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MASTL encodes a microtubule-associated serine/threonine kinase. Additionally we are shipping MASTL Antibodies (94) and MASTL Kits (8) and many more products for this protein.
Showing 5 out of 6 products:
transient knockdown of MASTL correlates with a decrease in the expression of c-mpl and GpIIb, and reduction of circulating thrombocytes
E2F8 (show E2F8 Proteins) can shorten cisplatin induced G2/M arrest by promoting MASTL mediated mitotic progression in ER+ breast cancer cells, conferring drug resistance.
Using mathematical modelling, this paper confirms that deactivation of MASTL is essential for mitotic exit.
these results established that precise control of MASTL is essential to couple DNA damage to mitosis through the rate of mitotic entry and APC (show APC Proteins)/C activation.
Thus, GWL is a human oncoprotein that promotes the hyperactivation of AKT via the degradation of its phosphatase, PHLPP, in human malignancies.
Thus, Fcp1 (show CTDP1 Proteins) coordinates Cdk1 (show CDK1 Proteins) and Gwl inactivation to derepress PP2A (show PPP2R4 Proteins)-B55 (show MINK1 Proteins), generating a dephosphorylation switch that drives mitosis progression.
Boolean modeling identifies Greatwall/MASTL as an important regulator in the AURKA (show AURKA Proteins) network of neuroblastoma (show ARHGEF16 Proteins).
Data show that siRNA knockdown of Forkhead box M1 (FOXM1 (show FOXM1 Proteins)) or microtubule-associated serine/threonine kinase-like (MASTL) induces radiosensitivity in non-small cell lung cancer (NSCLC).
Mastl upregulation is involved in cancer progression and tumor recurrence after initial cancer therapy
data demonstrate that GWL acts in a pathway with PP2A (show PPP2R4 Proteins) which is essential for prophase I exit and metaphase I microtubule assembly in mouse oocytes.
Taken together our results suggest a hierarchy of phosphatases coordinating Greatwall, Ensa (show ENSA Proteins)/ARPP19 and Cdk (show CDK4 Proteins) substrate dephosphorylation during mitotic exit.
using in vitro dephosphorylation assays, we demonstrate that Mastl promotes persistent MPS1 phosphorylation by inhibiting PP2A (show PPP2R2B Proteins)/B55 (show MINK1 Proteins)-mediated MPS1 dephosphorylation rather than affecting Cdk1 (show CDK1 Proteins) kinase activity. Our findings establish a key regulatory function of the Greatwall kinase/Mastl - PP2A (show PPP2R2B Proteins)/B55 (show MINK1 Proteins) pathway in preventing premature SAC (show ADCY10 Proteins) silencing
Mastl is required for the timely activation of anaphase-promoting complex (show CDC26 Proteins)/cyclosome to allow meiosis I exit and for the rapid rise of Cdk1 (show CDK1 Proteins) activity.
Data show that Mastl (Greatwall)-null cells display mitotic collapse after nuclear envelope breakdown (NEB) characterized by defective chromosome condensation and prometaphase arrest.
Data suggest Greatwall kinase (Gwl) associates with protein phosphatase 1 (show PPP1CB Proteins) (PP1), particularly PP1gamma subunit, which mediates dephosphorylation of Gwl Ser (show SIGLEC1 Proteins)-883; consistent with mitotic activation of Gwl, its association with PP1 is disrupted in mitotic cells; subunits PPP1R3B (show PPP1R3B Proteins) and PPP1R13L (show PPP1R13L Proteins) associate with Gwl; thus, PPP1R3B (show PPP1R3B Proteins) appears to act as cell cycle regulator in oocytes that functions by governing Gwl dephosphorylation.
Full dephosphorylation of Gwl results in complete inactivation of Arpp19 (show ARPP19 Proteins) and ENSA (show ENSA Proteins), and dephosphorylation of mitotic substrates. this feed-back loop irreversibly induces mitotic exit.
study provides evidence that PP1 targets the auto-phosphorylation site of Gwl, resulting in efficient Gwl inactivation; this step is necessary to facilitate subsequent complete dephosphorylation of Gwl by PP2A (show PPP2R2B Proteins)-B55 (show MINK1 Proteins)
we showed that the Gwl nuclear localization is indispensable for the biochemical function of Gwl in promoting mitotic entry.
PP2A (show PPP2R2B Proteins)-B55delta, Greatwall and ARPP19 (show ARPP19 Proteins) are not only required for entry into meiotic divisions, but are also pivotal effectors within the Cdk1 (show CDK1 Proteins) auto-regulatory loop responsible for its independence with respect to the PKA-negative control.
Greatwall kinase and cyclin B-Cdk1 (show CDK1 Proteins) are both critical constituents of M-phase-promoting factor.
inhibition of PP2A (show PPP2R2B Proteins)-B55delta results from Ensa (show ENSA Proteins), that is phosphorylated in mitosis by the protein kinase (show CSNK1D Proteins) Greatwall; this converts Ensa (show ENSA Proteins) into specific inhibitor of PP2A (show PPP2R2B Proteins)-B55delta; this pathway represents a previously unknown element in mitosis control
3 phosphorylation sites (phosphosites) critical to Gwl activation (pT193, pT206, and pS883 in Xenopus laevis) located in evolutionarily conserved domains that differentiate Gwl from related kinases
Coordinated interplays between Plx1 and Gwl are required for reactivation of these kinases from the G(2)/M DNA damage checkpoint and efficient checkpoint recovery.
mitotic entry and maintenance is not only mediated by the activation of cyclin B-Cdc2 but also by the regulation of PP2A (show PPP2R2B Proteins) by GW
This gene encodes a microtubule-associated serine/threonine kinase. Mutations at this locus have been associated with autosomal dominant thrombocytopenia, also known as thrombocytopenia-2. Alternatively spliced transcript variants have been described for this locus.
microtubule-associated serine/threonine-protein kinase-like
, serine/threonine-protein kinase greatwall
, microtubule associated serine/threonine kinase-like
, greatwall protein kinase
, Serine/threonine-protein kinase greatwall
, Microtubule-associated serine/threonine-protein kinase-like