Repulsive guidance molecule B

Last updated
RGMB
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases RGMB , DRAGON, repulsive guidance molecule family member b, repulsive guidance molecule BMP co-receptor b
External IDs OMIM: 612687 MGI: 1916049 HomoloGene: 65355 GeneCards: RGMB
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_178615

RefSeq (protein)

NP_001012779
NP_001353437
NP_001353438
NP_001353439
NP_001353440

Contents

NP_848730

Location (UCSC) Chr 5: 98.77 – 98.8 Mb Chr 17: 15.8 – 15.83 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Repulsive guidance molecule B (RGMb), also known as DRAGON (DRG11-responsive axonal guidance and outgrowth of neurite), is a bone morphogenetic protein (BMP) co-receptor of the repulsive guidance molecule family. [5] In humans this protein is encoded by the RGMB gene. [6]

Function

RGMB is a glycosylphosphatidylinositol (GPI)-anchored member of the repulsive guidance molecule family (see also RGMA and RGMC) and contributes to the patterning of the developing nervous system. [7] [8]

There is a potential association between RGMs and cancer bone metastasis, as RGMs coordinate bone morphogenetic protein (BMP) signaling. RGMB may act as a negative regulator in vitro in breast cancer and prostate cancer through BMP signalling. [9] [10] Furthermore, aberrant expression of RGMs was indicated in breast cancer. The perturbed expression was associated with disease progression and poor prognosis. [11]

Related Research Articles

Bone morphogenetic proteins (BMPs) are a group of growth factors also known as cytokines and as metabologens. Originally discovered by their ability to induce the formation of bone and cartilage, BMPs are now considered to constitute a group of pivotal morphogenetic signals, orchestrating tissue architecture throughout the body. The important functioning of BMP signals in physiology is emphasized by the multitude of roles for dysregulated BMP signalling in pathological processes. Cancerous disease often involves misregulation of the BMP signalling system. Absence of BMP signalling is, for instance, an important factor in the progression of colon cancer, and conversely, overactivation of BMP signalling following reflux-induced esophagitis provokes Barrett's esophagus and is thus instrumental in the development of esophageal adenocarcinoma.

<span class="mw-page-title-main">Growth differentiation factor-9</span>

Growth/differentiation factor 9 is a protein that in humans is encoded by the GDF9 gene.

<span class="mw-page-title-main">Bone morphogenetic protein 7</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 7 or BMP7 is a protein that in humans is encoded by the BMP7 gene.

<span class="mw-page-title-main">Bone morphogenetic protein 2</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 2 or BMP-2 belongs to the TGF-β superfamily of proteins.

<span class="mw-page-title-main">Bone morphogenetic protein 4</span> Gene of the species Homo sapiens

Bone morphogenetic protein 4 is a protein that in humans is encoded by BMP4 gene. BMP4 is found on chromosome 14q22-q23.

<span class="mw-page-title-main">Bone morphogenetic protein 15</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 15 (BMP-15) is a protein that in humans is encoded by the BMP15 gene. It is involved in folliculogenesis, the process in which primordial follicles develop into pre-ovulatory follicles.

<span class="mw-page-title-main">Bone morphogenetic protein 10</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 10 (BMP10) is a protein that in humans is encoded by the BMP10 gene.

<span class="mw-page-title-main">Bone morphogenetic protein 6</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 6 is a protein that in humans is encoded by the BMP6 gene.

<span class="mw-page-title-main">Bone morphogenetic protein 5</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 5 is a protein that in humans is encoded by the BMP5 gene.

<span class="mw-page-title-main">Bone morphogenetic protein 3</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 3, also known as osteogenin, is a protein in humans that is encoded by the BMP3 gene.

<span class="mw-page-title-main">BMPR2</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein receptor type II or BMPR2 is a serine/threonine receptor kinase. It binds Bone morphogenetic proteins, members of the TGF beta superfamily of ligands, which are involved in paracrine signalling. BMPs are involved in a host of cellular functions including osteogenesis, cell growth and cell differentiation. Signaling in the BMP pathway begins with the binding of a BMP to the type II receptor. This causes the recruitment of a BMP type I receptor, which it phosphorylates. The Type I receptor phosphorylates an R-SMAD a transcriptional regulator.

<span class="mw-page-title-main">BMPR1A</span> Bone morphogenetic protein receptor

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.

<span class="mw-page-title-main">ACVR1</span> Protein-coding gene

Activin A receptor, type I (ACVR1) is a protein which in humans is encoded by the ACVR1 gene; also known as ALK-2. ACVR1 has been linked to the 2q23-24 region of the genome. This protein is important in the bone morphogenic protein (BMP) pathway which is responsible for the development and repair of the skeletal system. While knock-out models with this gene are in progress, the ACVR1 gene has been connected to fibrodysplasia ossificans progressiva, a disease characterized by the formation of heterotopic bone throughout the body. It is a bone morphogenetic protein receptor, type 1.

<span class="mw-page-title-main">Hemojuvelin</span>

Hemojuvelin (HJV), also known as repulsive guidance molecule C (RGMc) or hemochromatosis type 2 protein (HFE2), is a membrane-bound and soluble protein in mammals that is responsible for the iron overload condition known as juvenile hemochromatosis in humans, a severe form of hemochromatosis. In humans, the hemojuvelin protein is encoded by the HFE2 gene. Hemojuvelin is a member of the repulsive guidance molecule family of proteins. Both RGMa and RGMb are found in the nervous system, while hemojuvelin is found in skeletal muscle and the liver.

<span class="mw-page-title-main">GDF2</span>

Growth differentiation factor 2 (GDF2) also known as bone morphogenetic protein (BMP)-9 is a protein that in humans is encoded by the GDF2 gene. GDF2 belongs to the transforming growth factor beta superfamily.

<span class="mw-page-title-main">GDF6</span> Protein-coding gene in the species Homo sapiens

Growth differentiation factor 6 (GDF6) is a protein that in humans is encoded by the GDF6 gene.

<span class="mw-page-title-main">Nuclear receptor coactivator 3</span>

The nuclear receptor coactivator 3 also known as NCOA3 is a protein that, in humans, is encoded by the NCOA3 gene. NCOA3 is also frequently called 'amplified in breast 1' (AIB1), steroid receptor coactivator-3 (SRC-3), or thyroid hormone receptor activator molecule 1 (TRAM-1).

<span class="mw-page-title-main">NEO1</span>

Neogenin is a protein that in humans is encoded by the NEO1 gene.

<span class="mw-page-title-main">Repulsive guidance molecule A</span> Protein-coding gene in the species Homo sapiens

Repulsive guidance molecule A (RGMa) is a bone morphogenetic protein (BMP) co-receptor of the repulsive guidance molecule family. Together with BMPR1A and BMPR1B, as well as ACVR2A and BMPR2, it binds BMPs thereby activating the intracellular SMAD1/5/8 signalling pathway. In humans this protein is encoded by the RGMA gene.

<span class="mw-page-title-main">Chordin-like 1</span> Protein-coding gene in the species Homo sapiens

Chordin-like 1 is a protein that in humans is encoded by the CHRDL1 gene. Chordin-Like 1 (CHRDL1) is a structural glycoprotein that sits on the X chromosome and specifically encodes Venotropin, which is an antagonistic protein to bone morphogenic protein 4.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000174136 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000048027 - 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. Corradini, Elena; Babitt, Jodie L.; Lin, Herbert Y. (October 2009). "The RGM/DRAGON family of BMP co-receptors". Cytokine & Growth Factor Reviews. 20 (5–6): 389–398. doi:10.1016/j.cytogfr.2009.10.008. PMC   3715994 . PMID   19897400.
  6. "Entrez Gene: RGM domain family".
  7. Samad TA, Rebbapragada A, Bell E, Zhang Y, Sidis Y, Jeong SJ, Campagna JA, Perusini S, Fabrizio DA, Schneyer AL, Lin HY, Brivanlou AH, Attisano L, Woolf CJ (April 2005). "DRAGON, a bone morphogenetic protein co-receptor". J. Biol. Chem. 280 (14): 14122–9. doi: 10.1074/jbc.M410034200 . PMID   15671031.
  8. Severyn CJ, Shinde U, Rotwein P (September 2009). "Molecular biology, genetics and biochemistry of the repulsive guidance molecule family". Biochem. J. 422 (3): 393–403. doi:10.1042/BJ20090978. PMC   4242795 . PMID   19698085.
  9. Li J, Ye L, Sanders AJ, Jiang WG (March 2012). "Repulsive guidance molecule B (RGMB) plays negative roles in breast cancer by coordinating BMP signaling". J Cell Biochem. 113 (7): 2523–31. doi:10.1002/jcb.24128. PMID   22415859. S2CID   35629616.
  10. Li J, Ye L, Kynaston HG, Jiang WG (February 2012). "Repulsive guidance molecules, novel bone morphogenetic protein co-receptors, are key regulators of the growth and aggressiveness of prostate cancer cells". Int. J. Oncol. 40 (2): 544–50. doi: 10.3892/ijo.2011.1251 . PMID   22076499.
  11. Li J, Ye L, Mansel RE, Jiang WG (May 2011). "Potential prognostic value of repulsive guidance molecules in breast cancer". Anticancer Res. 31 (5): 1703–11. PMID   21617229.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.