BMPR1A: Wikis


Note: Many of our articles have direct quotes from sources you can cite, within the Wikipedia article! This article doesn't yet, but we're working on it! See more info or our list of citable articles.


From Wikipedia, the free encyclopedia

Bone morphogenetic protein receptor, type IA

PDB rendering based on 1es7.
Available structures
1es7, 1rew, 2goo, 2h62, 2h64
Symbols BMPR1A; ACVRLK3; ALK3; CD292
External IDs OMIM601299 MGI1338938 HomoloGene20911 GeneCards: BMPR1A Gene
RNA expression pattern
PBB GE BMPR1A 213578 at tn.png
PBB GE BMPR1A 204832 s at tn.png
More reference expression data
Species Human Mouse
Entrez 657 12166
Ensembl ENSG00000107779 ENSMUSG00000021796
UniProt P36894 Q3UP52
RefSeq (mRNA) NM_004329 NM_009758
RefSeq (protein) NP_004320 NP_033888
Location (UCSC) Chr 10:
88.51 - 88.67 Mb
Chr 14:
33.24 - 33.33 Mb
PubMed search [1] [2]

The bone morphogenetic protein receptor, type IA also known as BMPR1A is a protein which in humans is encoded by the BMPR1A gene. BMPR1A has also been designated as CD292 (cluster of differentiation 290).[1]



The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A (this protein) and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF beta superfamily. TGF-betas and activins transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.[1]

BMP's repress WNT signaling to maintain stable stem cell populations. BMPR1A null mice died at embyonic day 8.0 without mesoderm specification, demonstrating its vital role in gastrulation.[2] It has been demonstrated in experiments using dominant negative BMPR1A chick embryos that BMPR1A plays a role in apoptosis and adipocyte development.[2] Using constitutively active forms of BMR1A it has been shown that it plays a role in cell differentiation.[2] Signals tranduced by the BMPR1A receptor are not essential for osteoblast formation or proliferation; however, BMPR1A is necessary for the extracellular matrix depostition by osteoblasts.[2] In the chick embryo, BMPR1A receptors are found in low levels in limb bud mesenchyme, a differing location to BMPR1B, supporting the differing roles they play in osteogenesis.[3]



BMPR1A, SMAD4 and PTEN are responsible for Juvenile polyposis syndrome, juvenile intestinal polyposis and Cowden's disease.


BMPR1A has been shown to interact with SF3B4,[4] ZMYND11[5] and Bone morphogenetic protein 2.[6][7][8][9]


  1. ^ a b "Entrez Gene: BMPR1A bone morphogenetic protein receptor, type IA".  
  2. ^ a b c d Mishina Y, Starbuck MW, Gentile MA, Fukuda T, Kasparcova V, Seedor JG, Hanks MC, Amling M, Pinero GJ, Harada S, Behringer RR (2004). "Bone morphogenetic protein type IA receptor signaling regulates postnatal osteoblast function and bone remodeling". J. Biol. Chem. 279 (26): 27560–6. doi:10.1074/jbc.M404222200. PMID 15090551.  
  3. ^ Yoon BS, Ovchinnikov DA, Yoshii I, Mishina Y, Behringer RR, Lyons KM (2005). "Bmpr1a and Bmpr1b have overlapping functions and are essential for chondrogenesis in vivo". Proc. Natl. Acad. Sci. U.S.A. 102 (14): 5062–7. doi:10.1073/pnas.0500031102. PMID 15781876.  
  4. ^ Nishanian, Tagvor G; Waldman Todd (Oct. 2004). "Interaction of the BMPR-IA tumor suppressor with a developmentally relevant splicing factor". Biochem. Biophys. Res. Commun. (United States) 323 (1): 91–7. doi:10.1016/j.bbrc.2004.08.060. ISSN 0006-291X. PMID 15351706.  
  5. ^ Kurozumi, K; Nishita M, Yamaguchi K, Fujita T, Ueno N, Shibuya H (Apr. 1998). "BRAM1, a BMP receptor-associated molecule involved in BMP signalling". Genes Cells (ENGLAND) 3 (4): 257–64. ISSN 1356-9597. PMID 9663660.  
  6. ^ Nickel, J; Dreyer M K, Kirsch T, Sebald W (2001). "The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists". The Journal of bone and joint surgery. American volume (United States) 83-A Suppl 1 (Pt 1): S7-14. ISSN 0021-9355. PMID 11263668.  
  7. ^ Kirsch, T; Nickel J, Sebald W (Feb. 2000). "Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2". FEBS Lett. (NETHERLANDS) 468 (2-3): 215–9. ISSN 0014-5793. PMID 10692589.  
  8. ^ Kirsch, T; Nickel J, Sebald W (Jul. 2000). "BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II". EMBO J. (ENGLAND) 19 (13): 3314–24. doi:10.1093/emboj/19.13.3314. ISSN 0261-4189. PMID 10880444.  
  9. ^ Gilboa, L; Nohe A, Geissendörfer T, Sebald W, Henis Y I, Knaus P (Mar. 2000). "Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors". Mol. Biol. Cell (UNITED STATES) 11 (3): 1023–35. ISSN 1059-1524. PMID 10712517.  

