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Related Concept Videos

Activation of Integrins01:15

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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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Integrins01:10

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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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Intracellular Signaling Affects Focal Adhesions01:17

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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.
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Fibronectins Connect Cells with ECM01:25

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Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
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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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Immunoglobulin-like Cell Adhesion Molecules01:31

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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MAP4K4 regulates integrin-FERM binding to control endothelial cell motility.

Philip Vitorino1, Stacey Yeung1, Ailey Crow1

  • 1Molecular Biology Department, Genentech, Inc., South San Francisco, California 94080, USA.

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|March 25, 2015
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A novel molecular pathway involving MAP4K4, moesin, talin, and β1-integrin is crucial for endothelial cell migration and membrane retraction. This pathway regulates cell movement and blood vessel formation, offering a potential therapeutic target.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Angiogenesis Research

Background:

  • Cell migration is a complex process essential for development and disease.
  • Understanding the molecular mechanisms of endothelial cell migration is critical for controlling angiogenesis.

Purpose of the Study:

  • To identify key molecular players regulating plasma membrane retraction during endothelial cell migration.
  • To elucidate the functional role of the MAP4K4-moesin-talin-β1-integrin pathway in cell migration and angiogenesis.

Main Methods:

  • In vitro angiogenesis screens utilizing short interfering RNA (siRNA) and chemical inhibitors.
  • Analysis of protein phosphorylation and protein-protein interactions.
  • In vitro and in vivo assays to assess cell migration, membrane dynamics, and angiogenesis.
  • Epistasis analyses to determine the order of molecular events.

Main Results:

  • A MAP4K4-moesin-talin-β1-integrin pathway was identified, promoting plasma membrane retraction in migrating endothelial cells.
  • Loss of MAP4K4 impaired endothelial cell migration, reduced membrane dynamics, and inhibited angiogenesis in vitro and in vivo.
  • MAP4K4 phosphorylates moesin, which then competes with talin for β1-integrin binding, facilitating focal adhesion disassembly.
  • Blocking α5β1-integrin reversed the migration defects caused by MAP4K4 loss.
  • MAP4K4 inhibition suppressed pathological angiogenesis in disease models.

Conclusions:

  • MAP4K4 is a key regulator of endothelial cell migration through the moesin-talin-β1-integrin pathway.
  • This pathway is essential for efficient membrane retraction and focal adhesion disassembly.
  • MAP4K4 represents a promising therapeutic target for diseases involving pathological angiogenesis.