Highlights We conducted a narrative review of articles on mental health aspects of children and adolescents during the COVID-19 pandemic and lockdown. Most studies are cross-sectional in nature. Findings show that quality and magnitude of impact is determined by vulnerability factors like developmental age, educational status, pre-existing mental health condition, being economically underprivileged or being quarantined due to infection or fear of infection. There is a crucial requirement for planning longitudinal and developmental studies, and evidence based elaborative strategies to cater to mental health needs of the vulnerable children and adolescents during and after the pandemic by mobilising direct and digital collaborative networks.

Golgi fragmentation occurs in neurons of patients with Alzheimer's disease (AD), but the underlying molecular mechanism causing the defects and the subsequent effects on disease development remain unknown. In this study, we examined the Golgi structure in APPswe/PS1ΔE9 transgenic mouse and tissue culture models. Our results show that accumulation of amyloid beta peptides (Aβ) leads to Golgi fragmentation. Further biochemistry and cell biology studies revealed that Golgi fragmentation in AD is caused by phosphorylation of Golgi structural proteins, such as GRASP65, which is induced by Aβ-triggered cyclin-dependent kinase-5 activation. Significantly, both inhibition of cyclin-dependent kinase-5 and expression of nonphosphorylatable GRASP65 mutants rescued the Golgi structure and reduced Aβ secretion by elevating α-cleavage of the amyloid precursor protein. Our study demonstrates a molecular mechanism for Golgi fragmentation and its effects on amyloid precursor protein trafficking and processing in AD, suggesting Golgi as a potential drug target for AD treatment.Golgi stacking | APP processing | GRASP55 | amyloidogenic

Background:The neural cell adhesion molecule L1 is important in the developing and adult nervous system. Results: L1 stimulation leads to sumoylation and proteolytic processing of L1 and translocation of a sumoylated transmembrane fragment to the nucleus. Conclusion: Sumoylation and nuclear localization of the L1 fragment are required for L1-dependent functions. Significance: Unraveling the molecular mechanisms underlying L1-activated cellular responses helps understanding L1-linked disorders.

The Golgi apparatus is an essential cellular organelle for post-translational modifications, sorting, and trafficking of membrane and secretory proteins. Proper functionality of the Golgi requires the formation of its unique cisternal-stacking morphology. The Golgi structure is disrupted in a variety of neurodegenerative diseases, suggesting a common mechanism and contribution of Golgi defects in neurodegenerative disorders. A recent study on Alzheimer's disease (AD) revealed that phosphorylation of the Golgi stacking protein GRASP65 disrupts its function in Golgi structure formation, resulting in Golgi fragmentation. Inhibiting GRASP65 phosphorylation restores the Golgi morphology from Aβ-induced fragmentation and reduces Aβ production. Perturbing Golgi structure and function in neurons may directly impact trafficking, processing, and sorting of a variety of proteins essential for synaptic and dendritic integrity. Therefore, Golgi defects may ultimately promote the development of AD. In the current review, we focus on the cellular impact of impaired Golgi morphology and its potential relationship to AD disease development.