BMPR1A

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 292).[5]

BMPR1A
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBMPR1A, 10q23del, ACVRLK3, ALK3, CD292, SKR5, bone morphogenetic protein receptor type 1A
External IDsOMIM: 601299 MGI: 1338938 HomoloGene: 20911 GeneCards: BMPR1A
Orthologs
SpeciesHumanMouse
Entrez

657

12166

Ensembl

ENSG00000107779

ENSMUSG00000021796

UniProt

P36894

P36895

RefSeq (mRNA)

NM_004329

NM_009758

RefSeq (protein)

NP_004320

NP_033888

Location (UCSC)Chr 10: 86.76 – 86.93 MbChr 14: 34.13 – 34.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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 heterodimeric 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.[5]

BMP's repress WNT signaling to maintain stable stem cell populations. BMPR1A null mice died at embryonic day 8.0 without mesoderm specification, demonstrating its vital role in gastrulation.[6] It has been demonstrated in experiments using dominant negative BMPR1A chick embryos that BMPR1A plays a role in apoptosis and adipocyte development.[6] Using constitutively active forms of BMPR1A, it has been shown that BMPR1A plays a role in cell differentiation.[6] Signals transduced by the BMPR1A receptor are not essential for osteoblast formation or proliferation; however, BMPR1A is necessary for the extracellular matrix deposition by osteoblasts.[6] 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.[7]

Ligands

Diseases

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

Interactions

BMPR1A has been shown to interact with:

References
  1. GRCh38: Ensembl release 89: ENSG00000107779 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000021796 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: BMPR1A bone morphogenetic protein receptor, type IA".
  6. 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.
  7. 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. Bibcode:2005PNAS..102.5062Y. doi:10.1073/pnas.0500031102. PMC 555995. PMID 15781876.
  8. 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". J Bone Joint Surg Am. 83-A Suppl 1 (Pt 1): S7–14. PMID 11263668.
  9. Kirsch T, Nickel J, Sebald W (February 2000). "Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2". FEBS Lett. 468 (2–3): 215–9. doi:10.1016/s0014-5793(00)01214-x. PMID 10692589. S2CID 30068719.
  10. Kirsch T, Nickel J, Sebald W (July 2000). "BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II". EMBO J. 19 (13): 3314–24. doi:10.1093/emboj/19.13.3314. PMC 313944. PMID 10880444.
  11. Gilboa L, Nohe A, Geissendörfer T, Sebald W, Henis YI, Knaus P (March 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. doi:10.1091/mbc.11.3.1023. PMC 14828. PMID 10712517.
  12. Nishanian TG, Waldman T (October 2004). "Interaction of the BMPR-IA tumor suppressor with a developmentally relevant splicing factor". Biochem. Biophys. Res. Commun. 323 (1): 91–7. doi:10.1016/j.bbrc.2004.08.060. PMID 15351706.
  13. Kurozumi K, Nishita M, Yamaguchi K, Fujita T, Ueno N, Shibuya H (April 1998). "BRAM1, a BMP receptor-associated molecule involved in BMP signalling". Genes Cells. 3 (4): 257–64. doi:10.1046/j.1365-2443.1998.00186.x. PMID 9663660. S2CID 29818690.

Further reading
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