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In the two wild type (WT) cases, two novel alterations were detected: a complex deletion of APC and a pathogenic mutation of LAMTOR2. Focusing on WT DT subtype, deep sequencing of CTNNB1, APC and LAMTOR2 was conducted on a retrospective series of 11 WT DT using a targeted approach
identified polymorphisms in LAMTOR2 and LAMTOR3 do not seem to play a relevant role in breast cancer
The ROBLD3 C-A, thorn23 mutation creates a 50SS capable of recruiting an inhibitory U1 snRNP complex leading to a failure of proper 30 end formation and rapid degradation of p14 mRNA.
simulations constitute a multi-dimensional exploration of how EGF-dependent EGFR endocytosis and ERK activation are dynamically affected by scaffolds KSR and MP1, co-regulated by Cbl-CIN85 and Endophilin A1
A complex encoded by the MAPKSP1, ROBLD3, and c11orf59 genes interacts with the Rag GTPases, recruits them to lysosomes, and is essential for mTORC1 activation
Hotair silence activates P16(Ink4a) and P14(ARF) signaling by enhancing miR-218 expression and suppressing Bmi-1 expression, resulting in the suppression of tumorigenesis in HCC.
LAMTOR2 has a role in regulating dendritic cell homeostasis through FLT3-dependent mTOR signalling
Lamtor2 deficiency affects TGFbeta1 sensitivity of Langerhan cells, which is mandatory for their homeostasis and subsequently for their immunological function during contact hypersensitivity.
We show an essential function for late endosomes carrying the p14-MP1 (LAMTOR2/3) complex in focal adhesion dynamics.
The late endosomal adaptor molecule p14 (LAMTOR2) represents a novel regulator of Langerhans cell homeostasis.
Data indicate that LAMTOR3 protein is stabilized by associating with LAMTOR2.
The late endosomal adaptor p14 (also known as LAMTOR2) is one of the components for cellular host defense against the intracellular pathogen Salmonella enterica serovar Typhimurium.
analysis of interactions between kinase scaffold MP1/p14 and its endosomal anchoring protein p18
A combination of cell fractionation, two-dimensional gel electrophoresis and mass spectrometry revealed 31 proteins differentially regulated in p14/ organelles, which were rescued by reexpression of pEGFP-p14 in p14/ endosomes
spatial regulation of MAPK signaling, illustrating how p14 and MP1 collaborate as an endosomal adaptor/scaffold complex
Data report the three-dimensional solution structure of the adaptor protein p14, which includes a profilin-like fold with a central five-stranded beta-sheet sandwiched between alpha-helices.
The product of this gene is highly conserved with a mouse protein associated with the cytoplasmic face of late endosomes and lysosomes. The mouse protein interacts with MAPK scaffold protein 1, a component of the mitogen-activated protein kinase pathway. In humans, a mutation in this gene has been associated with a primary immunodeficiency syndrome, and suggests a role for this protein in endosomal biogenesis. Multiple transcript variants encoding different isoforms have been found for this gene.
MAPKSP1 adaptor protein
, endosomal adaptor protein p14
, late endosomal/lysosomal Mp1-interacting protein
, late endosomal/lysosomal adaptor and MAPK and MTOR activator 2
, mitogen-activated protein-binding protein-interacting protein (MAPBPIP)
, ragulator complex protein LAMTOR2
, roadblock domain containing 3
, roadblock domain-containing protein 3
, mitogen-activated protein-binding protein-interacting protein
, late endosomal/lysosomal MP1 interacting protein
, mitogen activated protein binding protein interacting protein
, mitogen-activated protein binding protein interacting protein
, Mitogen-activated protein-binding protein-interacting protein
, Roadblock domain-containing protein 3
, putative mitogen-activated protein-binding protein-interacting protein