MEGF10

Last updated
MEGF10
Identifiers
Aliases MEGF10 , EMARDD, multiple EGF like domains 10, SR-F3
External IDs OMIM: 612453 MGI: 2685177 HomoloGene: 23771 GeneCards: MEGF10
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001256545
NM_001308119
NM_001308121
NM_032446

NM_001001979

RefSeq (protein)

NP_001243474
NP_001295048
NP_001295050
NP_115822

NP_001001979

Location (UCSC) Chr 5: 127.29 – 127.47 Mb Chr 18: 57.27 – 57.43 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Multiple EGF-like-domains 10 is a protein that in humans is encoded by the MEGF10 gene. [5]

Contents

MEGF10 is a regulator of satellite cell myogenesis and interacts with Notch1 in myoblasts. [6] It has been shown to be the cause of early-onset myopathy, areflexia, respiratory distress and dysphagia. [7]

MEGF10 and MEGF11, have critical roles in the formation of mosaics by two retinal interneuron subtypes, starburst amacrine cells and horizontal cells in mice. These cells are less likely to be near neighbours of the same subtype than would occur by chance, resulting in 'exclusion zones' that separate them. Mosaic arrangements provide a mechanism to distribute each cell type evenly across the retina, ensuring that all parts of the visual field have access to a full set of processing elements. [8]

Related Research Articles

<span class="mw-page-title-main">Notch signaling pathway</span> Series of molecular signals

The Notch signaling pathway is a highly conserved cell signaling system present in most animals. Mammals possess four different notch receptors, referred to as NOTCH1, NOTCH2, NOTCH3, and NOTCH4. The notch receptor is a single-pass transmembrane receptor protein. It is a hetero-oligomer composed of a large extracellular portion, which associates in a calcium-dependent, non-covalent interaction with a smaller piece of the notch protein composed of a short extracellular region, a single transmembrane-pass, and a small intracellular region.

<span class="mw-page-title-main">MyoD</span> Mammalian protein found in Homo sapiens

MyoD, also known as myoblast determination protein 1, is a protein in animals that plays a major role in regulating muscle differentiation. MyoD, which was discovered in the laboratory of Harold M. Weintraub, belongs to a family of proteins known as myogenic regulatory factors (MRFs). These bHLH transcription factors act sequentially in myogenic differentiation. Vertebrate MRF family members include MyoD1, Myf5, myogenin, and MRF4 (Myf6). In non-vertebrate animals, a single MyoD protein is typically found.

<span class="mw-page-title-main">Desmin</span> Mammalian protein found in humans

Desmin is a protein that in humans is encoded by the DES gene. Desmin is a muscle-specific, type III intermediate filament that integrates the sarcolemma, Z disk, and nuclear membrane in sarcomeres and regulates sarcomere architecture.

<span class="mw-page-title-main">Myogenesis</span> Formation of muscular tissue, particularly during embryonic development

Myogenesis is the formation of skeletal muscular tissue, particularly during embryonic development.

<span class="mw-page-title-main">Myogenin</span> Mammalian protein found in Homo sapiens

Myogenin, is a transcriptional activator encoded by the MYOG gene. Myogenin is a muscle-specific basic-helix-loop-helix (bHLH) transcription factor involved in the coordination of skeletal muscle development or myogenesis and repair. Myogenin is a member of the MyoD family of transcription factors, which also includes MyoD, Myf5, and MRF4.

<span class="mw-page-title-main">Heparin-binding EGF-like growth factor</span> Protein-coding gene in the species Homo sapiens

Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of proteins that in humans is encoded by the HBEGF gene.

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

Dysbindin, short for dystrobrevin-binding protein 1, is a protein constituent of the dystrophin-associated protein complex (DPC) of skeletal muscle cells. It is also a part of BLOC-1, or biogenesis of lysosome-related organelles complex 1. Dysbindin was discovered by the research group of Derek Blake via yeast two-hybrid screening for binding partners of α-dystrobrevin. In addition, dysbindin is found in neural tissue of the brain, particularly in axon bundles and especially in certain axon terminals, notably mossy fiber synaptic terminals in the cerebellum and hippocampus. In humans, dysbindin is encoded by the DTNBP1 gene.

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

Neurogenic locus notch homolog protein 1(Notch 1) is a protein encoded in humans by the NOTCH1 gene. Notch 1 is a single-pass transmembrane receptor.

<span class="mw-page-title-main">ERBB4</span> Protein-coding gene in the species Homo sapiens

Receptor tyrosine-protein kinase erbB-4 is an enzyme that in humans is encoded by the ERBB4 gene. Alternatively spliced variants that encode different protein isoforms have been described; however, not all variants have been fully characterized.

<span class="mw-page-title-main">CELSR1</span> Protein-coding gene in humans

Cadherin EGF LAG seven-pass G-type receptor 1 also known as flamingo homolog 2 or cadherin family member 9 is a protein that in humans is encoded by the CELSR1 gene.

