HELPING HANDS

Beschreibung

Only properly folded proteins are able to full their function, therefore it is crucial for every cell to ensure successful folding of its proteins. Misfolding of proteins has dramatic consequences for cell and organism: fatal diseases such as cancer, cystic brosis, Alzheimer's disease and the Creutzfeldt-Jakob disease originate from aberrations in protein folding. Members of distinct families of evolutionary conserved molecular chaperones assist client proteins on their folding pathways. One of the most prominent chaperone families, which are conserved from bacteria to mammals, is the Hsp90 class. Hsp90 assists folding of proteins involved in cell signalling, many of which are protein kinases. Hsp90 functions in complex with co-chaperones, some of which control the substrate speci_city of this chaperone machinery. Unravelling the molecular mechanism of Hsp90 machinery and the role of its cohort of co-chaperones is of major importance. Kinases undergo activation and deactivation by phosphorylation to rule vital processes such as cell division. Strict regulation of their activity is necessary for proper signalling. More than 100 kinases have been identi ed to require Hsp90 for their folding. During their active cycle they undergo structural changes, which may inuence their stability. Do kinases therefore have a stability problem and in particular rely on the molecular chaperone Hsp90? Chapter 1 provides an overview of the current knowledge and questions regarding Hsp90's relationship to kinases and co chaperones.

Autor*in

Sandra Kling

Themen in »HELPING HANDS«

cellfree protein synthesis protein folding ATPase cycle Hsp90 Hsp90-p50Cdc37-complex cochaperone kinase p50Cdc37 protein aggregation protein stability rotein insolubility

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