bioRxiv Science⌕ Search

Biology subjects

Evans, G. J. O.

Publications and source records attributed to Evans, G. J. O..

5 recordsLinked to original sources

Neuronal differentiation enhances a cytoplasmic pool of tousled-like kinase 2 (TLK2)

Mental retardation autosomal dominant 57 (MRD57) is a rare neurodevelopmental disorder characterised by delayed language and psychomotor development, intellectual disability, hypotonia, gastrointestinal issues and facial dysmorphia. It is linked to genetic mutations in the serine/threonine kinase TLK2, characterised by haploinsufficiency and in some cases, its loss or impaired kinase function. TLK2 is an established cell cycle regulator that has been extensively studied in mitotic cells. It is upregulated in cancers, driving tumour growth, however, the role of TLK2 in postmitotic neurons is not understood. We therefore aimed to gain insight into how TLK2 mutations cause MRD57 by determining where TLK2 is expressed in the brain and its subcellular localisation during neuronal differentiation. Public human and mouse brain transcriptomic data revealed splice variant diversity in the N-terminus of TLK2, which contains its nuclear localisation sequence (NLS). Using splice-specific in situ hybridisation probes, we observed expression of TLK2 isoforms that contain and lack the NLS in the mouse hippocampus and cerebellum. We confirmed these findings in human SH-SY5Y neuroblastoma cells, and found that neuronal differentiation of these cells enhances a cytoplasmic pool of TLK2 by two mechanisms: nuclear export of full length TLK2 and increased expression of TLK2 splice variants lacking the NLS. Finally, acute stimuli that mimic synaptic activity were sufficient to elicit nuclear export of TLK2. Our data highlight the need to establish the neuronal cytoplasmic substrates of TLK2 and determine how the loss of TLK2 activity in MRD57 might impact their function in the developing and mature brain.

neuroscience↗

Mis-regulation of GSK-3β causes axonal microtubule curling through Shot and Tau

Glycogen Synthase Kinase 3{beta} (GSK-3{beta}) is a key coordinator of neuronal development and maintenance; hyperactive GSK-3{beta} is linked to neurodevelopmental and -degenerative diseases and therefore a promising therapeutic target. In neurons, GSK-3{beta} coordinates the cytoskeleton by phosphorylating microtubule-binding proteins. In this study, we found that tight regulation of GSK-3{beta} kinase activity is required for the maintenance of parallel microtubule bundles in Drosophila and rat axons. Up- or down-regulation of GSK-3{beta} led to axons forming pathological swellings in which microtubule bundles disintegrated into disorganised, curled microtubules. We identified the microtubule bundling proteins Shot and Tau as key GSK-3{beta} targets and found that GSK-3{beta} exerted its regulatory effect on microtubule bundling through them. GSK-3{beta} regulates the ability of Shot and Tau to attach to microtubules and/or the plus-end protein Eb1. Mis-regulation of GSK-3{beta} leads to the loss of Eb1-Shot-mediated guidance of polymerising microtubules into parallel bundles, thus causing disorganisation. We propose microtubule disorganisation as a new explanation for how GSK-3{beta} hyperactivity leads to neurodegeneration and why global inhibition of GSK-3{beta} has not been successful in clinical trials for neuronal disorders.

cell biology↗

The phosphatase Glc7 controls eisosomal response to starvation via posttranslational modification of Pil1

The yeast plasma membrane (PM) is organised into specific subdomains that regulate surface membrane proteins. Surface transporters actively uptake nutrients in particular regions of the PM where they are also susceptible to substrate induced endocytosis. However, transporters also diffuse into distinct subdomains termed eisosomes, where they are protected from endocytosis. Although most nutrient transporter populations are downregulated in the vacuole following glucose starvation, a small pool is retained in eisosomes to provide efficient recovery from starvation. We find the core eisosome subunit Pil1, a Bin, Amphiphysin and Rvs (BAR) domain protein required for eisosome biogenesis, is phosphorylated primarily by the kinase Pkh2. In response to acute glucose starvation, Pil1 is rapidly dephosphorylated. Enzyme localisation and activity screens implicate the phosphatase Glc7 is the primary enzyme responsible for Pil1 dephosphorylation. Both depletion of GLC7 and phospho-ablative or phospho-mimetic mutations of Pil1 correlate with Pil1 phosphorylation status, failure to properly retain transporters in eisosomes, and results in defective starvation recovery. We propose precise posttranslational control of Pil1 modulates nutrient transporter retention within eisosomes depending on extracellular nutrient levels, to maximise recovery following starvation.

cell biology↗

Sodium regulates PLC and IP3R-mediated calcium signalling in invasive breast cancer cells

Intracellular Ca2+ signalling and Na+ homeostasis are inextricably linked via ion channels and co-transporters, with alterations in the concentration of one ion having profound effects on the other. Evidence indicates that intracellular Na+ concentration ([Na+]i) is elevated in breast tumours, and that aberrant Ca2+ signalling regulates numerous key cancer hallmark processes. The present study therefore aimed to determine the effects of Na+ depletion on intracellular Ca2+ handling in metastatic breast cancer cell lines. The relationship between Na+ and Ca2+ was probed using fura-2 and SBFI fluorescence imaging and replacement of extracellular Na+ with equimolar N-methyl-D-glucamine (0Na+/NMDG) or choline chloride (0Na+/ChoCl). In triple-negative MDA-MB-231 and MDA-MB-468 cells and Her2+ SKBR3 cells, but not ER+ MCF-7 cells, 0Na+/NMDG and 0Na+/ChoCl resulted in a slow, sustained depletion in [Na+]i that was accompanied by a rapid and sustained increase in intracellular Ca2+ concentration ([Ca2+]i). Application of La3+ in nominal Ca2+-free conditions had no effect on this response, ruling out reverse-mode NCX activity and Ca2+ entry channels. Moreover, the Na+-linked [Ca2+]i increase was independent of membrane potential hyperpolarisation (NS-1619), but was inhibited by pharmacological blockade of IP3 receptors (2-APB), phospholipase C (PLC, U73122) or following depletion of endoplasmic reticulum Ca2+ stores (cyclopiazonic acid). Thus, Na+ is linked to PLC/IP3-mediated activation of endoplasmic reticulum Ca2+ release in metastatic breast cancer cells and this may have an important role in breast tumours where [Na+]i is perturbed.

cancer biology↗

JNK signalling regulates antioxidant responses in neurons

Reactive oxygen species (ROS) are generated during physiological bouts of synaptic activity and as a consequence of pathological conditions in the central nervous system. How neurons respond to and distinguish between ROS in these different contexts is currently unknown. In Drosophila mutants with enhanced JNK activity, lower levels of ROS are observed and these animals are resistant to both changes in ROS and changes in synapse morphology induced by oxidative stress. In wild type flies, disrupting JNK-AP-1 signalling perturbs redox homeostasis suggesting JNK activity positively regulates neuronal antioxidant defense. We validated this hypothesis in mammalian neurons, finding that JNK activity regulates the expression of the antioxidant gene Srxn-1, in a c-Jun dependent manner. We describe a conserved adaptive role for neuronal JNK in the maintenance of redox homeostasis that is relevant to several neurodegenerative diseases.

neuroscience↗