Protein folding in the cytoplasm and the heat shock response.
Proteins generally must fold into precise three-dimensional conformations to fulfill their biological functions. In the cell, this fundamental process is aided by molecular chaperones, which act in preventing protein misfolding and aggregation. How this machinery assists newly synthesized polypeptide chains in navigating the complex folding energy landscape is now being understood in considerable detail. The mechanisms that ensure the maintenance of a functional proteome under normal and stress conditions are also of great medical relevance, as the aggregation of proteins that escape the cellular quality control underlies a range of debilitating diseases, including many age-of-onset neurodegenerative disorders.
Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
R Martin
RM
Vabulas
Swasti
S
Raychaudhuri
Manajit
M
Hayer-Hartl
F Ulrich
FU
Hartl
D003593:Cytoplasm / Q000378:metabolism*; D005786:Gene Expression Regulation / Q000502:physiology; D018869:Heat-Shock Response / Q000235:genetics / Q000502:physiology*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*; D013312:Stress, Physiological / Q000502:physiology
D018832:Molecular Chaperones; D011506:Proteins