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Science's STKE, 2001
The small guanosine triphosphatase Ran is involved in transport of proteins into the nucleus and has been recognized more recently as a regulator of formation of the mitotic spindle. Wiese et al. show that Ran uses the same binding partner, importin-β, to control microtubule formation that it uses to promote protein
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The small guanosine triphosphatase Ran is involved in transport of proteins into the nucleus and has been recognized more recently as a regulator of formation of the mitotic spindle. Wiese et al. show that Ran uses the same binding partner, importin-β, to control microtubule formation that it uses to promote protein
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Importin-mediated nuclear transport in neurons
Current Opinion in Neurobiology, 2006The polarized morphology of neurons poses a particular challenge to intracellular signal transduction. Local signals generated at distal sites must be retrogradely transported to the nucleus to produce persistent changes in neuronal function. Such communication of signals between distal neuronal compartments and the nucleus occurs during axon guidance,
Klara Olofsdotter, Otis +2 more
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Trends in Cell Biology, 1995
The accumulation of karyophilic proteins in the nucleus requires cytoplasmic factors. Cell-free systems that reconstitute nuclear protein import have been used to identify several of these factors and to define the biochemical requirements for the import process.
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The accumulation of karyophilic proteins in the nucleus requires cytoplasmic factors. Cell-free systems that reconstitute nuclear protein import have been used to identify several of these factors and to define the biochemical requirements for the import process.
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The Interaction Between Importin‐α and Nup153 Promotes Importin‐α/β‐Mediated Nuclear Import
Traffic, 2012AbstractNuclear transport is mediated by transport factors, including the importin β family members. The directionality of nuclear transport is governed by the asymmetrical distribution of the small GTPase Ran. Of note, importin α/β‐mediated import of classical nuclear localization signal (cNLS) – containing cargo is more efficient than other Ran ...
Yutaka, Ogawa +3 more
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2002
Importins are nuclear transport receptors of the karyopherin superfamily. They recognize nuclear proteins that are synthesized in the cytoplasm and translocate them to the nucleus (Mattaj and Englmeier 1998; Weis 1998; Gorlich and Kutay 1999; Nakielny and Dreyfuss 1999).
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Importins are nuclear transport receptors of the karyopherin superfamily. They recognize nuclear proteins that are synthesized in the cytoplasm and translocate them to the nucleus (Mattaj and Englmeier 1998; Weis 1998; Gorlich and Kutay 1999; Nakielny and Dreyfuss 1999).
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Regulated importin expression throughout spermatogenesis
2021This thesis was scanned from the print manuscript for digital preservation and is copyright the author. Researchers can access this thesis by asking their local university, institution or public library to make a request on their behalf. Monash staff and postgraduate students can use the link in the References field.
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Structure of importin-beta bound to the IBB domain of importin-alpha.
Nature, 1999Cytosolic proteins bearing a classical nuclear localization signal enter the nucleus bound to a heterodimer of importin-alpha and importin-beta (also called karyopherin-alpha and -beta). The formation of this heterodimer involves the importin-beta-binding (IBB) domain of importin-alpha, a highly basic amino-terminal region of roughly 40 amino-acid ...
G, Cingolani +3 more
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Losing Importin Functions Under Stress
Science's STKE, 2004Proteins bearing a nuclear localization sequence (NLS) are transported into the nucleus in a complex with importin α and importin β. The small guanosine triphosphatase (GTPase) Ran is found in the nucleus, mostly in its GTP-bound form, and binds as Ran-GTP to importin β, causing dissociation of the complex and release of the protein cargo ...
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