PULLMAN, Wash. — Linda Randall, a professor at Washington State University since 1981, has been elected a Fellow in the American Association for the Advancement of Science in recognition of her contributions to the understanding of cellular protein secretion.
Randall will receive the award at the Jan. 23 annual meeting in Anaheim, Calif.
All living cells produce a myriad of proteins. Some, such as insulin or digestive enzymes, do their work outside the cell. How it is these large protein molecules are selected for export and are able to pass through the surrounding cell membrane has been the object of Randall’s research.
Proteins are synthesized within a cell as chains of amino acids and tend to quickly fold up into the protein’s “native,” or working, shape. Proteins cannot pass through the cell membrane in their native condition, so folding must somehow be delayed until the protein is secreted. The proteins destined for export have been found to have a short “leader” of amino acids that slows folding long enough for a small “chaperone” protein called SecB to bind.
Randall’s team has established that the chaperone SecB maintains the newly synthesized protein in a non-native state and delivers it to the cell membrane where the leader is cleaved off as the protein passes through. Once secreted from the cell, the protein is free to assume its native shape and go to work.
Randall’s research and conclusions concerning protein synthesis and secretion have considerably altered and expanded the partial explanation of the traditional “signal hypothesis.” Randall’s work has major implications for better understanding hormone production, antibody secretion and other vital processes and has prompted discussion in leading science journals.
The National Academy of Science referred to Randall’s “characteristic originality and clarity of experimental design” when it elected her to membership in 1997. While at Washington State University, Randall has received numerous awards and honors, including the Eli Lilly Award in Microbiology and the President’s Faculty Excellence Award for Research.

ts127-98