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TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
Notch Signaling Pathway03:14

Notch Signaling Pathway

The Notch signaling pathway is a major intracellular signaling pathway that is highly conserved over a broad spectrum of metazoan species. It stands unique from other intracellular signaling mechanisms in animals because notch protein itself acts as the receptor as well as the primary signaling molecule.
The Notch gene came into the limelight in 1914 after the discovery that its mutation in Drosophila melanogaster leads to a serrated (or "notched") wing margin phenotype. It was not until 1985...
Notch Signaling Pathway03:14

Notch Signaling Pathway

The Notch signaling pathway is a major intracellular signaling pathway that is highly conserved over a broad spectrum of metazoan species. It stands unique from other intracellular signaling mechanisms in animals because notch protein itself acts as the receptor as well as the primary signaling molecule.
The Notch gene came into the limelight in 1914 after the discovery that its mutation in Drosophila melanogaster leads to a serrated (or "notched") wing margin phenotype. It was not until 1985...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

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Bone Remodeling and Repair

Osteoclasts are cells responsible for bone resorption and remodeling. They originate from hematopoietic progenitor cells present in the bone marrow. Numerous progenitor cells fuse to form multinucleated cells, each with 10-20 nuclei. A single osteoclast has a diameter of 150 to 200 µM. These cells have ruffled borders that break down the underlying bone tissue and release minerals such as calcium into the blood in bone resorption. Osteoclasts cling to bones with their ruffled edges during bone...

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Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach
10:23

Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach

Published on: August 26, 2013

Neogenin, a receptor for bone morphogenetic proteins.

Meiko Hagihara1, Mitsuharu Endo, Katsuhiko Hata

  • 1Department of Molecular Neuroscience, Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

The Journal of Biological Chemistry
|December 15, 2010
PubMed
Summary

Neogenin acts as a receptor for bone morphogenetic proteins (BMPs), negatively regulating their functions. It modulates Smad signaling and osteoblastic differentiation through RhoA activation.

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Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
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Last Updated: Jun 6, 2026

Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach
10:23

Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach

Published on: August 26, 2013

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
07:26

Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis

Published on: April 1, 2022

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Biochemistry

Background:

  • Bone morphogenetic proteins (BMPs) are crucial regulators of mammalian physiological and pathological processes.
  • BMPs signal through kinase receptors (BMPR-I, BMPR-II) to activate Smad transcription factors.

Purpose of the Study:

  • To investigate the role of neogenin as a BMP receptor.
  • To elucidate neogenin's mechanism in modulating BMP-induced Smad signal transduction and osteoblastic differentiation.

Main Methods:

  • Direct binding assays of neogenin with various BMPs (BMP-2, BMP-4, BMP-6, BMP-7).
  • Neogenin knockdown and overexpression in C2C12 cells to assess effects on BMP-2 signaling.
  • Analysis of Smad1/5/8 phosphorylation and RhoA activation.
  • Pharmacological inhibition of RhoA and Rho-associated protein kinase (ROCK).

Main Results:

  • Neogenin directly binds to BMP-2, BMP-4, BMP-6, and BMP-7.
  • Neogenin knockdown enhances BMP-2-induced osteoblastic differentiation and Smad phosphorylation; overexpression suppresses these effects.
  • Neogenin mediates BMP-induced RhoA activation, which is critical for regulating osteoblastic differentiation and Smad phosphorylation.

Conclusions:

  • Neogenin functions as a BMP receptor, negatively regulating BMP signaling pathways.
  • Neogenin's inhibitory effect on BMPs is mediated through the activation of RhoA.
  • These findings reveal a novel regulatory mechanism for BMP signaling involving neogenin and RhoA.