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Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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Differential relays are used to protect generators, buses, and transformers by comparing electrical quantities at different points. When a fault occurs, the difference in current between the two points triggers the relay to operate, opening the circuit breaker. Under normal conditions, the current entering (i1) and leaving (i2) a generator are equal. When a fault occurs, however, these currents become unequal, and the difference current flows in the relay operating coil, causing the relay to...
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IP3/DAG Signaling Pathway01:11

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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Line Protection with Impedance Relays01:27

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Coordinating time-delay overcurrent relays in complex radial systems and directional overcurrent relays in multi-source transmission loops can be challenging. Impedance relays address these issues by responding to the voltage-to-current ratio, specifically measuring the apparent impedance of a line. These relays become more sensitive during faults as current increases and voltage decreases, thereby reducing the apparent impedance.
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Anchoring Junctions01:03

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Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
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Related Experiment Video

Updated: Jan 4, 2026

Real-Time Proxy-Control of Re-Parameterized Peripheral Signals using a Close-Loop Interface
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The Kindlin Outside Connection.

Mary R Starich1, Nico Tjandra1

  • 1Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.

Structure (London, England : 1993)
|November 7, 2019
PubMed
Summary
This summary is machine-generated.

This study reveals how kindlin-2 recruits paxillin, an initial step in activating transmembrane integrin. This process is crucial for connecting the cell

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Area of Science:

  • Cellular biology
  • Molecular mechanisms
  • Protein interactions

Background:

  • Transmembrane integrins link extracellular matrix to intracellular signaling pathways.
  • Integrin activation is mediated by focal adhesion proteins like talin and kindlin.
  • Integrin signaling regulates cellular responses and adhesion.

Purpose of the Study:

  • To elucidate the initial molecular events in integrin activation.
  • To describe the role of kindlin-2 in the recruitment of key signaling proteins.
  • To provide structural insights into the early stages of focal adhesion assembly.

Main Methods:

  • Structural biology techniques (e.g., X-ray crystallography, cryo-EM).
  • Biochemical assays to study protein-protein interactions.
  • Cell-based assays to investigate signaling dynamics.

Main Results:

  • Zhu et al. (2019) detail the interaction between kindlin-2 and paxillin.
  • An initial recruitment step involving the ubiquitin-like domain of kindlin-2 was identified.
  • This interaction is proposed as a critical early event in integrin activation.

Conclusions:

  • The findings provide a structural basis for understanding how kindlin-2 initiates integrin-mediated signaling.
  • This work sheds light on the assembly of focal adhesions.
  • Understanding these early steps is vital for comprehending cell adhesion and migration.