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Related Concept Videos

Role of Septins01:02

Role of Septins

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
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Septins01:19

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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
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EPS and iPS Cells in Disease Research01:21

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Embryonic and induced pluripotent stem cells are excellent models for disease research because of their ability to self-renew and differentiate into most cell types. Somatic cells from a patient are isolated and reprogrammed into induced pluripotent stem cells or iPSCs. These iPSCs are later differentiated into the desired cell type, which mirrors the diseased cell of the patient. In this way, disease models have been created for investigating diseases such as Down syndrome, type I diabetes,...
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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
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SEPHS1: Its evolution, function and roles in development and diseases.

Jeyoung Bang1, Donghyun Kang2, Jisu Jung2

  • 1Interdisciplinary Program in Bioinformatics, College of Natural Sciences, Seoul National University, Seoul, South Korea.

Archives of Biochemistry and Biophysics
|October 6, 2022
PubMed
Summary
This summary is machine-generated.

Selenophosphate synthetase 1 (SEPHS1) is crucial for maintaining cellular redox balance. Its deficiency disrupts gene expression, leading to reactive oxygen species accumulation and developmental defects, impacting various diseases.

Keywords:
Cell deathDevelopmentOsteoarthritisReactive oxygen speciesSeleniumSelenophosphate synthetase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Selenophosphate synthetase (SEPHS) enzymes are vital for selenium metabolism.
  • Eukaryotes possess two SEPHS paralogs: SEPHS1 and SEPHS2, unlike prokaryotes with a single SEPHS (SelD).
  • SEPHS2 performs selenophosphate synthesis, while SEPHS1 lacks this activity but retains ATPase function.

Purpose of the Study:

  • To elucidate the distinct roles and evolutionary divergence of SEPHS1 and SEPHS2.
  • To investigate the function of SEPHS1 in cellular redox homeostasis.
  • To understand the consequences of SEPHS1 deficiency in eukaryotic systems.

Main Methods:

  • Phylogenetic analysis of SEPHS family proteins.
  • Structural analysis of SEPHS1 homodimer.
  • Investigation of gene expression changes in SEPHS1-deficient cells and embryos.
  • Assessment of reactive oxygen species (ROS) levels and developmental phenotypes.

Main Results:

  • SEPHS1 lost selenophosphate synthesis activity but retained ATPase activity.
  • SEPHS1 plays a key role in regulating cellular redox homeostasis.
  • SEPHS1 deficiency causes ROS accumulation, growth retardation, apoptosis, DNA damage, and embryonic lethality.
  • SEPHS1 deficiency impacts retinoic acid signaling and other pathways in developing embryos.

Conclusions:

  • SEPHS1 is essential for maintaining redox balance and normal embryonic development.
  • Dysregulation of SEPHS1 is linked to various diseases, including cancer and inflammatory conditions.
  • Understanding SEPHS1 function provides insights into selenium metabolism and disease pathogenesis.