Chapter title |
Plant Proteostasis
|
---|---|
Chapter number | 18 |
Book title |
Plant Proteostasis
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3759-2_18 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3757-8, 978-1-4939-3759-2
|
Authors |
Farmaki, T, T. Farmaki |
Editors |
L. Maria Lois, Rune Matthiesen |
Abstract |
Protein functionality depends directly on its accurately defined three-dimensional organization, correct and efficient posttranslational modification, and transport. However, proteins are continuously under a hostile environment threatening with folding aberrations, aggregation, and mistargeting. Therefore, proteins must be constantly "followed up" by a tightly regulated homeostatic mechanism specifically known as proteostasis. To this end other proteins ensure this close surveillance including chaperones as well as structural and functional members of the proteolytic mechanisms, mainly the autophagy and the proteasome related. They accomplish their action via interactions not only with other proteins but also with lipids as well as cytoskeletal components. We describe a protocol based on an affinity chromatographic approach aiming at the isolation of phosphatidyl inositol phosphate binding proteins, a procedure which results into the enrichment and purification of several members of the proteostasis mechanism, e.g. autophagy and proteasome, among other components of the cell signaling pathways. |
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
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Unknown | 4 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 1 | 25% |
Researcher | 1 | 25% |
Other | 1 | 25% |
Lecturer > Senior Lecturer | 1 | 25% |
Readers by discipline | Count | As % |
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Biochemistry, Genetics and Molecular Biology | 3 | 75% |
Medicine and Dentistry | 1 | 25% |