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The product of PRIMA1 functions to organize acetylcholinesterase (AChE) into tetramers, and to anchor AChE at neural cell membranes.
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Hypermethylation of the selected markers (MAL (show MAL Proteins), PRIMA1, PTGDR (show PTGDR Proteins) and SFRP1 (show SFRP1 Proteins)) can result in reduced gene expression and may contribute to the formation of colorectal cancer.
The autophagic potential of PRIMA-1 could be modulated in a different way by the presence of wild type or mutant p53 (show TP53 Proteins).
By using site-directed mutagenesis, the asparagine-43 was identified to be the N-linked glycosylation site of PRiMA. Abolishing glycosylation on mouse PRiMA appeared not to affect its assembly with AChE(T).
A strong association of AChE with PRiMA at the plasma membrane is therefore a feature specific to principal cholinergic neurons that innervate the central nervous system.
PRiMA in neurons has a role in targeting acetylcholinesterase (show AChE Proteins) to membrane rafts
PRiMA-Luc promotor-driven luciferase activity was increased during cell differentiation
These results suggested that a MAP kinase (show MAPK1 Proteins) signaling pathway served as one of the transcriptional regulators in controlling PRiMA gene expression during the neuronal differentiation process.
It interacts with PS1 (show PSEN1 Proteins) and undergoes proteolytic processing.
Elevated expression of muscarinic receptors is responsible for physiological adaptation of PRiMA-deficient developing mice.
the relative content of AChE, BuChE and PRiMA mRNAs were compared in normal and Lama2dy muscle and sciatic nerve
Data show that along the nerve terminus the vast majority of acetylcholinesterase (show AChE Proteins) is anchored by collagen Q that is only produced by the muscle, whereas very minor amounts of AChE are anchored by PRiMA that is produced by motoneurons.
PRiMA expression is predominantly to the cholinergic system and that anchoring of cholinesterases to cell membranes by PRiMA represents a limiting factor for production of the AChE tailed splice variant (AChET)-PRiMA complex.
A peptidic motif of PRiMA1 is defined which is nearly as efficient as the complete extracellular domain of PRiMA for recruitment of acetylcholinesterase (show AChE Proteins) subunits into secreted heteromeric complexes.
expression of PRiMA, as well as PRiMA-associated G(4) AChE, in muscle is suppressed by muscle regulatory factors, muscular activity, and nerve-derived trophic factors
Acetylcholinesterase (show AChE Proteins) associates differently with its anchoring proteins ColQ and PRiMA
PRIMA-1MET targets mouse tumors carrying mutant p53 (show TP53 Proteins)
Proline-rich membrane anchor protein (show CELSR3 Proteins) is necessary to target and/or to stabilize nascent acetylcholinesterase (show AChE Proteins) in neurons.
The product of this gene functions to organize acetylcholinesterase (AChE) into tetramers, and to anchor AChE at neural cell membranes.
acetylcholinesterase membrane anchor precursor PRiMA
, proline-rich membrane anchor 1
, acetylcholinesterase membrane anchor
, proline rich membrane anchor 1-like