Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies.

ABSTRACT: Neurodegeneration, a result of multiple dysregulatory events, is a lengthy multistep process manifested by accrual of mutant variants and abnormal expression, posttranslational modification, and processing of certain proteins. Accumulation of these dysregulated processes requires a mechanism that maintains their functional stability and allows the evolution of the neurodegenerative phenotype. In malignant cells, the capacity to buffer transformation has been attributed to heat-shock protein 90 (Hsp90). Although normal proteins seem to require limited assistance from the chaperone, their aberrant counterparts seem to be highly dependent on Hsp90. Whereas enhanced Hsp90 affinity for mutated or functionally deregulated client proteins has been observed for several oncoproteins, it is unknown

SUBMITTER: Luo W 

PROVIDER: S-EPMC1890525 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature