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The direct cleavage of APLP1 is a novel feature of the gamma-secretase.
Results provide direct evidence that APLP1 functions as a neuronal zinc-dependent adhesion protein and allow a more detailed understanding of the molecular mechanisms driving the formation of APLP1 adhesion platforms.
The results show that in cognitively normal young adults carrying APlp1 mutations showed different spontaneous brain activity patterns without cerebral structural differences.
These data reveal a conserved mechanism for the binding of APP-family proteins to HS and imply a specific regulatory role of HS modifications in the biology of APP and APP-like proteins.
APLP1 and APLP2, behave similarly to APP in that they both associate with assembled NMDA receptors in the endoplasmic reticulum
CSF levels of 3 endogenous peptides derived from APLP1 (APL1beta25, APL1beta27 and APL1beta28) were decreased in Down syndrome.
APLP1 has a regulatory role in the nuclear translocation of APP family intracellular domains due to the sequestration of Fe65.
[review] APP and its mammalian homologs, amyloid precursor-like proteins APLP1 and APLP2, participate under physiological conditions via trans-cellular dimerization in synaptogenesis.
APLP1 binds the II-III loop of the Ca(v)2.3 calcium channel and that this binding promotes internalization of the channel.
Both APLP1 and APLP2, form transcriptionally active triple protein complexes with Mint3 and transcriptional co-activators Taz andYap.
The 2.1 A resolution electron density map reveals phosphate ions that are bound to the protein surface. Mutational analysis shows that protein residues interacting with the phosphate ions are also involved in heparin binding.
Human cerebrospinal fluid contains three APLP1-derived Abeta-like peptides that are generated by beta- and gamma-cleavages at a concentration of approximately 4.5 nM.
APLP1 and APLP2 are processed by the gamma-secretase in a Presenilin 1-dependent manner and the extreme carboxyl-terminal fragments produced by this processing (APP-like Intracellular Domain) are able to enhance Fe65-dependent gene activation
APLP1 does not undergo the same type of regulated processing as APP and APLP2.
APLP1 and APLP2 and APP are processed similarly to act via the same nuclear target and are regulated by BACE 1 in neurons
APLP-1 and APLP-2 are processed by alpha- and gamma-secretase-like cleavages, and their intracellular domains can be released by cleavage at epsilon-sites. APLP-2 processing appears to be the most elaborate and to involve alternative cleavage sites.
The 5' UTR of the Aplp1 gene lacks any type of CAGA box. This may explain its inability to form amyloid plaques.
APLP1 affects the endocytosis of APP and makes more APP available for alpha-secretase cleavage
These results suggest a possible role of APLP1 in regulation of alpha2A-adrenergic receptor trafficking.
APLP1 is differentially upregulated in gastrointestinal neuroendocrine tumours and may be important for the dissemination of small intestinal carcinoids
APLP1 exhibits synaptogenic activity, involving trans-synaptic dimerization. APLP1 knock-out mice show impaired basal transmission and a reduced mEPSC frequency.
Results suggest that APLP1 deficiency on its own does not lead to defects in synaptic plasticity, but affects synaptic transmission and network inhibition in the dentate gyrus
[review] A role of APP and its two closely related homologues APLP1 and APLP2 has been determined in various aspects of nervous system development and function, in particular, for synapse formation and function.
findings demonstrated that NB-2 interacts with APLP and that both NB-2 and APLP1 are localized at presynaptic sites, suggesting that NB-2 associates with APLP1 in a cis manner on the presynaptic membrane
Crystal structure of the E2 domain of amyloid precursor protein-like protein 1 in complex with sucrose octasulfate.
Cytoplasmic polyadenylation element (CPE) binding factor binds the small intracellular domain (ICD) of APLP1.
The results demonstrated that cell viability and neurite outgrowth of N2a cells undergoing knockdown of Aplp1 were significantly reduced, compared with N2a cells undergoing knockdown of either App or Aplp2.
This gene encodes a member of the highly conserved amyloid precursor protein gene family. The encoded protein is a membrane-associated glycoprotein that is cleaved by secretases in a manner similar to amyloid beta A4 precursor protein cleavage. This cleavage liberates an intracellular cytoplasmic fragment that may act as a transcriptional activator. The encoded protein may also play a role in synaptic maturation during cortical development. Alternatively spliced transcript variants encoding different isoforms have been described.
amyloid-like protein 1
, amyloid beta (A4) precursor-like protein 1
, amyloid-like protein 1-like
, amyloid precursor-like protein 1