Phospho-serine 129
Phospho-serine 129 - Related Videos
10:52
Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation
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Cited by 21 •
2016
Phosphoinositides are signaling lipids whose relative abundance rapidly changes in response to various stimuli. This article describes a method to measure the abundance of phosphoinositides by metabolically labeling cells with 3H-myo-inositol, followed by extraction and deacylation. Extracted glycero-inositides are then separated by high-performance liquid chromatography and quantified by flow scintillation.
01:42
Phosphoinositides and PIPs
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2023
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs. Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
02:59
An In Vitro Assay for Measuring Neutrophil Serine Protease Activity Using a Fluorescent Reporter
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2025
This video demonstrates an in vitro assay to quantify neutrophil serine protease activity in sputum samples. The sample containing secreted protease is incubated with a fluorescent reporter bearing a recognition motif. Cleavage of the motif by the protease enables individual fluorescence emission by the donor and acceptor fluorophore of the reporter, indicating protease activity in the sample.
10:18
A Fast and Reliable Pipeline for Bacterial Transcriptome Analysis Case study: Serine-dependent Gene Regulation in Streptococcus pneumoniae
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Cited by 15 •
2015
This manuscript describes the use of state-of-the-art technology provided by DNA-microarrays. Microarrays provide an overview of the transcriptomic changes in bacteria incurred under a specific condition. Moreover, we highlight the ease by which large amounts of data can be analyzed by using convenient in-house developed software packages.
10:58
PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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Cited by 7 •
2017
Here we present a supported lipid bilayer in the context of a microfluidic platform to study protein-phosphoinositide interactions using a label-free method based on pH modulation.
FAQs
Kinases add phosphate from ATP to serine 129, whereas phosphatases remove it. The opposing activities create a reversible regulatory balance that can alter alpha-synuclein conformation, molecular interactions, and handling inside neurons. Studying this balance helps researchers determine whether changes in phosphorylation accompany altered protein behavior during synucleinopathy-related pathology.
Accumulation of phospho-serine 129 in pathological protein deposits provides a way to identify disease-associated alpha-synuclein pathology. Its presence does not by itself establish whether phosphorylation causes aggregation or results from it. Instead, researchers examine the relationship among phosphorylation, aggregate formation, and neuronal dysfunction to clarify its biological significance.
Phosphorylation at serine 129 can influence alpha-synuclein conformation, interactions with other molecules, and intracellular handling. These changes may affect how the protein behaves in neuronal environments and how it relates to pathological deposits. Consequently, pS129 research connects a specific post-translational modification with broader questions about protein aggregation and neuronal impairment.
Phospho-serine 129 measurements focus on a disease-associated modification rather than alpha-synuclein abundance alone. This distinction can help researchers map pathological deposits and examine whether the modified protein is associated with aggregation or neuronal dysfunction. Such measurements therefore provide modification-specific information that complements broader analyses of alpha-synuclein in neuroscience experiments.
Researchers commonly use pS129 immunostaining and related biochemical assays. Immunostaining helps map where disease-associated deposits occur, while biochemical assays provide complementary measurements of the modified protein in experimental material. Used together, these approaches allow investigators to connect the spatial distribution of pathology with biochemical evidence when examining alpha-synuclein-related disease mechanisms.
Researchers may evaluate pS129 when testing whether phosphorylation patterns reflect pathological alpha-synuclein deposits, neuronal dysfunction, or responses to experimental interventions. Its potential biomarker value comes from its association with disease-related deposits, while therapeutic studies can examine strategies that affect phosphorylation, aggregation, or protein handling. These uses remain subjects of investigation in experimental models.