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Related Concept Videos

Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
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Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Integrins01:10

Integrins

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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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
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Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

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Related Experiment Video

Updated: May 15, 2026

Improved Enzyme Protection Assay to Study Staphylococcus aureus Internalization and Intracellular Efficacy of Antimicrobial Compounds
06:36

Improved Enzyme Protection Assay to Study Staphylococcus aureus Internalization and Intracellular Efficacy of Antimicrobial Compounds

Published on: September 8, 2021

Integrin-mediated internalization of Staphylococcus aureus does not require vinculin.

Marina Borisova1, Yong Shi, Alexander Buntru

  • 1Lehrstuhl Zellbiologie, Universität Konstanz, Postfach X908, 78457 Konstanz, Germany.

BMC Cell Biology
|January 9, 2013
PubMed
Summary

Vinculin does not play a role in Staphylococcus aureus internalization by host cells, despite its known function in linking integrins to the actin cytoskeleton. This finding clarifies the molecular mechanisms of bacterial invasion.

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Last Updated: May 15, 2026

Improved Enzyme Protection Assay to Study Staphylococcus aureus Internalization and Intracellular Efficacy of Antimicrobial Compounds
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In Vitro and In Vivo Model to Study Bacterial Adhesion to the Vessel Wall Under Flow Conditions

Published on: June 11, 2015

Area of Science:

  • Microbiology
  • Cell Biology
  • Infectious Diseases

Background:

  • Staphylococcus aureus pathogenesis involves fibronectin binding, leading to host cell uptake via integrin engagement.
  • Actin cytoskeleton reorganization is crucial for bacterial entry into host cells.
  • Several cytoplasmic proteins are known to facilitate bacterial invasion.

Purpose of the Study:

  • To investigate the potential role of vinculin in the integrin-mediated internalization of Staphylococcus aureus.
  • To determine if vinculin contributes to the host cell entry mechanism of S. aureus.

Main Methods:

  • Utilized vinculin-deficient cells complemented with vinculin.
  • Employed vinculin overexpression studies.
  • Performed shRNA-mediated vinculin knockdown in various eukaryotic cell types.

Main Results:

  • Vinculin was found to have no functional role in the integrin-mediated uptake of Staphylococcus aureus.
  • Experimental manipulations of vinculin levels did not affect bacterial internalization.

Conclusions:

  • Vinculin is insignificant for Staphylococcus aureus internalization, despite its established role as an integrin-actin linker.
  • The study clarifies that vinculin is not a key mediator in this specific bacterial invasion pathway.