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Proteins move into the nucleus of a cell to regulate various biochemical pathways, with different types of proteins using different means to penetrate the nucleus. Researchers at Weizmann Institute of Science, in Rehovot, Israel, have now figured out the mechanism underlying one of these entry methods (Mol. Cell 2008, 31, 850). Most proteins destined for the nucleus possess a domain known as the nuclear localization signal. "Importin" proteins bind to this domain and help move the bound protein into the nucleus through a pore in the nuclear membrane. But some incoming proteins lack the nuclear localization signal domain. Rony Seger and colleagues report that they have identified a different domain that helps some of these proteins gain entry into the nucleus. The researchers found a short stretch of amino acids that, when phosphorylated, allow the proteins to bind to one type of importin and move across the nuclear membrane. The domain occurs in signaling proteins such as ERKs, MEKs, and SMADs, leading the scientists to believe that their findings might be applicable to other proteins.
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