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定位到特定的亚细胞区室。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置，而且在不适当的位置限制功能。蛋白质的核输入通常是通过核定位信号（NLSs）与可溶性细胞质受体蛋白相互作用介导的。典型NLSs要么包含一小段碱性氨基酸（单部分），要么包含两个紧密间隔的短段碱性氨基酸（双部分）。尽管典型NLSs的长度很短，只有4或5个氨基酸，但它们在细胞质中与NLS受体的输入蛋白家族成员（也称为核细胞蛋白）进行高亲和力相互作用。进口蛋白起着载体的作用，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.