Figures & data
Table I. HspB1 interactome.
Table II. HspB5 interactome.
Table III. HspB8 interactome.
![Figure 2. Native size and phosphorylation of HspB1 and structure-specific interaction with client protein targets. HeLa cells were lysed and the 10 000 × g cytosolic fraction containing all the cellular content of HspB1 was analysed by gel filtration column as previously described [Citation27]. Immunoblot analysis of two-by-two pooled fractions was performed using antibodies that are specific to either total HspB1 or phosphorylated (phospho-Ser15, phospho-Ser78 or phospho-Ser82) HspB1. The presence of three client proteins that interact with HspB1 was detected using specific antibodies recognising Pro-caspase-3, HDAC6 and STAT2. Three native size fractions could be defined depending on HspB1 phosphorylation: 50–200 kDa, phosphorylation at the level of serines 15 and 82, 200–400 kDa, phosphorylation at the level of serine 78 and 400–700 kDa oligomers containing phosphorylated serine 82. Note that pro-caspase-3 co-eluted mainly with the serine 15 phosphorylated small oligomers. HDAC6 was at the level of the large serine 82 phosphorylated oligomers while STAT2 had a less defined elution profile between the medium and large sized oligomers. Interactions of these proteins with different phospho-oligomeric structures of HspB1 was confirmed by co-immunoprecipitation [Citation44].](/cms/asset/375c23d3-279a-4314-b429-82b606ff3108/ihyt_a_792956_f0002_b.jpg)