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these findings reveal a new regulatory mechanism of HSPB6 in cell survival through its interaction with BECN1.
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Structural basis for the interaction of a human HSPB6 protein with the 14-3-3 universal signaling regulator has been reported.
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Data suggest that HSPB6 forms hetero-oligomers with HSPB1 under the following rules: (1) highly conserved motif RLFDQXFG is necessary for subunit exchange among oligomers, (2) a site about 20 residues downstream of this motif determines size of resultant hetero-oligomers, and (3) a region in the N-terminal domain that is unique to HSPB6 dictates preferential formation of heterodimers. (HSP = heat shock protein)
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findings strongly suggest that phosphorylated HSP20 inhibits TGF-alpha-induced HCC cell migration and invasion via suppression of the JNK signaling pathway
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multiple sclerosis lesions revealed exclusive induction of HSPB6 in astrocytes, as confirmed by co-localization of HSPB6 with GFAP.
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N-terminal mutations increase stability of large HspB1 homooligomers, prevent their phosphorylation-dependent dissociation, modulate their interaction with HspB6 and decrease their chaperoning capacity, preventing normal functioning of HspB1.
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Findings strongly suggest that HSP20 directly associates with Bax and stimulates caspase cascade in human hepatocellular carcinoma cells.
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Data suggest that heat shock protein 20 (HSP20) may have value as a prognostic tumor marker and its overexpression might be a novel strategy for colorectal cancer (CRC) therapy.
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peptides in heat-shock protein Hsp20 (G71HFSVLLDVKHFSPEEIAVK91) and Hsp27 (D93RWRVSLDVNHFAPDELTVK113) with sequence homology to alpha-crystallin also have robust chaperone and anti-apoptotic activities.
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These findings strongly suggest that HSP20 might decrease the IKK-alpha protein level and that it down-regulates the TNF-alpha-stimulated intracellular signaling in HCC, thus resulting in the suppression of HCC progression.
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HSP20 may play a protective role against the progression of ovarian cancer.
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HSP20 directly associates with PI3K subunits and suppresses its activity in hepatocellular carcinoma, resulting in the inhibition of the AKT pathway, and subsequently decreasing the growth of hepatocellular carcinoma.
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14-3-3zeta and possibly other 14-3-3 isoforms may have additional functional roles conducted by the monomeric state
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the cytosolic protein AKAP-Lbc (AKAP13) as the anchoring protein responsible for directing PKA phosphorylation of Hsp20 on Ser(16)
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Hsp20 serves as a novel cardiokine in regulating myocardial angiogenesis through activation of the VEGFR signaling cascade.
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cofilins 1 and 2 only weakly interact with 14-3-3 and therefore cannot directly compete with phosphorylated small heat shock protein HspB6 for its binding to 14-3-3
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Properties of the monomeric form of 14-3-3zeta protein and its interaction with tau and HspB6. This interaction requires phosphorylation of tau protein and HspB6.
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A potential molecular mechanism by which Hsp20 acetylation can affect myometrial activity by liberating cofilin
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Overexpression of HSPB1, as well as HSPB6, HSPB7 and HSPB8 independently protect against tachycardia remodeling by attenuation of the RhoA GTPase pathway at different levels.
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Nevertheless, in solution, both alpha-crystallin domain proteins form stable dimers via the symmetric antiparallel interaction of beta7 strands.
