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Related Concept Videos

Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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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Nuclear Localization Signals and Import01:46

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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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Protein Transport to the Stroma01:24

Protein Transport to the Stroma

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Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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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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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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STING1 in Different Organelles: Location Dictates Function.

Ruoxi Zhang1, Rui Kang1, Daolin Tang1

  • 1Department of Surgery, University of Texas (UT) Southwestern Medical Center, Dallas, TX, United States.

Frontiers in Immunology
|April 4, 2022
PubMed
Summary
This summary is machine-generated.

Stimulator of interferon response cGAMP interactor 1 (STING1) protein moves to various organelles, influencing immune responses and other cell functions. Understanding STING1

Keywords:
STING1adaptor proteinautophagycell deathimmunityorganelle

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Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Stimulator of interferon response cGAMP interactor 1 (STING1), also known as TMEM173, is a key immune adaptor protein.
  • STING1 regulates signal crosstalk involved in numerous physiological and pathological processes.
  • While STING1 is known to traffic from the endoplasmic reticulum (ER) to the Golgi apparatus upon DNA-triggered activation, its organelle-specific functions are increasingly recognized.

Purpose of the Study:

  • To review the diverse roles of STING1 across various cellular organelles.
  • To discuss the implications of STING1's organelle localization for its immune-dependent and independent functions.
  • To explore the relevance of these STING1 functions in disease pathogenesis and potential therapeutic strategies.

Main Methods:

  • Literature review of studies investigating STING1 localization and function.
  • Analysis of STING1's involvement in immune signaling pathways.
  • Examination of STING1's non-immune functions, such as autophagy and cell death.

Main Results:

  • STING1's localization extends beyond the ER and Golgi to include mitochondria, endosomes, lysosomes, and the nucleus.
  • STING1 orchestrates both immune-dependent (e.g., Type I Interferon production) and immune-independent functions (e.g., autophagy, cell death) based on its organelle.
  • STING1's diverse organelle roles are linked to various disease states.

Conclusions:

  • STING1's localization to different organelles dictates its multifaceted functions.
  • Targeting STING1 in specific organelles may offer novel therapeutic avenues for diseases.
  • Further research into STING1's organelle-specific activities is crucial for developing targeted pharmacological interventions.