NSP-interacting GTPase: A cytosolic protein as cofactor for nuclear shuttle proteins.
Despite the significant progress in the identification of essential components of the nuclear transport machinery, some events of this process are still unclear. Particularly, functional information about the release of nuclear-exported macromolecules at the cytoplasmic side of the nuclear pore complex and their subsequent trans-cytoplasmic movement is lacking. Recently, we identified a cytoplasmic GTPase, designated NIG (NSP-interacting GTPase), which may play a relevant role in these processes. NIG interacts in vivo with the geminivirus NSP and promotes the translocation of the viral protein from the nucleus to the cytoplasm where it is redirected to the cell surface to interact with the viral movement protein, MP. Here we position the NIG function into the mechanistic model for the intracellular trafficking of viral DNA and discuss the putative role of NIG in general cellular nucleocytoplasmic transport of nucleic acid-protein complexes.
Carvalho
Claudine M
CM
Departamento de Fitopatologia; BIOAGRO; Universidade Federal de Viçosa; Viçosa, Minas Gerais Brazil.
Machado
Joao Paulo B
JP
Zerbini
Francisco Murilo
FM
Fontes
Elizabeth Pb
EP
Plant Cell. 1999 Jul;11(7):1267-76
10402428
Annu Rev Microbiol. 1998;52:491-532
9891806
Curr Genet. 2003 Dec;44(5):231-60
14523572
Annu Rev Phytopathol. 2005;43:361-94
16078889
Plant J. 2008 Sep;55(5):869-80
18489709
Cell. 2006 Jun 16;125(6):1041-53
16777596
Trends Biochem Sci. 1998 May;23(5):185-9
9612083
Genes Dev. 2004 Jan 1;18(1):23-34
14701878