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Related Concept Videos

Golgi Matrix Proteins01:12

Golgi Matrix Proteins

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Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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GPI Anchoring of Proteins in the ER Membrane01:29

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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
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Cytoskeletal Accessory Proteins01:13

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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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HO-2 Pockets Myristoylated Gag.

Marilyn D Resh1

  • 1Cell Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, Box 143, New York, NY 10065, USA.

Cell Host & Microbe
|February 10, 2017
PubMed
Summary

Viral and cellular N-myristoylated proteins bind membranes. Heme oxygenase-2 sequesters myristate, inhibiting N-myristoylated protein function by trapping the myristate molecule.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • N-myristoylated proteins are crucial for viral and cellular functions.
  • Membrane association of these proteins is regulated by myristate.
  • Dysregulation of N-myristoylated protein function is implicated in various diseases.

Purpose of the Study:

  • To investigate the mechanism of myristate sequestration by cellular proteins.
  • To identify cellular factors that regulate N-myristoylated protein activity.
  • To explore potential therapeutic targets for diseases involving N-myristoylated proteins.

Main Methods:

  • Biochemical assays to study protein-myristate interactions.
  • Site-directed mutagenesis to identify key residues in heme oxygenase-2.

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  • Cellular assays to assess the impact on N-myristoylated protein function.

    • Main Results:

    • A novel myristate binding site was identified in heme oxygenase-2.
    • Heme oxygenase-2 acts as a myristate 'trap', sequestering it from N-myristoylated proteins.
    • This sequestration inhibits the membrane binding and function of N-myristoylated proteins.

    Conclusions:

    • Heme oxygenase-2 plays a regulatory role in N-myristoylated protein function.
    • Targeting the myristate binding site of heme oxygenase-2 could offer therapeutic strategies.
    • Understanding myristate dynamics is key to controlling protein localization and function.