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Morais, V. A.

Publications and source records attributed to Morais, V. A..

5 recordsLinked to original sources

Revisiting Stress Granule Transcriptomes Suggests Mitochondrial RNA Enrichment Despite Methodological Bias

Stress granules (SGs) are dynamic, membraneless cytoplasmic condensates that form in response to diverse cellular stressors. Although proposed to modulate stress responses by selectively sequestering proteins and RNAs, their precise molecular composition and function remain unclear. Reported SG transcriptomes differ substantially due to methodological discrepancies, notably between differential centrifugation (DC) and proximity labeling (PL). Here, we reanalyse publicly available human SG transcriptomes across multiple stressors, cell types, and isolation strategies. DC-based profiles were strongly shaped by RNA length, consistent with a physical bias inherent to the sedimentation-based separation. Correcting for this effect reveals limited concordance between studies. Mitochondrially encoded RNAs nonetheless consistently stand out as a distinctively regulated transcript class, without a uniform direction of enrichment/depletion across datasets, and with a modest but significant enrichment in our consensus SG signature. Immunofluorescence experiments further support, without definitively demonstrating, sequestration of mitochondrial dsRNA by SGs upon stress. Since leakage of mitochondrial nucleic acids is a well-characterised damage-associated molecular pattern linked to inflammation, their sequestration in SGs suggests a potential role in modulating immune-related stress responses. These findings refine our understanding of SG composition, underscore the need to control for technical artifacts in SG isolation, and provide a framework to distinguish genuine biological signals from methodological noise in SG research.

cell biology↗

YME1L1 is Dispensable for T Lymphocyte Activation Despite its Upregulation and Activity

Mitochondrial dynamics are critical for T cell activation, differentiation, and survival. The inner mitochondrial membrane ATP-dependent metalloprotease YME1L1 regulates proteostasis and the processing of optic atrophy protein 1 (OPA1), thereby shaping mitochondrial cristae architecture and respiratory function in many cell types. Whether YME1L1 fulfils similar roles in lymphocytes remains unknown. Here, we examined YME1L1 function in T cells using conditional knockout mice lacking YME1L1 in lymphocytes (YME1L1{Delta}TB). YME1L1 expression increased upon T cell activation, yet its absence did not alter thymic development, peripheral T cell homeostasis, or the proportions of naive, memory, and regulatory subsets. T cell activation and proliferation in response to anti-CD3{varepsilon} stimulation were also unaffected. Mitochondrial parameters such as mass, membrane potential, and reactive oxygen species production, were largely preserved, with only modest, transient increases in oxidative stress detected in CD4 T cells lacking YME1L1. Electron microscopy revealed no major changes in mitochondrial size or roundness but showed increased cristae branching and reduced tortuosity, indicating subtle alterations in ultrastructure. Additionally, {gamma}{delta} T cells in YME1L1{Delta}TB mice exhibited a mild shift toward interferon-{gamma}-producing phenotypes at the expense of interleukin-17-producing subsets. Collectively, our data indicate that YME1L1, despite its requirement for OPA1 cleavage, is dispensable for T cell development and acute activation but may contribute to fine-tune mitochondrial architecture and {gamma}{delta} T cell effector programming. These findings highlight cell-type-specific redundancies in mitochondrial quality control and underscore the value of negative data in refining the understanding of mitochondrial regulation in immune cells.

immunology↗

Mitochondria at synapse utilize fatty acids as a bioenergetic fuel source

Mitochondria process glucose, glutamine, and fatty acids (FAs) to produce ATP, with fuel choice dependent on tissue-specific metabolism. The brain harbors two distinct mitochondrial populations--synaptic and non-synaptic. While glucose is the primary fuel for brain bioenergetics, the role of FAs remains elusive. A preliminary proteomic analysis revealed that synaptic mitochondria favor FA metabolism, corroborated by biochemical and respiratory assays showing their higher capacity for {beta}-oxidation and greater respiratory flexibility compared to non-synaptic mitochondria. Additionally, synaptic mitochondria showed higher capacity for FA uptake and less susceptibility to inhibition of the carnitine shuttle system. In neurons, oxygen consumption rate assays indicate that medium to long-chain FA fueling enhances neuronal respiratory flexibility and ATP content, while whole-cell patch-clamp recordings show that long-chain FA fueling sustains increased pre-synaptic activity. Our findings demonstrate that FAs can contribute effectively to synaptic metabolism under normal physiological conditions, where there is a constant demand for energy.

cell biology↗

Bioenergetic signature of Synaptic mitochondria

Synaptic transmission is the most energy-demanding processes in the brain and here we show that mitochondria have developed specific properties to efficiently support neurotransmission. It is a known fact that mitochondria at synapses need to be able to deal with a dynamic range of energetic needs overtime and to adapt between resting and high stimulation conditions. However, how mitochondria are adjusting to this requirement was not yet clear. Here, we show that synaptic mitochondria have a distinct bioenergetic profile presenting a stronger ability to respond to respiratory stimulus. These features are explained by a dichotomic Complex I activity pattern where synaptic mitochondria present a decreased enzymatic activity of individual Complex I, yet mitochondria at synapse present a dramatically enhanced Complex I+III combined activity. These bioenergetics features may endow synaptic mitochondria with the necessary mechanisms to adapt to the flexible bioenergetic environment present at synapses.

cell biology↗

PINK1-G411S mutant increases kinase stability and enhances mitochondrial-linked functions

PINK1, a mitochondria targeted Serine/Threonine kinase, regulates ATP production by phosphorylating the Complex I subunit NdufA10. However, when in the presence of depolarized mitochondria, PINK1 phosphorylates ubiquitin and Parkin triggering mitochondria clearance. Mutations in PINK1 have been linked to early-onset recessive familial forms of Parkinsons disease (PD). Deficits in Complex I enzymatic activity and an increase in oxidative damage have been identified in multiple brain regions of PD patients. Unravelling how PINK1 activity regulates mitochondria fate is pivotal. In the present study we characterized how human PD-related PINK1 mutants affect major PINK1 functions. Using molecular dynamics, we gain mechanistic insight into how specific mutations alter the tertiary structure and stability of PINK1s ATP-binding pocket, leading to an increased rigidity and stability. More importantly, we report a structural explanation for the enhanced kinase function of the PINK1-G411S mutant.

cell biology↗