Further reading

  • Nickel J, Dreyer MK, Kirsch T, Sebald W (2001). "The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists.". The Journal of bone and joint surgery. American volume 83-A Suppl 1 (Pt 1): S7-14. PMID 11263668.  
  • Liu F, Ventura F, Doody J, Massagué J (1995). "Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs.". Mol. Cell. Biol. 15 (7): 3479–86. PMID 7791754.  
  • ten Dijke P, Ichijo H, Franzén P, et al. (1993). "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity.". Oncogene 8 (10): 2879–87. PMID 8397373.  
  • Ishidou Y, Kitajima I, Obama H, et al. (1996). "Enhanced expression of type I receptors for bone morphogenetic proteins during bone formation.". J. Bone Miner. Res. 10 (11): 1651–9. PMID 8592941.  
  • Yamada N, Kato M, ten Dijke P, et al. (1996). "Bone morphogenetic protein type IB receptor is progressively expressed in malignant glioma tumours.". Br. J. Cancer 73 (5): 624–9. PMID 8605097.  
  • Nishitoh H, Ichijo H, Kimura M, et al. (1996). "Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5.". J. Biol. Chem. 271 (35): 21345–52. PMID 8702914.  
  • Wu X, Robinson CE, Fong HW, Gimble JM (1996). "Analysis of the native murine bone morphogenetic protein serine threonine kinase type I receptor (ALK-3).". J. Cell. Physiol. 168 (2): 453–61. doi:10.1002/(SICI)1097-4652(199608)168:2<453::AID-JCP24>3.0.CO;2-2. PMID 8707881.  
  • Erlacher L, McCartney J, Piek E, et al. (1998). "Cartilage-derived morphogenetic proteins and osteogenic protein-1 differentially regulate osteogenesis.". J. Bone Miner. Res. 13 (3): 383–92. PMID 9525338.  
  • Zhang D, Mehler MF, Song Q, Kessler JA (1998). "Development of bone morphogenetic protein receptors in the nervous system and possible roles in regulating trkC expression.". J. Neurosci. 18 (9): 3314–26. PMID 9547239.  
  • Kurozumi K, Nishita M, Yamaguchi K, et al. (1998). "BRAM1, a BMP receptor-associated molecule involved in BMP signalling.". Genes Cells 3 (4): 257–64. PMID 9663660.  
  • Ide H, Saito-Ohara F, Ohnami S, et al. (1998). "Assignment of the BMPR1A and BMPR1B genes to human chromosome 10q22.3 and 4q23→q24 byin situ hybridization and radiation hybrid map ping.". Cytogenet. Cell Genet. 81 (3-4): 285–6. PMID 9730621.  
  • Souchelnytskyi S, Nakayama T, Nakao A, et al. (1998). "Physical and functional interaction of murine and Xenopus Smad7 with bone morphogenetic protein receptors and transforming growth factor-beta receptors.". J. Biol. Chem. 273 (39): 25364–70. PMID 9738003.  
  • You L, Kruse FE, Pohl J, Völcker HE (1999). "Bone morphogenetic proteins and growth and differentiation factors in the human cornea.". Invest. Ophthalmol. Vis. Sci. 40 (2): 296–311. PMID 9950587.  
  • Aström AK, Jin D, Imamura T, et al. (1999). "Chromosomal localization of three human genes encoding bone morphogenetic protein receptors.". Mamm. Genome 10 (3): 299–302. PMID 10051328.  
  • Ebisawa T, Tada K, Kitajima I, et al. (2000). "Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation.". J. Cell. Sci. 112 ( Pt 20): 3519–27. PMID 10504300.  
  • Kirsch T, Nickel J, Sebald W (2000). "Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2.". FEBS Lett. 468 (2-3): 215–9. PMID 10692589.  
  • Gilboa L, Nohe A, Geissendörfer T, et al. (2000). "Bone morphogenetic protein receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors.". Mol. Biol. Cell 11 (3): 1023–35. PMID 10712517.  
  • Kim IY, Lee DH, Ahn HJ, et al. (2000). "Expression of bone morphogenetic protein receptors type-IA, -IB and -II correlates with tumor grade in human prostate cancer tissues.". Cancer Res. 60 (11): 2840–4. PMID 10850425.  
  • Kirsch T, Sebald W, Dreyer MK (2000). "Crystal structure of the BMP-2-BRIA ectodomain complex.". Nat. Struct. Biol. 7 (6): 492–6. doi:10.1038/75903. PMID 10881198.  
  • Wan M, Shi X, Feng X, Cao X (2001). "Transcriptional mechanisms of bone morphogenetic protein-induced osteoprotegrin gene expression.". J. Biol. Chem. 276 (13): 10119–25. doi:10.1074/jbc.M006918200. PMID 11139569.  

External links



Got something to say? Make a comment.
Your name
Your email address