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Related Concept Videos

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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The Unfolded Protein Response01:37

The Unfolded Protein Response

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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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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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.
These groups modify specific amino acids in a protein....
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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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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Related Experiment Video

Updated: Mar 12, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

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Structural Basis for Selective Interaction between the ESCRT Regulator HD-PTP and UBAP1.

Deepankar Gahloth1, Colin Levy1, Graham Heaven2

  • 1School of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.

Structure (London, England : 1993)
|November 15, 2016
PubMed
Summary
This summary is machine-generated.

The tumor suppressor HD-PTP regulates receptor degradation via ESCRT pathways. Structural studies reveal its unique coiled-coil domain interaction with UBAP1, offering insights for cancer therapies.

Keywords:
coiled-coil structureendosomal ESCRTs regulationmitogenic signaling downregulationtumor suppressor phosphataseubiquitin-dependent trafficking

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Related Experiment Videos

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Cancer Research

Background:

  • Endosomal sorting complexes required for transport (ESCRTs) are crucial for protein degradation.
  • Dysregulation of ESCRT pathways is implicated in cancer progression.
  • HD-PTP phosphatase controls ESCRT-mediated receptor sorting.

Purpose of the Study:

  • To structurally characterize the interaction between HD-PTP and UBAP1.
  • To elucidate the molecular mechanisms regulating ESCRT pathways.
  • To identify potential targets for anticancer therapies.

Main Methods:

  • X-ray crystallography
  • Double electron-electron resonance (DEER) spectroscopy

Main Results:

  • Determined the structure of the HD-PTP coiled-coil domain complexed with UBAP1.
  • Revealed an unexpected open and rigid conformation of the HD-PTP coiled-coil domain.
  • Identified key molecular interactions between HD-PTP and UBAP1.

Conclusions:

  • The HD-PTP:UBAP1 structure provides a molecular basis for their functional cooperation.
  • Findings offer insights into ESCRT pathway regulation in cancer.
  • The study may inform the development of novel anticancer strategies.