Sort   by:  
 Page size 
ProteomicsMolecular Basis of the mechanisms controlling MASTL - Proteomics analysis of MASTL substrate proteome and phosphorylation state
As part of our study on human MASTL (microtubule-associated serine/threonine kinase-like), we used mass spectrometry (MS)-based proteomics in the aim to unravel novel aspects about MASTL activation, regulation and potential substrates. Specifically, we performed a phosphoproteomics-based kinase assa...
ORGANISM(S): Homo sapiens (Human) 
2020-01-09 | PXD007991 | Pride
Human Lc-msms Mastl 
ProteomicsIn Cellulo Kinase Screen Identifies Novel MASTL Substrates
MASTL (microtubule-associated serine/threonine kinase-like) has emerged as a critical regulator of mitosis and as a potential oncogene in a variety of cancer types. To date, Arpp-19/ENSA are the only known substrates of MASTL. With the cellular roles of MASTL expanding and increased interest in deve...
ORGANISM(S): Homo sapiens (Human) 
2022-08-12 | PXD028678 | Pride
Akt Phospho-peptides Silac Agc kinase Kinase Mastl 
ProteomicsA cell cycle kinase-phosphatase module restrains PI3K- Akt activity in an mTORC1-dependent manner
The AKT-mTOR pathway is a central regulator of cell growth and metabolism. Upon sustained mTOR activity, AKT activity is attenuated by a feedback loop that restrains upstream signaling. However, how cells control the signals that limit AKT activity is not fully understood. Here we show that MASTL/Gr...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2022-11-23 | PXD032796 | Pride
Mastl Phosphosites Mouse Human 
ProteomicsThrombocytopenia-associated mutations in MASTL deregulate global phosphorylation and actin cytoskeleton dynamics in platelets
MASTL, also known as Greatwall, was originally characterized in flies and Xenopus as a mitotic kinase involved in the maintenance of the mitotic state by inhibiting PP2A-B55 complexes. A specific mutation (E167D) in the human MASTL gene was simultaneously linked to autosomal dominant thrombocytopeni...
ORGANISM(S): Mus musculus (Mouse) 
2019-11-12 | PXD009398 | Pride
Platelets Kinase Cell cycle Mastl Phosphoproteomics 
ProteomicsMicrotubule-associated serine/threonine-protein kinase-like (MASTL) surfaceome proteomics analysis
Microtubule-associated serine/threonine-protein kinase-like (MASTL; a.k.a. Greatwall (Gwl) kinase) has an established role in the acceleration of cell cycle progression through inhibition of the PP2A-B55 phosphatase activity. Importantly, MASTL has emerged as a putative oncogene. Especially in breas...
ORGANISM(S): Homo sapiens (Human) 
2022-06-28 | PXD019993 | Pride
Breast cancer Cell contractility Cell migration Silac Surfaceome proteomics Mastl Cell adhesion 
ProteomicsProteome of Human breast cancer cell line (MDA-MB-231) with sileced MASTL vs NT control
MASTL (Microtubule associated serine-threonine kinase-like) is a relatively recently identified mitotic accelerator. There are also indications of its role in cancer progression, especially in breast cancer, but the molecular mechanisms behind this and the cell cycle independent functions of MASTL a...
ORGANISM(S): Homo sapiens (Human) 
2020-04-14 | PXD013757 | Pride
Breast cancer Cell contractility Cell migration Silac Mastl Cell adhesion 
GenomicsGenome-wide RNA analysis of the effects of MASTL silencing in breast cancer cells
Genome-wide RNA analysis of the effects of MASTL silencing in breast cancer cells
PRJNA545096 | ENA
TranscriptomicsGenome-wide RNA analysis of the effects of MASTL silencing in breast cancer cells
The effect of short term (24h and 48h) silencing of MASTL for total transcriptome was studied in human breast cancer cell line (MDA-MB-231). Microtubule-associated serine/threonine-protein kinase-like (MASTL) is a mitosis-accelerating kinase with emerging roles in cancer progression. However, possib...
ORGANISM(S): Homo sapiens 
2020-04-14 | GSE131833 | GEO
UnknownSILAC kinase screen identifies potential MASTL substrates.
Not available
S-EPMC9217955 | biostudies-literature
UnknownMolecular Basis of the Mechanisms Controlling MASTL.
Not available
S-EPMC7000116 | biostudies-literature
Sort   by:  
 Page size