The ubiquitin molecule within all living cells<\/figcaption><\/figure>\nThroughout the \u201870s and \u201880s, Distinguished Professors Avram Hershko and Aaron Ciechanover unveiled the mysteries of \u00a0the ubiquitin system, revealing some masterkeys of human health. The ubiquitous protein ubiquitin, they showed, is the key factor in deciding when and how a cell should regenerate. Imbalance in ubiquitin reveals itself in some of the world\u2019s most incurable afflictions \u2013 such as cancer and neuro-degenerative disorders.<\/p>\n
By 2004, the Technion research was already revolutionizing medical understanding and opening the way to innovative cures and treatments. No wonder that, in that year, the two Technion Professors became Israel\u2019s first Nobel Laureates in science.<\/p>\n
<\/h2>\nThe Ubiquitin Story<\/h2>\n
In 1975, a protein of unknown function was identified by Dr. Gideon Goldstein which he\u00a0called Ubiquitin as he thought it was probably ubiquitous to all living cells \u2013 turning up\u00a0everywhere in animal and plant cells and even yeast. Each living cell is made up of many\u00a0tiny proteins. A protein is a molecule made up of one or more chains of amino acids in a\u00a0predetermined order. Proteins maintain structure, function and regulation of cells. Each\u00a0protein has its own unique function \u2013 some famous proteins being hormones, enzymes and antibodies.<\/p>\n
In the 1970s, protein synthesis was understood, yet the breakdown or destruction of\u00a0unwanted proteins in cells back to amino acid was still quite a mysterious process.<\/p>\n
Over three decades ago, Technion Profs. Hershko and Ciechanover were immersed in ideas as to\u00a0how to complete our picture of cell regeneration through understanding how proteins are\u00a0degraded.\u00a0Working closely with colleague and fellow\u00a0Nobel Prize Laureate Irwin Rose, then of Fox\u00a0Chase Cancer Center, Philadelphia, they\u00a0showed how the small and common protein\u00a0Ubiquitin attaches to other proteins, and\u00a0marks them for destruction. Ubiquitin is quite\u00a0a unique protein, as its task is that of a kind of\u00a0runner between other proteins, labeling them\u00a0if necessary for destruction or degradation.\u00a0\u201cMany knew how the body produces proteins,\u00a0but not how they were destroyed,\u201d says\u00a0Hershko. \u201cWithout an engine, a car\u00a0cannot run; without brakes, it is out of control.\u00a0Proteins provide ways to moderate the body\u2019s\u00a0machinery.\u201d<\/p>\n
At first the three scientists, Hershko, graduate\u00a0student Ciechanover and U.S. colleague\u00a0Irwin Rose noticed that Ubiqitin had a way of\u00a0binding to other proteins \u2013 but they didn\u2019t\u00a0know why.\u00a0\u201cHershko used a really simple system in\u00a0order to make the discovery \u2013 just a soup of\u00a0enzymes and proteins,\u201d colleague John Mayer\u00a0of Nottingham University told New Scientist. \u201cFrom this he was able to show the target protein\u00a0must be \u201cubiquitinated.\u201d<\/p>\n
Sometimes working in tandem, Ubiquitin molecules smartly seek out proteins that are no\u00a0longer needed, damaged or unhelpful and tag them\u00a0for degradation, escorting them to a barrel-shaped\u00a0structure called a proteasome \u2013 the cellular recycler.\u00a0It is a process that cognoscenti call \u201cubiquitination\u201d.\u00a0It is a \u201ckiss of death\u201d for protein, which is a \u201ckiss of\u00a0life\u201d for cells.\u00a0Later, the scientists identified three types of\u00a0enzymes involved in the ubiquitination process. The\u00a0third type \u2013 the Ubiquitin protein ligases \u2013 is the\u00a0one that identifies and singles out the target protein.\u00a0Ligases are the cellular whistle-blowers.\u00a0The sophisticated process takes place in cells all\u00a0over the body \u2013 it is highly ubiquitous. But at first,\u00a0few attached the label of \u201ctremendous discovery\u201d to\u00a0the work.<\/p>\n