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KMID : 0613820070170121760
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Journal of Life Science
2007 Volume.17 No. 12 p.1760 ~ p.1765
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Family of Hsp70 Molecular Chaperones and Their Regulators
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Chung Kyung-Tae
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Abstract
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Proteins are involved in promoting or controlling virtually every event on which our lives depend. Proteins are synthesized in cytosol and in the endoplasmic reticulum where their synthesis machinery are tightly controlled. However, not all of newly synthesized proteins are survived and conduct their essential functions to maintain cell’s lives. It was reported that one-third of synthesized proteins are rapidly destroyed by proteasome under the most physiological conditions. Full-length translated proteins, which survived, must undergo proper folding and assemble process. Some proteins are spontaneously folded while others require molecular chaperones and folding enzymes to be properly folded. Molecular chaperones are ubiquitously present within the subcellular organelles and from bacteria to animals and plants. Among those members of Hsp70 family have been extensively studied and their regulators have been discovered in the last decade. Here, a brief overview is presented for functional mechanism of Hsp70 homologues and the roles of their regulators. Since biological function of Hsp70 family other than chaperonic function are expending the review would give basic understanding of partnership between Hsp70 family and their regulators.
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KEYWORD
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Protein synthesis, molecular chaperones, Hsp70, BiP, cofactors
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