Search results for RPS6KA1

Showing 17 results out of 17

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Protein (7 results from a total of 7)

Identifier: R-HSA-444256
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RPS6KA1: Q15418
Identifier: R-HSA-199860
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: RPS6KA1: Q15418
Identifier: R-HSA-199829
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: RPS6KA1: Q15418
Identifier: R-HSA-9619957
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RPS6KA1: Q15418
Identifier: R-HSA-9619993
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RPS6KA1: Q15418
Identifier: R-HSA-444292
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: RPS6KA1: Q15418
Identifier: R-HSA-9619871
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: RPS6KA1: Q15418

Reaction (9 results from a total of 9)

Identifier: R-NUL-9619973
Species: Rattus norvegicus, Homo sapiens
Compartment: cytosol
Recombinant human MAPK1 (ERK2) phosphorylates recombinant rat Rps6ka1 on threonine residue T359, serine residue S363 and threonine residue T573 (Dalby et al. 1998).
Identifier: R-HSA-9824994
Species: Homo sapiens
Compartment: nucleoplasm
MITF-M is phosphorylated by RPS6KA1 (also known as RSK1) at serine S409 downstream of activated SCF-KIT signaling during development (Wu et al, 2000). S409 phosphorylation primes MITF-M for subsequent phosphorylation by GSK3B at serine residues S397, S401 and S405 in the C-terminus, modifications that are associated with degradation of the protein (Ploper et al, 2015, reviewed in Goding and Arnheiter, 2019).
The relationship between MITF and KITLG-KIT during melanocyte differentiation is not totally clear. Mutations of KIT or its ligand are associated with pigmentation defects and depleted levels of mature melanocytes. KIT signaling appears to contribute to the migration and survival of melanoblasts during development (Wehrle-Haller and Weston, 1995; Wehrle-Haller et al, 2001; Tabone-Eglinger et al, 2012; Kunisada et al, 1998; reviewed in White and Zon, 2008). MITF-M and KIT also appear to reciprocally affect each other's expression: although KIT does not appear to be required for the initial expression of MITF during development, activated KIT signaling increases the transcription factor activity of MITF to a variable extent at different MITF-M target genes (Hou et al, 2000; Price et al, 1998, Wu et al, 2000, Hemesath et al, 1998). Similarly, expression of MITF-M has been shown to increase expression of KIT in some systems (Tsujimura et al, 1996; Opdecamp et al, 1997; reviewed in Hou and Pavan, 2008)
Identifier: R-HSA-3857328
Species: Homo sapiens
Compartment: nucleoplasm
Phosphorylation of CEBPB (C/EBP-beta) serine residue S321 by ERK1/2-activated RSK1, RSK2 or RSK3, downstream of activated RAS, is necessary for the relief of CEBPB autoinhibiton (Lee et al. 2010). Phosphorylation on other sites may also be involved in CEBPB activation.
Identifier: R-NUL-3876071
Species: Rattus norvegicus, Mus musculus, Homo sapiens
Compartment: nucleoplasm
Phosphorylation of rat Cebpb (C/EBP-beta) serine residue S273 by ERK1/2-activated human RSK1, mouse RSK2 or human RSK3, downstream of activated RAS, is necessary for the relief of Cebpb autoinhibiton (Lee et al. 2010). Phosphorylation on other sites may also be involved in Cebpb activation.
Identifier: R-HSA-9620004
Species: Homo sapiens
Compartment: cytosol
Upon phosphorylation by activated ERKs, ribosomal S6 kinases (RSKs) autophosphorylate on conserved serine residue in the linker region (S380 in RPS6KA1) and a conserved threonine residue at the C-terminal ERK-docking domain (T732 in RPS6KA1) (Dalby et al. 1998, Roux et al. 2003). Autophosphorylation at the ERK-docking domain regulates binding to ERK and duration of RSK activity (Roux et al. 2003).
Identifier: R-HSA-9619843
Species: Homo sapiens
Compartment: cytosol
MAP kinases/ERKs (MAPK1 and MAPK3), activated downstream of RAS signaling, activate RSKs by phosphorylating conserved serine and threonine residues in the linker region and the C-terminal kinase domain (CTKD). In the linker region of RPS6KA1 (RSK1), ERKs phosphorylate threonine residue T359 and serine residue S363. In the CTKD of RPS6KA1, ERKs phosphorylate threonine residue T573 (Dalby et al. 1998, Roux et al. 2003).
Identifier: R-HSA-442739
Species: Homo sapiens
Compartment: nucleoplasm
PDPK1 (PDK1) activates ribosomal S6 kinases (RSKs) by phosphorylating a conserved serine residue S221 (in RPS6KA1). The binding site for PDPK1 on RSKs is available after RSK phosphorylation by MAPKs/ERKs. PDPK1 is present in the activated form at the plasma membrane where the phosphorylation occurs (Jensen et al. 1999).
Identifier: R-HSA-442724
Species: Homo sapiens
Compartment: nucleoplasm
CREB1 is phosphorylated at serine residue S133 by any of the three isoforms of ribosomal S6 kinase (RSK): RPS6KA1 (RSK1) (Song et al. 2003), RPS6KA2 (RSK3) (Schinelli et al. 2001), RPS6KA3 (RSK2) (De Cesare et al. 1998, Harum et al. 2001), and probably by RPS6KA6 (RSK4).
Identifier: R-HSA-9824995
Species: Homo sapiens
Compartment: nucleoplasm
RPS6KA1-dependent phosphorylation of MITF-M at serine 409 primes the protein for subsequent phosphorylations at three sites in the C-terminal region by GSK3B. Mutation of serine residues at S397, S401 and S405 to alanine increases the stability of MITF-M, suggesting a role for GSK3B in degradation of the protein. Consistent with this, WNT3A treatment, which inactivates GSK3B, increases MITF-M stability and increases its transcription factor activity towards target gene MART1 in the melanoma cell line M308 (Wu et al, 2000; Ploper et al, 2015; reviewed in Goding and Arnheiter, 2019).

