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Related Concept Videos

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.
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...
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.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...

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Related Experiment Videos

SHARPINing integrin inhibition.

Mark D Bass

    Nature Cell Biology
    |November 4, 2011
    PubMed
    Summary
    This summary is machine-generated.

    SHARPIN protein negatively regulates integrin activation by binding to the alpha-integrin subunit. This interaction interferes with the beta cytoplasmic domain

    Related Experiment Videos

    Area of Science:

    • Cell biology
    • Molecular biology
    • Biochemistry

    Background:

    • Integrin activity is essential for cell adhesion, migration, and differentiation.
    • Integrin regulation primarily involves protein interactions with the integrin β cytoplasmic domain.

    Discussion:

    • SHARPIN protein identified as a novel negative regulator of integrin activation.
    • SHARPIN binds to the α-integrin subunit, disrupting key protein associations.
    • This mechanism interferes with the β cytodomain's interaction with activating proteins.

    Key Insights:

    • SHARPIN acts as an inhibitory factor in integrin signaling pathways.
    • The α-integrin subunit is a direct binding target for SHARPIN.
    • Disruption of β cytodomain interactions is the mechanism of integrin inactivation.

    Outlook:

    • Potential therapeutic target for diseases involving abnormal cell adhesion or migration.
    • Further research into SHARPIN's role in various cellular processes.
    • Investigating the structural basis of SHARPIN-integrin interactions.