Small heat shock protein Hsp20 (HspB6) as a partner of 14-3-3gamma.
Interaction of human 14-3-3gamma with the small heat shock protein Hsp20 was analyzed by means of size-exclusion chromatography and chemical crosslinking. Unphosphorylated Hsp20 and its mutant S16D mimicking phosphorylation by cAMP-dependent protein kinase did not interact with 14-3-3. Phosphorylated Hsp20 formed a tight complex with 14-3-3 in which dimer of 14-3-3 was bound to dimer of Hsp20. 14-3-3 did not affect the chaperone activity of unphosphorylated Hsp20 but increased the chaperone activity of phosphorylated Hsp20 if insulin was used as a model substrate. Estimation of the effect of 14-3-3 on the chaperone activity of Hsp20 with other model substrates was complicated by the fact that under in vitro conditions isolated 14-3-3 possessed its own high chaperone activity. Taken into account high content of Hsp20 in different muscles it is supposed that upon phosphorylation Hsp20 might effectively compete with multiple protein targets of 14-3-3 and by this means indirectly affect many intracellular processes.
Chernik
Ivan S
IS
Department of Biochemistry, School of Biology, Moscow State University, Moscow, 119992, Russia.
Seit-Nebi
Alim S
AS
Marston
Steven B
SB
Gusev
Nikolai B
NB
D048948:14-3-3 Proteins / Q000378:metabolism*; D020134:Catalytic Domain / Q000187:drug effects; D002850:Chromatography, Gel; D003432:Cross-Linking Reagents / Q000494:pharmacology; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D050886:HSP20 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D007328:Insulin / Q000378:metabolism; D008970:Molecular Weight; D010766:Phosphorylation / Q000187:drug effects; D011485:Protein Binding / Q000187:drug effects; D020836:Protein Structure, Quaternary / Q000187:drug effects
D048948:14-3-3 Proteins; D003432:Cross-Linking Reagents; D050886:HSP20 Heat-Shock Proteins; D007328:Insulin; D017868:Cyclic AMP-Dependent Protein Kinases