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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
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G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
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Related Experiment Video

Updated: Jul 3, 2025

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Cingulin family: Structure, function and clinical significance.

Yuling Su1, You Long1, Keping Xie2

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|February 14, 2024
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Summary

Cingulin and paracingulin are key proteins in cell junctions, regulating barrier function and impacting diseases like inflammation and cancer. This review details their structure, interactions, and roles in health and pathology.

Keywords:
CingulinInflammationParacingulinTight junctionTumorigenesis

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cingulin and paracingulin are essential components of the apical junctional complex in vertebrate cells.
  • These proteins are localized to tight junctions (TJ) and adherens junctions (AJ), functioning as TJ cytoplasmic plaque proteins.

Purpose of the Study:

  • To review the discovery, structure, expression, subcellular distribution, and molecular interactions of cingulin family proteins.
  • To discuss the roles of cingulin and paracingulin in development, physiology, and pathological processes.

Main Methods:

  • Literature review of studies on cingulin and paracingulin.
  • Analysis of protein interactions, including cytoskeletal proteins and small GTPases (RhoA, Rac1).
  • Examination of their role in gene expression and barrier function regulation.

Main Results:

  • Cingulin and paracingulin interact with various proteins to modulate cellular functions.
  • These proteins influence small GTPase activity, gene expression, and epithelial/endothelial barrier integrity.
  • Dysregulation of cingulin and paracingulin is implicated in pathological conditions like inflammation and tumorigenesis.

Conclusions:

  • Cingulin family proteins are crucial regulators of cell junction function, development, and physiology.
  • Their involvement extends to pathological processes, highlighting their significance in disease.
  • Further research into cingulin and paracingulin interactions and functions can provide insights into therapeutic strategies.