Pathway (1 results from a total of 1)

Identifier: R-HSA-444257
Species: Homo sapiens
Compartment: cytosol, nucleoplasm
Ribosomal S6 kinase (RSK) has four isoforms in humans, RPS6KA1 (RSK1), RPS6KA2 (RSK3), RPS6KA3 (RSK2) and RPS6KA6 (RSK4), and each of the isoforms have six conserved phosphorylation sites (in RPS6KA1, these are serine residues S221, S363 and S380 and threonine residues T359, T573 and T732). Phosphorylation at four of these residues appears to be critically important for the catalytic activity of RSKs: S221, S363, S380 and T573 (in RPS6KA1).
Phosphorylation and activation of RSKs primarily occurs at the plasma membrane, but can occur in the cytoplasm and in the nucleus. ERKs (MAPK1 and MAPK3), activated downstream of RAS signaling, phosphorylate RSKs on threonine and serine residues T359, S363 and T573 (in RPS6KA1). Phosphorylation by ERKs enables autophosphorylation of RSKs on serine residue S380 and threonine residue T732 (in RPS6KA1). Phosphorylation of RSKs by PDPK1 (PDK1) at serine residue S221 (in RPS6KA1) is necessary for the full activation of RSKs and phosphorylation of RSK substrates (reviewed by Anjum and Blenis 2012). RSK4 differs from other RSKs because it shows high level of constitutive phosphorylation and activity in the absence of growth factors, although it is still responsive to growth factors and ERK activity (Dummler et al. 2005).
RSKs, especially RSK2, are highly expressed in brain regions with high synaptic activity. RSK2 mutations are the underlying cause of Coffin-Lowry syndrome (CLS), which is characterized by cognitive impairment and skeletal anomalies (Zeniou et al. 2002).
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