Profile of Tom A. Rapoport
- Tinsley H. Davis, Freelance Science Writer
Inside any cell, errant, misfolded proteins must be confiscated and destroyed. This process does not occur inside the endoplasmic reticulum, where secretory proteins are folded and packaged for export; instead, misfolded proteins must retrotranslocate—cross the endoplasmic reticulum membrane back into the cytosol. Biochemist Tom A. Rapoport, elected to the National Academy of Sciences in 2005, has spent much of his career studying the membrane channel Derlin-1, which exports proteins from the cytosol. In the last five years, he has studied the reverse protein movement process of retrotranslocation. In his Inaugural Article in this issue of PNAS, Rapoport identifies a class of proteins associated with the retrotranslocation complex (1).
Personal Translocations
Now a Professor of Cell Biology at Harvard Medical School (Boston, MA), Rapoport was born in Cincinnati, OH, in 1947 to parents who had fled the Nazi regime in Austria and Germany. When he was 3 years of age, his parents, a pediatrician and a biochemist, left behind the McCarthy era in the United States to return to Austria. In 1951, the family settled in East Germany.
“We had a scientific household,” Rapoport says. “My parents are responsible for my interest.” According to Rapoport, he performed his first experiment at the age of 5, while making pudding. His mother likes to recall how the young Rapoport stood in the kitchen cooking pudding and coloring it blue. He carefully labeled it “blue pudding,” and his mother made him write up the experiment in a notebook. He recalls this as his first laboratory report.
Mathematics held Rapoport's interest in his early teenage years, and he recalls, “There was a short period where I was interested in being a test pilot, but that didn't last long.” Rapoport majored in chemistry in his first three years of college and switched to biochemistry in his fourth …
