Search results for NUP62

Showing 9 results out of 9

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Species

Types

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Protein (2 results from a total of 2)

Identifier: R-HSA-157713
Species: Homo sapiens
Compartment: nuclear envelope
Primary external reference: UniProt: NUP62: P37198
Identifier: R-HSA-9634226
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: NUP62: P37198

Complex (4 results from a total of 4)

Identifier: R-HSA-157712
Species: Homo sapiens
Compartment: nuclear envelope
Identifier: R-HSA-9634220
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9634222
Species: Homo sapiens
Compartment: nuclear envelope
Identifier: R-HSA-9631759
Species: Homo sapiens
Compartment: nuclear envelope

Reaction (3 results from a total of 3)

Identifier: R-HSA-9634219
Species: Homo sapiens
Compartment: nuclear envelope, cytosol
The N-terminal domain of NUP93, the eponymous subunit of the Nup93 complex, recruits the Nup62 complex, consisting of phenylglycine (FG) repeat-containing nucleoporins NUP62, NUP58 and NUP54 (Chug et al. 2015), to the nascent nuclear pore complex (NPC) (Sachdev et al. 2012). The barrier function of the NPC is reestablished at this point (Dultz et al. 2008).
Identifier: R-HSA-3134914
Species: Homo sapiens
Compartment: cytosol, nuclear envelope, nucleoplasm
Phosphorylated beta-catenin migrates to the nucleus where it functions as a coactivator of IRF3-dependent transcription (Yang P et al. 2010).

Beta-catenin transport to the nucleus is thought to occur in a NLS (nuclear localization signal)- and importin-independent manner through direct interaction with the nuclear pore complex (NPC) components. This has been shown to be the case for Wnt-signaling in mammalian cells (Yokoya F et al. 1999; Koike M et al. 2004; Sharma M et al. 2012)

Identifier: R-HSA-5618080
Species: Homo sapiens
Compartment: cytosol, nuclear envelope, nucleoplasm
Steroid hormone receptors (SHRs) are shuttling proteins, which continuously undergo nuclear import and export. Although the various SHRs have different resting localizations in cells, rapid and almost complete nuclear translocation following ligand addition is a common behavior observed for almost all SHRs (except the already nuclear estrogen receptors). The Reactome event shows microtubule-associated nuclear translocation through the recruitment of the large immunophilin FKBP52 (FKBP4) to the SHR:HSP90 complex (Galigniana et al. 2002; Wochnik et al. 2005; Davies and Sanchez 2005; Galigniana MD et al. 2010). FKBP52 links glucocorticoid receptor (GR):HSP90 and mineralocorticoid receptor (MR):HSP90 complexes to dynein/dynactin motors favoring transport of the cytoplasmic SHR to the nucleus (Wochnik et al. 2005; Gallo L et al. 2007). Moreover, the cytoplasmic-nuclear movement of GR was blocked in fibroblasts co-expressing dynamitin, which dissociates dynein from its cargoes (Harrell et al. 2004). FKBP52 directly binds to the motor protein dynein through the peptidyl-prolyl isomerase (PPIase) domain (Wochnik et al. 2005). Interestingly, the PPIase domain of another immunophilin FKBP51 (FKBP5) is unable to interact with dynein. Without hormone, FKBP51 is the major immunophilin in GR:HSP90 complexes, whereas after hormone treatment, FKBP52 rapidly replaces FKBP51 such that these complexes are now able to translocate to the nucleus with an accelerated rate (Davies et al. 2002). In addition, replacement of FKPB52 by FKBP51 favored the cytoplasmic localization of MR (Galigniana MD et al. 2010). On the other hand, GR was apparently able to translocate to the nucleus with the same rate even if the microtubule network was completely disrupted suggesting that he subcellular localization of SHRs can be controlled by several coexisting mechanisms (Czar et al. 1995). Indeed, in yeast and mammalian cells liganded and unliganded SHRs can bind several importins to be translocated into the nucleus (Freedman & Yamamoto 2004; Picard & Yamamoto 1987). In addition, importin beta and the integral nuclear pore glycoprotein NUP62 interact with HSP90, HSP70, p23, and the TPR domain proteins FKBP52 and PP5. NUP62 and GR are able to interact in a more efficient manner when chaperoned by the HSP90-based heterocomplex (Echeverria et al. 2009). GR cross-linked to the HSP90 heterocomplex is able to translocate to the nucleus in digitonin-permeabilized cells treated with steroid, suggesting that GR could pass through the pore in its untransformed state (Echeverria et al. 2009).
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