Nuclear pore proteins and cancer.
Nucleocytoplasmic trafficking of macromolecules, a highly specific and tightly regulated process, occurs exclusively through the nuclear pore complex. This immense structure is assembled from approximately 30 proteins, termed nucleoporins. Here we discuss the four nucleoporins that have been linked to cancers, either through elevated expression in tumors (Nup88) or through involvement in chromosomal translocations that encode chimeric fusion proteins (Tpr, Nup98, Nup214). In each case we consider the normal function of the nucleoporin and its translocation partners, as well as what is known about their mechanistic contributions to carcinogenesis, particularly in leukemias. Studies of nucleoporin-linked cancers have revealed novel mechanisms of oncogenesis and in the future, should continue to expand our understanding of cancer biology.
Xu
Songli
S
Department of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Powers
Maureen A
MA
D000818:Animals; D014408:Biomarkers, Tumor / Q000378:metabolism; D052138:Genes, Neoplasm; D006801:Humans; D009369:Neoplasms / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000235:genetics / Q000378:metabolism*; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism; D014158:Transcription, Genetic
D014408:Biomarkers, Tumor; D028861:Nuclear Pore Complex Proteins; D020794:Receptor Protein-Tyrosine Kinases