ArticleJournal of cellular physiology2012
Initiation of BMP2 signaling in domains on the plasma membrane.
Article in Journal of cellular physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 47 citations in OpenAlex.
- Caspase-1 Mediated Cleavage of BMP Type I Receptor Drives BMP2-Induced Differentiation of Bone Marrow Mesenchymal Stem Cells into Adipocytes.Applied sciences (Basel, Switzerland) · 2025Article
- Methyl-Beta-Cyclodextrin Restores Aberrant Bone Morphogenetic Protein 2-Signaling in Bone Marrow Stromal Cells Obtained from Aged C57BL/6 Mice.Journal of developmental biology · 2024Article
- Osteogenic-Like Microenvironment of Renal Interstitium Induced by Osteomodulin Contributes to Randall's Plaque Formation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Efficient and scalable generation of primordial germ cells in 2D culture using basement membrane extract overlay.Cell reports methods · 2023Article
- Age-Related Low Bone Mineral Density in C57BL/6 Mice Is Reflective of Aberrant Bone Morphogenetic Protein-2 Signaling Observed in Human Patients Diagnosed with Osteoporosis.International journal of molecular sciences · 2022Article
- Differentiation of Cells Isolated from Human Femoral Heads into Functional Osteoclasts.Journal of developmental biology · 2022Article
- Cell trafficking and regulation of osteoblastogenesis by extracellular vesicle associated bone morphogenetic protein 2.Journal of extracellular vesicles · 2021Article
- Gene Mutation Annotation and Pedigree for Pulmonary Arterial Hypertension Patients in Han Chinese Patients.Global heart · 2021Article
- Bone Morphogenetic Protein-2 in Development and Bone Homeostasis.Journal of developmental biology · 2020Review
- Review
- Bone Morphogenetic Protein-2 Conjugated to Quantum DotNanomaterials (Basel, Switzerland) · 2020Article
- CK2.3, a Mimetic Peptide of the BMP Type I Receptor, Increases Activity in Osteoblasts over BMP2.International journal of molecular sciences · 2019Article
- Genetics and genomics of pulmonary arterial hypertension.The European respiratory journal · 2019Review
- Bone physiology as inspiration for tissue regenerative therapies.Biomaterials · 2018Review
- Mechanisms of Cellular Internalization of Quantum Dot® Conjugated Bone Formation Mimetic Peptide CK2.3.Nanomaterials (Basel, Switzerland) · 2018Article
- Mathematical modeling of the effects of CK2.3 on mineralization in osteoporotic bone.CPT: pharmacometrics & systems pharmacology · 2017Article
- Stiffness-dependent cellular internalization of matrix-bound BMP-2 and its relation to Smad and non-Smad signaling.Acta biomaterialia · 2016Article
- Article
- Tuning cellular responses to BMP-2 with material surfaces.Cytokine & growth factor reviews · 2016Review
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Bone morphogenetic protein 2 (BMP2) is a potent growth factor crucial for cell fate determination. It directs the differentiation of mesenchymal stem cells into osteoblasts, chondrocytes, adipocytes, and myocytes. Initiation of BMP2 signaling pathways occurs at the cell surface through type I and type II serine/threonine kinases housed in specific membrane domains such as caveolae enriched in the caveolin-1 beta isoform (CAV1β, caveolae) and clathrin-coated pits (CCPs). In order for BMP2 to initiate Smad signaling it must bind to its receptors on the plasma membrane resulting in the phosphorylation of the BMP type Ia receptor (BMPRIa) followed by activation of Smad signaling. The current model suggests that the canonical BMP signaling pathway, Smad, occurs in CCPs. However, several recent studies suggested Smad signaling may occur outside of CCPs. Here, we determined; (i) The location of BMP2 binding to receptors localized in caveolae, CCPs, or outside of these domains using AFM and confocal microscopy. (ii) The location of phosphorylation of BMPRIa on the plasma membrane using membrane fractionation, and (iii) the effect of down regulation of caveolae on Smad signaling. Our data indicate that BMP2 binds with highest force to BMP receptors (BMPRs) localized in caveolae. BMPRIa is phosphorylated in caveolae and the disruption of caveolae-inhibited Smad signaling in the presence of BMP2. This suggests caveolae are necessary for the initiation of Smad signaling. We propose an extension of the current model of BMP2 signaling, in which the initiation of Smad signaling is mediated by BMPRs in caveolae.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.