Search results for NRF1

Showing 14 results out of 19

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Species

Types

Compartments

Reaction types

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Protein (1 results from a total of 1)

Identifier: R-HSA-1592205
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: NRF1: Q16656

Interactor (2 results from a total of 2)

Identifier: Q16656-4
Species: Homo sapiens
Primary external reference: UniProt: Q16656-4
Identifier: Q14494-2
Species: Homo sapiens
Primary external reference: UniProt: Q14494-2

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-4686148
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000106459

Reaction (5 results from a total of 10)

Identifier: R-HSA-1592242
Species: Homo sapiens
Compartment: nucleoplasm
The NRF1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein. NRF1 protein is located in the nucleus where it regulates transcription.
Identifier: R-HSA-1592245
Species: Homo sapiens
Compartment: nucleoplasm
As inferred from mouse, PGC-1beta (PPARGC1B) binds NRF1 and coactivates genes regulated by NRF1.
Identifier: R-HSA-2466369
Species: Homo sapiens
Compartment: nucleoplasm
As inferred from mouse, PGC-1beta (PPARGC1B) binds NRF1 and coactivates genes regulated by NRF1.
Identifier: R-HSA-2466370
Species: Homo sapiens
Compartment: nucleoplasm
As inferred from mouse, PGC-1beta (PPARGC1B) binds NRF1 and coactivates genes regulated by NRF1.
Identifier: R-HSA-1592249
Species: Homo sapiens
Compartment: nucleoplasm
PRC (PPRC1) binds NRF1 and coactivates genes regulated by NRF1 (Andersson and Scarpulla 2001, Vercauteren et al. 2008).

Complex (3 results from a total of 3)

Identifier: R-HSA-2466384
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-2466375
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-2466382
Species: Homo sapiens
Compartment: nucleoplasm

Pathway (2 results from a total of 2)

Identifier: R-HSA-2151201
Species: Homo sapiens
Compartment: cytosol, nucleoplasm, mitochondrial matrix
Phosphorylated PPARGC1A (PGC-1alpha) does not bind DNA directly but instead interacts with other transcription factors, notably NRF1 and NRF2 (via HCF1). NRF1 and NRF2 together with PPARGC1A activate the transcription of nuclear-encoded, mitochondrially targeted proteins such as TFB2M, TFB1M, and TFAM. PGC-1beta and PPRC appear to act similarly to PGC-1alpha but have not been as well studied. Transcription of PPARGC1A itself is upregulated by CREB1 (in response to calcium), MEF2C/D, ATF2, and PPARGC1A. Transcription of PPARGC1A is repressed by NR1D1 (REV-ERBA).
Identifier: R-HSA-1592230
Species: Homo sapiens
Compartment: cytosol, mitochondrial matrix, nucleoplasm
Mitochondrial biogenesis and remodeling occur in response to exercise and redox state (reviewed in Scarpulla et al. 2012, Handy and Loscalzo 2012, Piantadosi and Suliman 2012, Scarpulla 2011, Wenz et al. 2011, Bo et al. 2010, Jornayvaz and Shulman 2010, Ljubicic et al. 2010, Hock and Kralli 2009, Canto and Auwerx 2009, Lin 2009, Scarpulla 2008, Ventura-Clapier et al. 2008). It is hypothesized that calcium influx and energy depletion are the signals that initiate changes in gene expression leading to new mitochondrial proteins. Energy depletion causes a reduction in ATP and an increase in AMP which activates AMPK. AMPK in turn phosphorylates the coactivator PGC-1alpha (PPARGC1A), one of the master regulators of mitochondrial biosynthesis. Likewise, p38 MAPK is activated by muscle contraction (possibly via calcium and CaMKII) and phosphorylates PGC-1alpha. CaMKIV responds to intracellular calcium by phosphorylating CREB, which activates expression of PGC-1alpha.
Deacetylation of PGC-1alpha by SIRT1 may also play a role in activation (Canto et al. 2009, Gurd et al. 2011), however Sirt11 deacetylation of Ppargc1a in mouse impacted genes related to glucose metabolism rather than mitochondrial biogenesis (Rodgers et al. 2005) and mice lacking SIRT1 in muscle had normal levels of mitochondrial biogenesis in response to exercise (Philp et al. 2011) so the role of deacetylation is not fully defined. PGC-1beta and PPRC appear to act similarly to PGC-1alpha but they have not been as well studied.
Phosphorylated PGC-1alpha does not bind DNA directly but instead interacts with other transcription factors, notably NRF1 and NRF2 (via HCF1). NRF1 and NRF2 together with PGC-1alpha activate the transcription of nuclear-encoded, mitochondrially targeted proteins such as TFB2M, TFB1M, and TFAM.
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