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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
These groups modify specific amino acids in a protein.
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Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...

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Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
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Published on: May 18, 2009

Characterizing the novel protein p33MONOX.

Manisha Mishra1, Noriko Inoue, Klaus Heese

  • 1Department of Molecular and Cell Biology, Nanyang Technological University, Singapore.

Molecular and Cellular Biochemistry
|December 15, 2010
PubMed
Summary
This summary is machine-generated.

The novel protein p33MONOX inhibits amyloid precursor protein and Bcl2 phosphorylation while activating Mapk1/3. This protein localizes to the hippocampus and interacts with COBRA1, NOL12, and PRNP, suggesting a role in neuronal growth cone guidance.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • The protein p33MONOX (p33Monooxygenase) is newly identified.
  • Its role in cellular processes, particularly in neuronal development, is largely unknown.

Purpose of the Study:

  • To characterize the novel protein p33MONOX.
  • To investigate its cellular localization, protein interactions, and functional effects in neuronal cells.

Main Methods:

  • Over-expression of p33MONOX in neuroblastoma cells.
  • Cell biology techniques for protein localization in mouse hippocampus.
  • Yeast-two-hybrid screening, co-immunoprecipitation, and bioinformatics for interaction studies.

Main Results:

  • p33MONOX inhibits phosphorylation of amyloid precursor protein (App) and B-cell lymphoma 2 (Bcl2).
  • p33MONOX enhances activation of mitogen-activated protein kinase 1/3 (Mapk1/3).
  • p33MONOX localizes to the cytoplasm of hippocampal pyramidal neurons and interacts with COBRA1, NOL12, and PRNP.

Conclusions:

  • p33MONOX possesses a flavine-containing monooxygenase (FMO)-1 motif, linking it to the MICALs protein family.
  • p33MONOX may regulate pre- and post-transcriptional processes involved in growth cone guidance.