Biology:BMPR1A

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Short description: Bone morphogenetic protein receptor


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

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).[1]

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.[1]

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.[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 BMPR1A, it has been shown that BMPR1A plays a role in cell differentiation.[2] 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.[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]

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. 1.0 1.1 "Entrez Gene: BMPR1A bone morphogenetic protein receptor, type IA". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=657. 
  2. 2.0 2.1 2.2 2.3 "Bone morphogenetic protein type IA receptor signaling regulates postnatal osteoblast function and bone remodeling". J. Biol. Chem. 279 (26): 27560–6. 2004. doi:10.1074/jbc.M404222200. PMID 15090551. 
  3. "Bmpr1a and Bmpr1b have overlapping functions and are essential for chondrogenesis in vivo". Proc. Natl. Acad. Sci. U.S.A. 102 (14): 5062–7. 2005. doi:10.1073/pnas.0500031102. PMID 15781876. Bibcode2005PNAS..102.5062Y. 
  4. "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. 2001. PMID 11263668. 
  5. "Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2". FEBS Lett. 468 (2–3): 215–9. February 2000. doi:10.1016/s0014-5793(00)01214-x. PMID 10692589. 
  6. "BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II". EMBO J. 19 (13): 3314–24. July 2000. doi:10.1093/emboj/19.13.3314. PMID 10880444. 
  7. "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. March 2000. doi:10.1091/mbc.11.3.1023. PMID 10712517. 
  8. "Interaction of the BMPR-IA tumor suppressor with a developmentally relevant splicing factor". Biochem. Biophys. Res. Commun. 323 (1): 91–7. October 2004. doi:10.1016/j.bbrc.2004.08.060. PMID 15351706. 
  9. "BRAM1, a BMP receptor-associated molecule involved in BMP signalling". Genes Cells 3 (4): 257–64. April 1998. doi:10.1046/j.1365-2443.1998.00186.x. PMID 9663660. 

Further reading

External links