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SPAK is a powerful regulator of peptide transporters PEPT1 and PEPT2
aberrant nuclear accumulation of LKB1 (show STK11 Proteins) caused by STRADalpha deficiency contributes to hyperactivation of mTORC1 signaling and disruption of neuronal lamination during corticogenesis
Several novel splice isoforms of STRADalpha that differentially affect the kinase activity, complex assembly, subcellular localization of LKB1 (show STK11 Proteins) and the activation of the LKB1 (show STK11 Proteins)-dependent AMPK (show PRKAA1 Proteins) pathway were discovered.
study describes structure of the core heterotrimeric LKB1 (show STK11 Proteins)-STRADalpha-MO25alpha (show CAB39 Proteins) complex, revealing an unusual allosteric mechanism of LKB1 (show STK11 Proteins) activation; structure also reveals how mutations in Peutz-Jeghers syndrome & sporadic cancers impair LKB1 (show STK11 Proteins) function
Identification and characterization of an LKB1 (show STK11 Proteins)-specific adaptor protein and substrate, STRAD. Results imply that STRAD plays a key role in regulating the tumor suppressor activities of LKB1 (show STK11 Proteins).
identify a multifactored mechanism to control LKB1 (show STK11 Proteins) localization, and they suggest that the STRADbeta-LKB1 (show STK11 Proteins) complex might possess unique functions in the nucleus
LKB1 (show STK11 Proteins) deacetylation is regulated by SIRT1 (show SIRT1 Proteins) and that this in turn influences its intracellular localization, association with STRAD, kinase activity, and ability to activate AMPK (show PRKAA1 Proteins).
STRADalpha.MO25alpha complexes containing LKB1 (show STK11 Proteins) variants were equally effective at phosphorylating and activating AMPK (show PRKAA1 Proteins), BRSK1 (show BRSK1 Proteins), and BRSK2 (show BRSK2 Proteins)
These data define a brush border induction pathway downstream of the Lkb1 (show STK11 Proteins)/Strad/Mo25 (show CAB39 Proteins) polarization complex, yet separate from other polarity events.
ATP and MO25alpha (show CAB39 Proteins) cooperate to maintain STRADalpha in an "active" closed conformation required for LKB1 (show STK11 Proteins) activation.
Quantitative PCR revealed significantly reduced LKB1 (show STK11 Proteins), MO25alpha (show CAB39 Proteins), and STRADbeta mRNA in LKB1 (show STK11 Proteins)(-/-) muscle. These findings demonstrate that the LKB1 (show STK11 Proteins)-MO25 (show CAB39 Proteins)-STRAD complex is the principal AMPKK in skeletal muscle.
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.
protein kinase LYK5
, STE20-related kinase adapter protein alpha
, STE20-related kinase adaptor alpha
, STE20-related kinase adapter protein alpha-like
, STE20-like pseudokinase
, STRAD alpha
, serologically defined breast cancer antigen NY-BR-96
, STE20-related adapter protein