title: The nuclear pore complex: a new dynamic in HIV-1 replication.
abstract: The ability to traverse an intact nuclear envelope and productively infect non-dividing cells is a salient feature of human immunodeficiency virus type 1 (HIV-1) and other lentiviruses, but the viral factors and mechanism of nuclear entry have not been defined. We have recently reported a functional role for the nucleoporin NUP153 in the nuclear import of the HIV-1 preintegration complex (PIC). Our findings suggest that HIV-1 sub-viral particles gain access to the nucleus by interacting directly with the nuclear pore complex (NPC) via the binding of PIC-associated integrase (IN) to the C-terminal domain of NUP153. This article discusses how NPC conformation and constitution might influence nuclear import of the PIC, and the subsequent integration of the viral cDNA into actively transcribed genes.
authors.affiliation: Department of Molecular and Medical Pharmacology, and UCLA AIDS Institute, UCLA School of Medicine, Los Angeles, CA, USA.
authors.forename: Cora L
authors.initials: CL
authors.lastname: Woodward
authors.forename: Samson A
authors.initials: SA
authors.lastname: Chow
mesh_terms: D021581:Active Transport, Cell Nucleus; D019427:HIV Integrase / Q000378:metabolism; D015497:HIV-1 / Q000502:physiology*; D006801:Humans; D008958:Models, Molecular; D022022:Nuclear Pore / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000378:metabolism; D011485:Protein Binding; D014779:Virus Replication
chemical_list: C079377:NUP153 protein, human; D028861:Nuclear Pore Complex Proteins; D019427:HIV Integrase