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    STRADA STE20 related adaptor alpha [ Homo sapiens (human) ]

    Gene ID: 92335, updated on 17-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Two further cases of polyhydramnios, megalencephaly, and symptomatic epilepsy syndrome, caused by a truncating variant in STRADA.

    Two further cases of polyhydramnios, megalencephaly, and symptomatic epilepsy syndrome, caused by a truncating variant in STRADA.
    Alsaif HS, Khashab HYEL, Alkuraya FS.

    07/10/2021
    Type II Binders Targeting the ""GLR-Out"" Conformation of the Pseudokinase STRADalpha.

    Type II Binders Targeting the "GLR-Out" Conformation of the Pseudokinase STRADĪ±.
    Smith RHB, Khan ZM, Ung PM, Scopton AP, Silber L, Mack SM, Real AM, Schlessinger A, Dar AC., Free PMC Article

    05/15/2021
    We identified for the first time a homozygous point mutation in STRADA causing PMSE. Additional bi-allelic mutations related to PMSE thus far have not been observed in Baylor approximately 6,000 consecutive clinical WES cases, supporting the rarity of this disorder.

    Whole exome sequencing identifies the first STRADA point mutation in a patient with polyhydramnios, megalencephaly, and symptomatic epilepsy syndrome (PMSE).
    Bi W, Glass IA, Muzny DM, Gibbs RA, Eng CM, Yang Y, Sun A.

    10/28/2017
    aberrant nuclear accumulation of LKB1 caused by STRADalpha deficiency contributes to hyperactivation of mTORC1 signaling and disruption of neuronal lamination during corticogenesis

    STRADalpha deficiency results in aberrant mTORC1 signaling during corticogenesis in humans and mice.
    Orlova KA, Parker WE, Heuer GG, Tsai V, Yoon J, Baybis M, Fenning RS, Strauss K, Crino PB., Free PMC Article

    05/31/2010
    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

    Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation.
    Zeqiraj E, Filippi BM, Deak M, Alessi DR, van Aalten DM., Free PMC Article

    01/25/2010
    ATP and MO25alpha cooperate to maintain STRADalpha in an "active" closed conformation required for LKB1 activation.

    ATP and MO25alpha regulate the conformational state of the STRADalpha pseudokinase and activation of the LKB1 tumour suppressor.
    Zeqiraj E, Filippi BM, Goldie S, Navratilova I, Boudeau J, Deak M, Alessi DR, van Aalten DM., Free PMC Article

    01/21/2010
    These data define a brush border induction pathway downstream of the Lkb1/Strad/Mo25 polarization complex, yet separate from other polarity events.

    Mst4 and Ezrin induce brush borders downstream of the Lkb1/Strad/Mo25 polarization complex.
    ten Klooster JP, Jansen M, Yuan J, Oorschot V, Begthel H, Di Giacomo V, Colland F, de Koning J, Maurice MM, Hornbeck P, Clevers H.

    01/21/2010
    STRADalpha.MO25alpha complexes containing LKB1 variants were equally effective at phosphorylating and activating AMPK, BRSK1, and BRSK2

    C-terminal phosphorylation of LKB1 is not required for regulation of AMP-activated protein kinase, BRSK1, BRSK2, or cell cycle arrest.
    Fogarty S, Hardie DG., Free PMC Article

    01/21/2010
    LKB1 deacetylation is regulated by SIRT1 and that this in turn influences its intracellular localization, association with STRAD, kinase activity, and ability to activate AMPK.

    SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation.
    Lan F, Cacicedo JM, Ruderman N, Ido Y., Free PMC Article

    01/21/2010
    identify a multifactored mechanism to control LKB1 localization, and they suggest that the STRADbeta-LKB1 complex might possess unique functions in the nucleus

    STRADalpha regulates LKB1 localization by blocking access to importin-alpha, and by association with Crm1 and exportin-7.
    Dorfman J, Macara IG., Free PMC Article

    01/21/2010
    Several novel splice isoforms of STRADalpha that differentially affect the kinase activity, complex assembly, subcellular localization of LKB1 and the activation of the LKB1-dependent AMPK pathway were discovered.

    Novel splice isoforms of STRADalpha differentially affect LKB1 activity, complex assembly and subcellular localization.
    Marignani PA, Scott KD, Bagnulo R, Cannone D, Ferrari E, Stella A, Guanti G, Simone C, Resta N.

    01/26/2010
    Identification and characterization of an LKB1-specific adaptor protein and substrate, STRAD. Results imply that STRAD plays a key role in regulating the tumor suppressor activities of LKB1.

    Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD.
    Baas AF, Boudeau J, Sapkota GP, Smit L, Medema R, Morrice NA, Alessi DR, Clevers HC., Free PMC Article

    01/21/2010
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