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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Protein Kinases and Phosphatases02:54

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Regulation of Nuclear Protein Sorting01:45

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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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.
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Phosphorylation of NLGN4X Regulates Spinogenesis and Synaptic Function.

Alexander W Lehr1,2, Thien A Nguyen1,3, Wenyan Han4

  • 1Receptor Biology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892.

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Summary

Researchers identified a specific phosphorylation site (serine 712) on Neuroligin 4 (NLGN4) proteins. This modification by different kinases impacts synapse structure and function, offering new insights into synaptic plasticity.

Keywords:
autism spectrum disorderneuroliginphosphorylationsex-linkedspine morphologyspinogenesis

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Synaptic Plasticity

Background:

  • Neuroligins (NLGNs) are crucial postsynaptic adhesion molecules that interact with presynaptic neurexins to form and maintain synapses.
  • Five NLGN genes exist in humans (NLGN1-3, NLGN4X, NLGN4Y), with NLGN1-3 conserved in rodents, enabling translational research.
  • Post-translational modifications, particularly phosphorylation, play a key role in modulating NLGN functions temporally and spatially.

Purpose of the Study:

  • To characterize the conserved phosphorylation site serine 712 (S712) on human Neuroligin 4X (NLGN4X) and Neuroligin 4Y (NLGN4Y).
  • To investigate the kinase specificity for NLGN4X and NLGN4Y S712 phosphorylation.
  • To determine the functional consequences of NLGN4X S712 phosphorylation on synaptic structure and function.

Main Methods:

  • Site-directed mutagenesis to identify and study the conserved S712 phosphorylation site.
  • In vitro kinase assays using Protein Kinase A (PKA) and Cyclin-dependent Kinase 5 (Cdk5).
  • Analysis of dendritic spine density and miniature excitatory postsynaptic current (mEPSC) frequency in neurons expressing different NLGN4 variants.

Main Results:

  • Serine 712 (S712) is a conserved phosphorylation site on both NLGN4X and NLGN4Y.
  • Protein Kinase A (PKA) specifically phosphorylates NLGN4X S712, while Cyclin-dependent Kinase 5 (Cdk5) phosphorylates S712 on both NLGN4X and NLGN4Y.
  • Phosphorylation of NLGN4X S712 reduced mature mushroom spine density, whereas unphosphorylated S712 increased spine density and enhanced mEPSC frequency.

Conclusions:

  • NLGN4X and NLGN4Y S712 phosphorylation exhibits kinase-specific regulation, impacting synaptic organization.
  • NLGN4X S712 phosphorylation is a critical regulator of dendritic spine morphology and excitatory synaptic transmission.
  • These findings highlight the importance of specific post-translational modifications in controlling synaptic function and plasticity.