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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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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.
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Diversity of Antigen Receptors01:28

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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
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Conservation of Protein Domains Over Different Proteins02:26

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Intrinsically Disordered Proteins02:18

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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.
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Diversity in Cell Signaling Responses01:22

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The physiological function of a cell and cellular communication are outcomes of a range of extrinsic signals, intracellular signaling pathways, and cellular responses. No two cell types express the same repertoire of signaling components. Receptors are highly selective for their cognate ligands, but once activated, they can alter multiple cellular processes such as DNA transcription, protein synthesis, and metabolic activity. 
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Related Experiment Video

Updated: Jul 1, 2025

Mitigation of Blood Borne Cell Attachment to Metal Implants through CD47-Derived Peptide Immobilization
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Mitigation of Blood Borne Cell Attachment to Metal Implants through CD47-Derived Peptide Immobilization

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Structural-functional diversity of CD47 proteoforms.

Ting Zhang1,2, Feng Wang1,2, Lu Xu1,2

  • 1Key Laboratory of Organ Regeneration and Transplantation of the Ministry of Education, Institute of Immunology, The First Hospital of Jilin University, Changchun, Jilin, China.

Frontiers in Immunology
|March 1, 2024
PubMed
Summary
This summary is machine-generated.

The CD47 protein, crucial for cell functions and immune evasion in cancer, exists in diverse forms generated by alternative splicing and modifications. Understanding CD47 proteoforms offers new therapeutic targets for cancer treatment.

Keywords:
CD47CD47-SIRPalfaalternative splicingimmune checkpointsimmunotherapypost-translational modificationproteoform

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Last Updated: Jul 1, 2025

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • CD47 is a transmembrane glycoprotein involved in critical physiological processes like phagocytosis and cell migration.
  • Aberrant CD47 expression in cancer cells facilitates immune evasion, making CD47-SIRPα blockade a promising therapeutic strategy.
  • Recent discoveries reveal a diverse array of CD47 protein variants (proteoforms) with specific expression and functional profiles.

Purpose of the Study:

  • To explore the origins and molecular properties of CD47 proteoforms.
  • To elucidate the roles of CD47 proteoforms in both physiological and pathological conditions.
  • To identify novel therapeutic strategies targeting CD47-SIRPα immune checkpoints.

Main Methods:

  • Review of existing literature on CD47 protein expression, alternative splicing, and post-translational modifications.
  • Analysis of CD47 proteoform diversity arising from single-gene variations.
  • Examination of CD47 clustering and subcellular localization regulation.

Main Results:

  • CD47 proteoforms are generated through alternative splicing, post-translational modifications (glycosylation, pyroglutamate, GAG modification, proteolytic cleavage), and APA.
  • Specific CD47 proteoforms exhibit distinct cell-, tissue-, and temporal-specific expression and functional profiles.
  • CD47 clustering and subcellular localization are regulated, contributing to its diverse roles.

Conclusions:

  • CD47 proteoform diversity significantly expands our understanding beyond a single CD47 protein interaction.
  • Identifying and characterizing CD47 proteoforms can lead to novel clinical targets for cancer immunotherapy.
  • Developing strategies to enhance responses to CD47-SIRPα inhibition is crucial for effective cancer treatment.