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STE20-related kinase adaptor beta

This gene encodes a protein that belongs to the serine/threonine protein kinase STE20 subfamily. One of the active site residues in the protein kinase domain of this protein is altered, and it is thus a pseudokinase. This protein is a component of a complex involved in the activation of serine/threonine kinase 11, a master kinase that regulates cell polarity and energy-generating metabolism. This complex regulates the relocation of this kinase from the nucleus to the cytoplasm, and it is essential for G1 cell cycle arrest mediated by this kinase. The protein encoded by this gene can also interact with the X chromosome-linked inhibitor of apoptosis protein, and this interaction enhances the anti-apoptotic activity of this protein via the JNK1 signal transduction pathway. Two pseudogenes, located on chromosomes 1 and 7, have been found for this gene. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2011] (from NCBI)
Top mentioned proteins: V1a, LKB1, calcium-binding protein,, STRAD, Gli3
Papers on PAPK
Characterization of the liver kinase B1-mouse protein-25 -Ste-20-related adaptor protein complex in adult mouse skeletal muscle.
Winder et al., Provo, United States. In J Appl Physiol, 2011
Quantitative PCR revealed significantly reduced LKB1, MO25alpha, and STRADbeta mRNA in LKB1(-/-) muscle. These findings demonstrate that the LKB1-MO25-STRAD complex is the principal AMPKK in skeletal muscle.
Human embryonic stem cells and metastatic colorectal cancer cells shared the common endogenous human microRNA-26b.
Qin et al., Shanghai, China. In J Cell Mol Med, 2011
Four genes (TAF12, PTP4A1, CHFR and ALS2CR2) with intersection were found to be the targets of miR-26b.
STRADalpha regulates LKB1 localization by blocking access to importin-alpha, and by association with Crm1 and exportin-7.
Macara et al., Charlottesville, United States. In Mol Biol Cell, 2008
Strikingly, the STRADbeta, isoform which differs from STRADalpha in the N- and C-terminal domains that are responsible for interaction with export receptors, does not efficiently relocalize LKB1 from the nucleus to the cytoplasm.
Phosphorylation of movement proteins by the plasmodesmal-associated protein kinase.
Lee, Newark, United States. In Methods Mol Biol, 2007
Recently, we have reported the identification of a host protein kinase named plasmodesmal-associated protein kinase (PAPK) which specifically phosphorylates a subset of noncell autonomous proteins in vitro, including MPs of Tobacco mosaic virus (TMV) and Bean dwarf mosaic virus (BDMV).
A molecular dynamics study of pilus subunits: insights into pilus biogenesis.
Berisio et al., Napoli, Italy. In J Mol Biol, 2007
These analyses were extended to the complexes of PapE with the complementary G(1) strand of PapD and with the N-terminal extension of PapK.
C-terminal repetitive motifs in Vp130 present at the unique vertex of the Chlorovirus capsid are essential for binding to the host Chlorella cell wall.
Yamada et al., Hiroshima, Japan. In Virology, 2006
In NC64A-viruses, Vp130 consists of a highly conserved N-terminal domain, internal repeats of 70-73 aa motifs and a C-terminal domain occupied by 23-26 tandem repeats of a PAPK motif.
Characterization of the AMP-activated protein kinase pathway in chickens.
McMurtry et al., Beltsville, United States. In Comp Biochem Physiol B Biochem Mol Biol, 2006
Genes encoding LKB1, MO25 alpha, MO25 beta, and STRAD beta were expressed in all examined tissues, whereas STRAD alpha was expressed exclusively in brain, hypothalamus, heart and skeletal muscle.
Plasmodesmal-associated protein kinase in tobacco and Arabidopsis recognizes a subset of non-cell-autonomous proteins.
Lucas et al., Davis, United States. In Plant Cell, 2005
Here, we describe the molecular characterization of a plasmodesmal-associated protein kinase (PAPK).
Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network.
Drewes et al., Heidelberg, Germany. In J Biol Chem, 2004
We demonstrate that the complex formation between LKB1.Par-4, PAPK, and Mo25 results in the translocation of LKB1 from the nucleus to the cytoplasm and to tight junctions and show that the LKB1 complex may activate MARKs, which are known to introduce 14-3-3 binding sites into several substrates.
Vp130, a chloroviral surface protein that interacts with the host Chlorella cell wall.
Yamada et al., Hiroshima, Japan. In Virology, 2004
In Vp130, the N-terminus was somehow modified and the C-terminus was occupied by 23-26 tandem repeats of a PAPK motif.
MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm.
Alessi et al., Dundee, United Kingdom. In Embo J, 2003
We demonstrate that the related STRADbeta and MO25beta isoforms are also able to stabilize LKB1 in an active complex and that it is possible to isolate complexes of LKB1 bound to STRAD and MO25 isoforms, in which the subunits are present in equimolar amounts.
Identification and characterization of a novel Ste20/germinal center kinase-related kinase, polyploidy-associated protein kinase.
Ruscetti et al., Frederick, United States. In J Biol Chem, 2003
A novel protein kinase, polyploidy-associated protein kinase (PAPK), was isolated using a subtraction cDNA library approach from a mouse erythroleukemia cell line that had been induced to polyploidy after serum withdrawal.
Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade.
Hardie et al., Dundee, United Kingdom. In J Biol, 2002
Third, catalytically active LKB1, STRAD alpha or STRAD beta and MO25 alpha or MO25 beta are required for full activity.
ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated activation of JNK1 and protection against apoptosis.
Ulevitch et al., Los Angeles, United States. In J Biol Chem, 2002
a novel XIAP-interacting protein that acts as a co-factor enhancing XIAP-mediated activation of JNK1 and the caspase-independent protection of XIAP against apoptosis
Structural basis of chaperone function and pilus biogenesis.
Waksman et al., Saint Louis, United States. In Science, 1999
The crystal structure of the PapD-PapK chaperone-subunit complex, determined at 2.4 angstrom resolution, reveals that the chaperone functions by donating its G(1) beta strand to complete the immunoglobulin-like fold of the subunit via a mechanism termed donor strand complementation.
Structural polymorphism of bacterial adhesion pili.
Makowski et al., Boston, United States. In Nature, 1995
They are attached to the outer membrane by a minor structural protein, PapH and are terminated by an approximately 20 A diameter fibrillus composed of PapK, PapE and PapF, which presents the host-binding adhesin PapG.
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