Identification of short linear peptides that function as protein interaction motifs and confer nuclear import

我们的目标是更多地了解调节蛋白质定位的过程。许多蛋白质通过特定的定位信号精确地靶向特定的亚细胞区室。正确的定位是必要的，以确保适当的活动不仅在细胞内的适当位点，而且还限制在不适当的位点的功能。蛋白质的核输入通常通过经由核定位信号（NLS）与可溶性胞质受体蛋白的相互作用来介导。典型的NLS包含一段短的碱性氨基酸（单组分）或两段间隔很近的碱性氨基酸（双组分）。尽管典型的NLS的长度很短，只有4或5个氨基酸，但它们在胞质溶胶中与NLS受体的输入素家族成员（也称为核转运蛋白）产生高亲和力的相互作用。输入蛋白作为载体将相互作用的货物导向细胞核。

Our goal is to learn more about processes regulating protein localization. Many proteins are precisely targeted to particular sub-cellular compartments by specific localization signals. Correct localization is necessary to ensure that the appropriate activity is not only at the appropriate site within the cell, but also to restrict function at inappropriate sites. Nuclear import of proteins is typically mediated by interaction with soluble cytosolic receptor proteins via nuclear localization signals (NLSs). Canonical NLSs containeither a short stretch of basic amino acids (monopartite) or two closely spaced short stretches of basic amino acids (bipartite). Despite theshort length of canonical NLSs, which are as little as 4 or 5 amino acids in length, they make high affinity interactions in the cytosol withmembers of the importin family of NLS receptors (also known as karyopherins). Importins function as carriers to direct the interacting cargo to the nucleus.