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Related Concept Videos

Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
Cell Polarization by Rho Proteins01:21

Cell Polarization by Rho Proteins

Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:

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Using Confocal Analysis of Xenopus laevis to Investigate Modulators of Wnt and Shh Morphogen Gradients
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Published on: December 14, 2015

Shaping morphogen gradients by proteoglycans.

Dong Yan1, Xinhua Lin

  • 1Division of Developmental Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio 45229, USA.

Cold Spring Harbor Perspectives in Biology
|January 13, 2010
PubMed
Summary
This summary is machine-generated.

Heparan sulfate proteoglycans (HSPGs) are crucial regulators of morphogen gradient formation during development. This review highlights HSPGs

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Area of Science:

  • Developmental biology
  • Cell biology
  • Biochemistry

Background:

  • Secreted morphogens like Wnt, Hedgehog (Hh), and BMP pattern tissues by forming concentration gradients.
  • Understanding morphogen gradient formation is key to developmental biology.
  • Heparan sulfate proteoglycans (HSPGs) have emerged as critical regulators in this process.

Purpose of the Study:

  • To review the mechanistic roles of HSPGs in controlling morphogen gradient formation.
  • To highlight recent findings on how HSPGs regulate morphogen activity.
  • To synthesize current knowledge on HSPG involvement in developmental patterning.

Main Methods:

  • Review of genetic studies in model organisms like Drosophila.
  • Analysis of cell biological data.
  • Integration of biochemical findings on HSPG-morphogen interactions.

Main Results:

  • HSPGs regulate morphogen movement, signaling, and intracellular trafficking.
  • Specific HSPGs are essential for establishing precise morphogen concentration gradients.
  • Mechanistic insights reveal how HSPGs modulate morphogen activity at various stages.

Conclusions:

  • HSPGs play indispensable roles in regulating morphogen gradient formation.
  • Targeting HSPG functions offers potential avenues for understanding developmental disorders.
  • Further research into HSPG-morphogen interactions will advance developmental biology.