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STE20-related kinase adaptor alpha

The protein encoded by this gene contains a STE20-like kinase domain, but lacks several residues that are critical for catalytic activity, so it is termed a 'pseudokinase'. The protein forms a heterotrimeric complex with serine/threonine kinase 11 (STK11, also known as LKB1) and the scaffolding protein calcium binding protein 39 (CAB39, also known as MO25). The protein activates STK11 leading to the phosphorylation of both proteins and excluding STK11 from the nucleus. The protein is necessary for STK11-induced G1 cell cycle arrest. A mutation in this gene has been shown to result in polyhydramnios, megalencephaly, and symptomatic epilepsy (PMSE) syndrome. Multiple transcript variants encoding different isoforms have been found for this gene. Additional transcript variants have been described but their full-length nature is not known. [provided by RefSeq, Sep 2009] (from NCBI)
Top mentioned proteins: LKB1, calcium-binding protein,, AMPK, PAK1, CAN
Papers on STRAD
GSK-3β controls autophagy by modulating LKB1-AMPK pathway in prostate cancer cells.
Li et al., Shaoxing, China. In Prostate, Feb 2016
Meanwhile, GSK-3β inhibition promoted LKB1 translocation from nuclear to cytoplasmic compartment and enhanced LKB1 interaction with its regulatory partners Mouse protein-25 (MO25) and STE20-related adaptor (STRAD).
LKB1/Mo25/STRAD uniquely impacts sarcomeric contractile function and posttranslational modification.
Konhilas et al., Tucson, United States. In Biophys J, Apr 2015
Binding of AMP to AMPK not only allosterically activates AMPK but also promotes phosphorylation of AMPK by an upstream kinase complex, LKB1/Mo25/STRAD (liver kinase B 1, mouse protein 25, STE-related adaptor protein).
Skp2-dependent ubiquitination and activation of LKB1 is essential for cancer cell survival under energy stress.
Lin et al., Houston, United States. In Mol Cell, Apr 2015
LKB1 is activated by forming a heterotrimeric complex with STRAD and MO25.
Hydrogen sulfide mitigates hyperglycemic remodeling via liver kinase B1-adenosine monophosphate-activated protein kinase signaling.
Sen et al., Louisville, United States. In Biochim Biophys Acta, 2014
Activation of LKB1 by the formation of heterotrimeric complex with STRAD and MO25 is known to activate AMPK.
Structural insights into regulatory mechanisms of MO25-mediated kinase activation.
Zhou et al., Shanghai, China. In J Struct Biol, 2014
The adaptor molecule MO25 not only recruits and activates LKB1 through the pseudokinase STRAD, but also may directly activate GCKs like MST3, MST4, STK25, OSR1 and SPAK.
STRAD pseudokinases regulate axogenesis and LKB1 stability.
Barnes et al., Portland, United States. In Neural Dev, 2013
RESULTS: We find that STRADα is highly spliced and appears to be the primal STRAD paralog.
Finding a better drug for epilepsy: the mTOR pathway as an antiepileptogenic target.
Cepeda et al., New York City, United States. In Epilepsia, 2012
These include tuberous sclerosis, which is due to mutations in TSC1 or TSC2 genes; mutations in phosphatase and tensin homolog (PTEN) as in Cowden syndrome, polyhydramnios, megalencephaly, symptomatic epilepsy syndrome (PMSE) due to mutations in the STE20-related kinase adaptor alpha (STRADalpha); and neurofibromatosis type 1 attributed to neurofibromin 1 mutations.
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.
STRADalpha deficiency results in aberrant mTORC1 signaling during corticogenesis in humans and mice.
Crino et al., Philadelphia, United States. In J Clin Invest, 2010
aberrant nuclear accumulation of LKB1 caused by STRADalpha deficiency contributes to hyperactivation of mTORC1 signaling and disruption of neuronal lamination during corticogenesis
Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation.
van Aalten et al., Dundee, United Kingdom. In Science, 2010
study describes structure of the core heterotrimeric LKB1-STRADalpha-MO25alpha complex, revealing an unusual allosteric mechanism of LKB1 activation; structure also reveals how mutations in Peutz-Jeghers syndrome & sporadic cancers impair LKB1 function
Allosteric protein kinase regulation by pseudokinases: insights from STRAD.
Sicheri et al., Toronto, Canada. In Sci Signal, 2009
A new structural and functional analysis of the pseudokinase STRAD provides insight into the mechanism by which it allosterically regulates the catalytic function of the protein kinase LKB1 and hints at an evolution from a classical kinase-substrate relationship.
ATP and MO25alpha regulate the conformational state of the STRADalpha pseudokinase and activation of the LKB1 tumour suppressor.
van Aalten et al., Dundee, United Kingdom. In Plos Biol, 2009
ATP and MO25alpha cooperate to maintain STRADalpha in an "active" closed conformation required for LKB1 activation.
Mst4 and Ezrin induce brush borders downstream of the Lkb1/Strad/Mo25 polarization complex.
Clevers et al., Utrecht, Netherlands. In Dev Cell, 2009
These data define a brush border induction pathway downstream of the Lkb1/Strad/Mo25 polarization complex, yet separate from other polarity events.
LKB1 and SAD kinases define a pathway required for the polarization of cortical neurons.
Polleux et al., Chapel Hill, United States. In Cell, 2007
LKB1 polarizing activity requires its association with the pseudokinase Stradalpha and phosphorylation by kinases such as PKA and p90RSK, which transduce neurite outgrowth-promoting cues.
LKB1/STRAD promotes axon initiation during neuronal polarization.
Poo et al., Berkeley, United States. In Cell, 2007
local LKB1/STRAD accumulation and PKA-dependent LKB1 phosphorylation represents an early signal for axon initiation [STRAD protein]
Emerging roles of pseudokinases.
Alessi et al., Dundee, United Kingdom. In Trends Cell Biol, 2006
We review evidence that the pseudokinase STRAD controls the function of the tumour suppressor kinase LKB1 and that a single amino acid substitution within the pseudokinase domain of the tyrosine kinase JAK2 leads to several malignant myeloproliferative disorders.
LKB1-dependent signaling pathways.
Bayascas et al., Dundee, United Kingdom. In Annu Rev Biochem, 2005
We discuss evidence that the cellular localization and activity of LKB1 is controlled through its interaction with a catalytically inactive protein resembling a protein kinase, termed STRAD, and an armadillo repeat-containing protein, named mouse protein 25 (MO25).
LKB1 tumor suppressor protein: PARtaker in cell polarity.
Clevers et al., Utrecht, Netherlands. In Trends Cell Biol, 2004
Recently, mammalian LKB1 was found to be active only in a complex with two other proteins--STRAD and MO25--and to induce complete polarization of intestinal epithelial cells in a cell-autonomous fashion.
Complete polarization of single intestinal epithelial cells upon activation of LKB1 by STRAD.
Clevers et al., Utrecht, Netherlands. In Cell, 2004
We have previously reported the identification and characterization of an LKB1-specific adaptor protein, STRAD, which activates LKB1 and translocates it from nucleus to cytoplasm.
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