p(HGNC:DNM1)

Entity

Name

DNM1

Namespace

HGNC

Namespace Version

20180215

Namespace URL

https://arty.scai.fraunhofer.de/artifactory/bel/namespace/hgnc/hgnc-20180215.belns

APP processing in Alzheimer's disease

This document contains the curation of the review article Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system by Taly et al. 2009

The cytoplasmic domain of the alpha4 nAChR subunit binds the scaffold protein 14-3-3η and the Ca2+ sensor visinin-like protein 1 (ReF. 69), and the beta2 subunit interacts with several cytoskeletal proteins, such as tubulin, dynamin and clathrin, and with G protein systems that are involved in intracellular signalling pathways70. PubMed:19721446

The cytoplasmic domain of the alpha4 nAChR subunit binds the scaffold protein 14-3-3η and the Ca2+ sensor visinin-like protein 1 (ReF. 69), and the beta2 subunit interacts with several cytoskeletal proteins, such as tubulin, dynamin and clathrin, and with G protein systems that are involved in intracellular signalling pathways70. PubMed:19721446

The amount of monomeric tau entering neurons, as measured by total fluorescent intensity of intracellular monomeric tau-pHrodo vesicles, was significantly reduced by dynamin inhibition, as shown at 1 and 3 hr after the addition of extracellular tau (Figure 4B) PubMed:29590627

The effect of dynamin inhibition on the entry of aggregated tau was more pronounced than on monomeric tau (Figures 4D–4F). The total fluorescent intensity of intracellular aggregated taupHrodo was consistently reduced by more than 70% at 1 and 3 hr after tau addition (Figure 4E), and the number of taupHrodo- positive objects was reduced by 95% (Figure 4F) PubMed:29590627

Conversely, dynamin inhibition significantly reduced the entry of aggregated tau, with no significant effects of Cytochalasin D (Figure S6) at this relatively high molar concent of aggregated tau PubMed:29590627