Marc Vidal

First Person | Marc Vidal Courtesy of The Marc Vidal Lab In 1996, Marc Vidal, proteomic cartographer and coinventor of the reverse two-hybrid system, couldn't find work that paid more than a postdoc's salary. He survived on a National Institutes of Health grant and the good graces (if not the prescience) of Harvard University cell biologist Ed Harlow, who believed in Vidal's vision to map protein to protein and let the young Belgian work in his lab. The ideas weren't fashionable, Vidal says. "Fellowship applications, forget it. Jobs in academia, forget it," recalls Vidal, now 41. "The reductionist approach was fantastic in terms of careers." Presently at the Dana-Farber Cancer Institute in Boston, Vidal stresses that he is not complaining. "It's important for young people... to commit yourself to your own passion, and what you develop has a chance to become the next fashion." How did you survive? I had to fight and scream. I went to NIH; they did give me funding early on. That's what saved me. [Albertha J.M.] Walhout, she came to my lab without a salary, but the chairman of the department [found] six months' salary for her. Fortunately, the NIH grant came through after. When did your break come? A few papers and a few maps later, I joined Harvard at the end of 1999. How did your formative years affect you? My mom had a grocery store, and my dad is in the insurance business. I always loved agriculture. I would spend my summers at the farms ... It's related to what I am doing today. I went to engineering school for agronomy. It made me discover the beautiful aspect of biology from an engineering side. Why did you switch? A molecular biology teacher... really changed my life. I absolutely loved his class. [I found] that DNA was one of the keys of understanding life. I didn't know that before. In a few weeks, I changed my mind [about my career]. When did you arrive in the United States? I came with a backpack [in 1988], and a few phone numbers. Richard Gaber was starting his lab at Northwestern. He said, 'Do you want to come to my lab?' I was shaking [with excitement] when I heard that .... The American Dream, from a scientific point of view, is to have your own lab. I didn't want to work for somebody else for 25 years. You said your work has come full circle. How? Gaber found gene TRK 1, [which] is required for potassium transport. I started working on mutants that needed these lower concentrations of potassium. I called these mutants Potassium Dependency. One is RPD3, a beautiful mutant. It was very pleiotropic. What happened, RPD3 was a transcriptional repressor that acted globally. It's also a transcriptional repressor of TRK 1. Go 10 years forward with expression profiling; you can measure expression of all yeast genes. The conclusion is that RPD3 is a repressor for one-third of the yeast genome. That's what we know today. (We also know that a product of RPD3 is an enzyme with histone deacetylase activity.) It was obvious that the genome projects would open huge spaces of uncharacterized genes. The little neighborhood, which I left once and came back to, was a small portion of the whole story. How do you deal with your work's computational challenges? It humbles you. I didn't grow up with a computational basis, so I hire people who I think are excellent. Together, we try to understand each other's languages, and work from different approaches. Agronomy is based on statistics, so I am feeling relatively comfortable with this. What was frustrating was the lack of holistic approaches. Your favorite paper? It started the protein interaction maps.1 It was a small network at the time; it definitely pointed to the direction we're all in now. What makes you laugh? Good Belgian humor. It has a tendency to be more surrealistic. From its politics to everything else, it's miracle that [Belgium] works. What makes you angry? If scientists are not committed to what they are doing, that makes me angry. And sloppiness, that makes me angry. What are you working on now? What's becoming a subfield is to analyze the structure of a proteome; the higher the level of organization, [then] there is something behind it. One physicist, Barabasi Laszlo, says that those networks we are mapping resemble the World Wide Web. Cites are hyperlinked, and you end up mapping hundreds of thousands of Web sites. You will get nodes representing cites, and edges representing links. Barabasi said both networks are scale-free. A small proportion of nodes are super-highly connected to other nodes, where a majority has few connections. Proteins are like that, too. This has tremendous implications for therapies. We are studying the hubs. We can extract a good number of hypotheses, a general model, on how hubs organize at the highest level.... The genome project allows this. 1. A.J. Walhout et al., "Protein interaction mapping in C. elegans using proteins involved in vulval development," Science, 287:116-22, 2000. function sendData() { document.frm.pathName.value = location.pathname; result = false if (document.frm.score[0].checked) result = true; if (document.frm.score[1].checked) result = true; if (document.frm.score[2].checked) result = true; if (document.frm.score[3].checked) result = true; if (document.frm.score[4].checked) result = true; if (!result) alert("Please select") return result; } .myradio{background-color : #94bee5} Please indicate on a 1 - 5 scale how strongly you would recommend this article to your colleagues? Not recommended 1 2 3 4 5 Highly recommended Please register your vote

Marc Vidal

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First Person | Marc Vidal

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