FEI LITwo crystal structures for translocator protein (TSPO)—from the bacteria Bacillus cereus and Rhodobacter sphaeroides—are the latest pieces in the puzzle that is determining the functions of this integral mitochondrial membrane protein. The structures, published in Science this week (January 29), are a match, but they differ from a published murine TSPO.
“Membrane proteins are very difficult to work on . . . so when you have two independent groups actually coming up with seemingly identical or very similar structures, it’s very gratifying,” said structural biologist Chris Tate of the Medical Research Council’s Laboratory of Molecular Biology in Cambridge, UK, who was not involved in the studies.
“This protein is 5 billion years old, so it has been evolving over all that time and has adapted to the various needs of the tissues, cells, and species. . . . It’s not surprising that it may really have diverse roles,” Vasillios Papadopoulos, a professor of medicine at McGill University in Montreal who was not involved in the work, told The Scientist.
MIT, EDWARD NIEH, KARA PREBREY, AND KAY TYEUsing a modified optogenetics approaches, two groups have zeroed in on neurons in the mouse lateral hypothalamus (LH) that are linked to eating in excess. Their studies were published in Cell this week (January 29).
