Giulia Favetta

ORCID: 0009-0002-2397-9218
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About
Contact & Profiles
Research Areas
  • Parkinson's Disease Mechanisms and Treatments
  • Biotin and Related Studies
  • Microtubule and mitosis dynamics
  • Neuroscience and Neuropharmacology Research
  • Nuclear Structure and Function
  • Cellular transport and secretion
  • Nerve injury and regeneration
  • Skin and Cellular Biology Research
  • Mitochondrial Function and Pathology
  • Autophagy in Disease and Therapy
  • Plant nutrient uptake and metabolism
  • Ubiquitin and proteasome pathways
  • Fungal and yeast genetics research
  • 14-3-3 protein interactions
  • Photosynthetic Processes and Mechanisms

University of Padua
2022-2024

Parkinson’s disease (PD) is a multisystemic disorder that manifests through motor and non-motor symptoms. Motor dysfunction the most debilitating it caused by degeneration of dopamine-producing neurons in substantia nigra pars compacta (SNpc). A body evidence indicates synapse demise precedes years neuronal death. Still, early synaptic dysfunctions PD are poorly deciphered.Here we combined literature metanalysis, proteomics phosphoproteomics with biochemical, imaging electrophysiological...

10.7554/elife.95987.1 preprint EN 2024-04-09

P21 activated kinase 6 (PAK6) is a serine-threonine with physiological expression enriched in the brain and overexpressed number of human tumors. While role PAK6 cancer cells has been extensively investigated, function context poorly understood. Our previous work uncovered link between Parkinson's disease (PD)-associated LRRK2, controlling LRRK2 activity subcellular localization via phosphorylation 14-3-3 proteins. Here, to gain more insights into function, we performed protein-protein...

10.1038/s41419-024-07124-4 article EN cc-by Cell Death and Disease 2024-10-17

Mutations in leucine-rich repeat kinase 2 (LRRK2) are a common cause of inherited and sporadic Parkinson’s disease (PD) previous work suggests that dephosphorylation LRRK2 at cluster heterologous phosphosites is associated to disease. We have previously reported subunits the PP1 PP2A classes phosphatases as well PAK6 regulators dephosphorylation. therefore hypothesized may functional link with LRRK2’s phosphatases. To investigate this, we used PhosTag gel electrophoresis purified proteins...

10.3389/fnmol.2023.1269387 article EN cc-by Frontiers in Molecular Neuroscience 2023-12-18

Abstract Alterations in the dopamine catabolic pathway are known to contribute degeneration of nigrostriatal neurons Parkinson’s disease (PD). The progressive cellular buildup highly reactive intermediate 3,4-dihydroxyphenylacetaldehye (DOPAL) generates protein cross-linking, oligomerization PD-linked αSynuclein (αSyn) and imbalance quality control. In this scenario, autophagic cargo sequestome-1 (SQSTM1/p62) emerges as a target DOPAL-dependent accumulation cytosolic clusters. Although...

10.1038/s41419-024-06763-x article EN cc-by Cell Death and Disease 2024-06-18

Abstract Parkinson’s disease (PD) is a multisystemic disorder that manifests through motor and non-motor symptoms. Motor dysfunction the most debilitating it caused by degeneration of dopamine-producing neurons in substantia nigra pars compacta (SNpc). A body evidence indicates synapse demise precedes years neuronal death. Still, early synaptic dysfunctions PD are poorly deciphered. Here we combined literature metanalysis, proteomics phosphoproteomics with biochemical, imaging...

10.1101/2022.10.31.514622 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2022-11-01

Parkinson’s disease (PD) is a multisystemic disorder that manifests through motor and non-motor symptoms. Motor dysfunction the most debilitating it caused by degeneration of dopamine-producing neurons in substantia nigra pars compacta (SNpc). A body evidence indicates synapse demise precedes years neuronal death. Still, early synaptic dysfunctions PD are poorly deciphered.Here we combined literature metanalysis, proteomics phosphoproteomics with biochemical, imaging electrophysiological...

10.7554/elife.95987 preprint EN 2024-04-09

P21 activated kinase 6 (PAK6) is a serine-threonine with physiological expression enriched in the brain and overexpressed number of human tumors. While role PAK6 cancer cells has been extensively investigated, function context poorly understood. Our previous work uncovered link between Parkinson's disease (PD)-associated LRRK2, controlling LRRK2 activity subcellular localization via phosphorylation 14-3-3 proteins. Here, to gain more insights into function, we performed protein-protein...

10.1101/2024.04.11.589075 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-04-14

<title>Abstract</title> P21 activated kinase 6 (PAK6) is a serine-threonine with physiological expression enriched in the brain and overexpressed number of human tumors. While role PAK6 cancer cells has been extensively investigated, function context poorly understood. Our previous work uncovered link between Parkinson’s disease (PD)-associated LRRK2, controlling LRRK2 activity subcellular localization <italic>via</italic> phosphorylation 14-3-3 proteins. Here, to gain more insights into...

10.21203/rs.3.rs-4262638/v1 preprint EN cc-by Research Square (Research Square) 2024-05-20
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