A growing body of evidence indicates that sHSPs confer stress
protection by preventing cytoskeleton aggregation. How these
small proteins afford protection at the molecular level still remains
uncertain. There is evidence, however, that their cytoprotective
functions may be due to their ability to interact with IF polymers
and IF subunits. In support of this hypothesis, mutations that affect
the ability of various sHSPs to interact with cytoskeleton proteins
have been found to lead to similar pathological disorders, and phenotypes,
as those due to mutations in a number of cytoskeleton
components. Abnormal cytoskeleton assembly may also involve
sHSPs and cytoskeleton components in other pathological conditions,
including the EMT process found in fibrosis and cancer,
opening the way for novel therapeutic opportunities.