Search results for AJUBA

Showing 10 results out of 10

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Species

Types

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Protein (3 results from a total of 3)

Identifier: R-HSA-2564698
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: AJUBA: Q96IF1
Identifier: R-HSA-5687935
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: AJUBA: Q96IF1
Identifier: R-HSA-2574841
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: Q96IF1

Reaction (2 results from a total of 2)

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).

Complex (3 results from a total of 3)

Identifier: R-HSA-8932458
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-8932472
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-1234125
Species: Homo sapiens
Compartment: cytosol

Set (1 results from a total of 1)

Identifier: R-HSA-8932471
Species: Homo sapiens
Compartment: cytosol

Pathway (1 results from a total of 1)

Identifier: R-HSA-2565942
Species: Homo sapiens
Compartment: cytosol
The kinase activity of PLK1 is required for cell cycle progression as PLK1 phosphorylates and regulates a number of cellular proteins during mitosis. Centrosomic AURKA (Aurora A kinase), catalytically activated through AJUBA facilitated autophosphorylation on threonine residue T288 at G2/M transition (Hirota et al. 2003), activates PLK1 on centrosomes by phosphorylating threonine residue T210 of PLK1, critical for PLK1 activity (Jang et al. 2002), in the presence of BORA (Macurek et al. 2008, Seki et al. 2008). Once activated, PLK1 phosphorylates BORA and targets it for ubiquitination mediated degradation by SCF-beta-TrCP ubiquitin ligases. Degradation of BORA is thought to allow PLK1 to interact with other substrates (Seki, Coppinger, Du et al. 2008, Seki et al. 2008).

The interaction of PLK1 with OPTN (optineurin) provides a negative-feedback mechanism for regulation of PLK1 activity. Phosphorylated PLK1 binds and phosphorylates OPTN associated with the Golgi membrane GTPase RAB8, promoting dissociation of OPTN from Golgi and translocation of OPTN to the nucleus. Phosphorylated OPTN facilitates the mitotic phosphorylation of the myosin phosphatase subunit PPP1R12A (MYPT1) and myosin phosphatase activation (Kachaner et al. 2012). The myosin phosphatase complex dephosphorylates threonine residue T210 of PLK1 and inactivates PLK1 (Yamashiro et al. 2008).
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