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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
G Protein-coupled Receptors01:15

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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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Cytoskeletal Linker Proteins - Plakins01:09

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Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...

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ERp57/GRP58: a protein with multiple functions.

Carlo Turano1, Elisa Gaucci, Caterina Grillo

  • 1Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Sapienza, Università di Roma, Roma, Italy. carlo.turano@uniroma1.it

Cellular & Molecular Biology Letters
|August 13, 2011
PubMed
Summary

The stress-responsive protein ERp57, also known as GRP58, has known roles in the endoplasmic reticulum but is also found elsewhere. Emerging evidence suggests ERp57 participates in crucial cellular processes beyond the ER, including signal transduction and DNA repair.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • ERp57/GRP58 is a stress-responsive protein within the protein disulfide isomerase family.
  • Its established functions include glycoprotein folding and quality control in the endoplasmic reticulum (ER) and MHC class I assembly.
  • ERp57 exhibits diverse subcellular localization beyond the ER, suggesting broader cellular roles.

Purpose of the Study:

  • To explore the multifaceted roles of ERp57/GRP58 beyond its canonical endoplasmic reticulum functions.
  • To consolidate evidence for ERp57's involvement in various cellular compartments and processes.
  • To highlight the significance of ERp57 in signal transduction, nuclear regulation, and DNA repair.

Main Methods:

  • Literature review and synthesis of existing research findings.
  • Analysis of studies investigating ERp57 localization and protein interactions.
  • Examination of experimental data supporting ERp57's functional involvement in different cellular pathways.

Main Results:

  • ERp57 participates in complexes with other proteins and DNA in various subcellular locations.
  • Evidence supports ERp57's role in signal transduction pathways originating from the cell surface.
  • Observations indicate ERp57's involvement in nuclear regulatory processes and DNA repair mechanisms.

Conclusions:

  • ERp57/GRP58 possesses critical functions extending far beyond the endoplasmic reticulum.
  • The protein is implicated in key cellular activities including signal transduction, nuclear regulation, and DNA repair.
  • Further research is warranted to fully elucidate the diverse roles and mechanisms of ERp57 in cellular physiology and pathology.