Search results for AURKA

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Reaction (7 results from a total of 14)

Identifier: R-HSA-8854041
Species: Homo sapiens
Compartment: cytosol
The SCF-FBXL7 E3 ubiquitin ligase complex, composed of SKP1, CUL1, RBX1 and FBXL7, ubiquitinates aurora kinase A (AURKA), targeting it for degradation (Coon et al. 2012).
Identifier: R-HSA-8853419
Species: Homo sapiens
Compartment: cytosol
TPX2 promotes aurora kinase A (AURKA) activation via autophosphorylation of AURKA on threonine residue T288. Continuous association of TPX2 with AURKA facilitates active state conformation of AURKA and may prevent inactivation of AURKA by protein phosphatases (Bayliss et al. 2003).

Molecular dynamic simulations suggest the existence of two TPX2-dependent switches for Aurora A activation. 1) TPX2 binding to Aurora A forces lysine residue K143 of AURKA into an “open” state, which pulls ADP out of the ATP binding site in AURKA to promote kinase activation. 2) Arginine residue R180 of AURKA undergoes a “closed” movement upon TPX2 binding, thus capturing phosphorylated threonine T288 of AURKA into a buried position and locking AURKA in its active conformation. The existence of two TPX2-dependent switches in AURKA activation was further verified by the analysis of two AURKA mutants (K143A and R180A) (Xu et al. 2011).AURKA activation is enabled through phosphorylation and TPX2 binding; these two activating switches act synergistically and withough a predefined order (Dodson and Bayliss 2012).

Identifier: R-HSA-3000319
Species: Homo sapiens
Compartment: cytosol
BORA is able to interact with both AURKA (Aurora A kinase) and PLK1. Binding of BORA to PLK1 increases the accessibility of PLK1 threonine residue T210 and also brings PLK1 in proximity to AURKA, enabling AURKA to phosphorylate T210 of PLK1 and thereby activate PLK1 (Seki et al. 2008). While BORA is required for mitotic activation of AURKA in Drosophila (Hutterer et al. 2006), it does not significantly activate AURKA in human cells (Seki et al. 2008). AURKA is able to phosphorylate BORA in vitro, but the functional significance of this modification has not been determined (Hutterer et al. 2006).
Identifier: R-HSA-8853405
Species: Homo sapiens
Compartment: cytosol
TPX2 binds to aurora kinase A (AURKA) at centrosomes. The first 43 amino acids at the N-terminus of TPX2 are needed for binding to AURKA (Bayliss et al. 2003). HMMR (RHAMM) binds to TPX2 (Groen et al. 2004, Maxwell et al. 2005) and is involved in the proper localization of TPX2 to centrosomes and TPX2-mediated AURKA activation (Chen et al. 2014, Scrofani et al. 2015).

TPX2 binding to Aurora A protects premature AURKA degradation by APC/C-mediated proteolysis during early mitosis. TPX2 differentially regulates AURKA stability, activity and localization. While amino acids 1-43 in TPX2 facilitate complex formation between AURKA and TPX2 and promote kinase activation, they are insufficient for AURKA targeting to the mitotic spindle (Giubettini et al. 2011).

Identifier: R-HSA-2574840
Species: Homo sapiens
Compartment: cytosol
AURKA (Aurora A kinase) activation through autophosphorylation of threonine T288 is facilitated by AJUBA binding. AJUBA is also phosphorylated by AURKA on an unidentified serine or threonine residue (Hirota et al. 2003).
Identifier: R-HSA-2574845
Species: Homo sapiens
Compartment: cytosol
AJUBA, a LIM domain-containing protein, binds centrosome-associated AURKA (Aurora A kinase) through interaction of LIM-2 and LIM-3 domains of AJUBA with the N-terminus of AURKA (Hirota et al. 2003).
Identifier: R-HSA-8854044
Species: Homo sapiens
Compartment: cytosol
Upon ubiquitination by the SCF-FBXL7 E3 ubiquitin ligase complex, aurora kinase A (AURKA) is degraded by the proteasome (Coon et al. 2012).
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