.1007/s10541-008-2012-y

DO - 10.1007/s10541-008-2012-y

M3 - Article

C2 - 18298377

AN - SCOPUS:40649120772

VL - 73

SP - 200

EP - 208

JO - Biochemistry. Biokhimiia

JF - Biochemistry. Biokhimiia

SN - 0006-2979

IS - 2

ER -