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Titolo:
Identification of a conserved loop in Mog1 that releases GTP from Ran
Autore:
Steggerda, SM; Paschal, BM;
Indirizzi:
Univ Virginia, Hlth Sci Ctr, Dept Biochem & Mol Genet, Ctr Cell Signaling,Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 ,Charlottesville, VA 22908 USA Univ Virginia, Hlth Sci Ctr, Program Mol & Cell Biol, Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA
Titolo Testata:
TRAFFIC
fascicolo: 11, volume: 2, anno: 2001,
pagine: 804 - 811
SICI:
1398-9219(200111)2:11<804:IOACLI>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
BINDING-PROTEIN RANBP1; NUCLEAR IMPORT; CHROMOSOME CONDENSATION; CRYSTAL-STRUCTURE; RCC1; REGULATOR; NTF2; INTERACTS; EXCHANGE; HOMOLOG;
Keywords:
GTPase; nuclear export; nuclear import; nucleotide exchange factor; nucleotide release factor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Paschal, BM Univ Virginia, Hlth Sci Ctr, Dept Biochem & Mol Genet, Ctr Cell Signaling,Charlottesville, VA 22908 USA Univ Virginia Charlottesville VAUSA 22908 ille, VA 22908 USA
Citazione:
S.M. Steggerda e B.M. Paschal, "Identification of a conserved loop in Mog1 that releases GTP from Ran", TRAFFIC, 2(11), 2001, pp. 804-811

Abstract

Ran regulates nuclear import and export pathways by coordinating the assembly and disassembly of transport complexes. These transport reactions are linked to the GTPase cycle and subcellular distribution of Ran. Mog1 is an evolutionarily conserved nuclear protein that binds RanGTP and stimulates guanine nucleotide release, suggesting Mog1 regulates the nuclear transport functions of Ran. In the present study, we have characterized the nuclear import pathway of Mog1, and we have defined the domain in Mog1 that stimulates GTP release from Ran. In permeabilized cells, nuclear import of Mog1 is independent of exogenously added factors, and is inhibited by wheat germ agglutinin, indicating that translocation of Mog1 involves physical interactions with the nuclear pore complex. In contrast to RanGEF, which is restricted to the nucleus, Mog1 shuttles between the nucleus and the cytoplasm. Single-point mutations in acidic residues of Mog1 (Asp25, Asp34, Glu37) dramatically reduce GTP release and Ran binding activity, whereas mutation of a single basic residue (Arg30) renders Mog1 hyperactive for GTP release. These mutations map within a conserved, solvent-exposed loop in Mog1 that is functionally similar to the p-wedge used by RanGEF to promote nucleotide release from Ran. These data suggest that Mog1 and RanGEF use similar mechanisms to facilitate guanine nucleotide release from Ran.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 20:34:57