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

Recombination signal binding protein for immunoglobulin kappa J region is a protein that in humans is encoded by the RBPJ gene.

<span class="mw-page-title-main">Dedicator of cytokinesis protein 1</span> Protein found in humans

Dedicator of cytokinesis protein 1 (Dock1), also (DOCK180), is a large protein encoded in the human by the DOCK1 gene, involved in intracellular signalling networks. It is the mammalian ortholog of the C. elegans protein CED-5 and belongs to the DOCK family of guanine nucleotide exchange factors (GEFs).

<span class="mw-page-title-main">TNNT1</span> Protein-coding gene in the species Homo sapiens

Slow skeletal muscle troponin T (sTnT) is a protein that in humans is encoded by the TNNT1 gene.

<span class="mw-page-title-main">CDH15</span> Protein-coding gene in the species Homo sapiens

Cadherin-15 is a protein that in humans is encoded by the CDH15 gene.

<span class="mw-page-title-main">Neurogenin-1</span> Protein-coding gene

Neurogenin-1 is a protein that in humans is encoded by the NEUROG1 gene.

<span class="mw-page-title-main">Neuregulin 3</span> Protein-coding gene in Homo sapiens

Neuregulin 3, also known as NRG3, is a neural-enriched member of the neuregulin protein family which in humans is encoded by the NRG3 gene. The NRGs are a group of signaling proteins part of the superfamily of epidermal growth factor, EGF like polypeptide growth factor. These groups of proteins possess an 'EGF-like domain' that consists of six cysteine residues and three disulfide bridges predicted by the consensus sequence of the cysteine residues.

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

Notch proteins are a family of type 1 transmembrane proteins that form a core component of the Notch signaling pathway, which is highly conserved in metazoans. The Notch extracellular domain mediates interactions with DSL family ligands, allowing it to participate in juxtacrine signaling. The Notch intracellular domain acts as a transcriptional activator when in complex with CSL family transcription factors. Members of this type 1 transmembrane protein family share several core structures, including an extracellular domain consisting of multiple epidermal growth factor (EGF)-like repeats and an intracellular domain transcriptional activation domain (TAD). Notch family members operate in a variety of different tissues and play a role in a variety of developmental processes by controlling cell fate decisions. Much of what is known about Notch function comes from studies done in Caenorhabditis elegans (C.elegans) and Drosophila melanogaster. Human homologs have also been identified, but details of Notch function and interactions with its ligands are not well known in this context.

<span class="mw-page-title-main">MYF5</span> Protein-coding gene in the species Homo sapiens

Myogenic factor 5 is a protein that in humans is encoded by the MYF5 gene. It is a protein with a key role in regulating muscle differentiation or myogenesis, specifically the development of skeletal muscle. Myf5 belongs to a family of proteins known as myogenic regulatory factors (MRFs). These basic helix loop helix transcription factors act sequentially in myogenic differentiation. MRF family members include Myf5, MyoD (Myf3), myogenin, and MRF4 (Myf6). This transcription factor is the earliest of all MRFs to be expressed in the embryo, where it is only markedly expressed for a few days. It functions during that time to commit myogenic precursor cells to become skeletal muscle. In fact, its expression in proliferating myoblasts has led to its classification as a determination factor. Furthermore, Myf5 is a master regulator of muscle development, possessing the ability to induce a muscle phenotype upon its forced expression in fibroblastic cells.

<span class="mw-page-title-main">MYF6</span> Protein-coding gene in the species Homo sapiens

Myogenic factor 6 is a protein that in humans is encoded by the MYF6 gene. This gene is also known in the biomedical literature as MRF4 and herculin. MYF6 is a myogenic regulatory factor (MRF) involved in the process known as myogenesis.

<span class="mw-page-title-main">Calponin 3, acidic</span> Protein-coding gene in the species Homo sapiens

Calponin 3. acidic is a protein that in humans is encoded by the CNN3 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000145794 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024593 - 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: Multiple EGF-like-domains 10" . Retrieved 2011-11-26.
  6. Saha M, Mitsuhashi S, Jones MD, Manko K, Reddy HM, Bruels C, Cho KA, Pacak CA, Draper I, Kang PB (May 2017). "Consequences of MEGF10 deficiency on myoblast function and Notch1 interactions". Human Molecular Genetics. 26 (15): 2984–3000. doi:10.1093/hmg/ddx189. PMC   6075367 . PMID   28498977.
  7. Logan CV, Lucke B, Pottinger C, Abdelhamed ZA, Parry DA, Szymanska K, Diggle CP, van Riesen A, Morgan JE, Markham G, Ellis I, Manzur AY, Markham AF, Shires M, Helliwell T, Scoto M, Hübner C, Bonthron DT, Taylor GR, Sheridan E, Muntoni F, Carr IM, Schuelke M, Johnson CA (November 2011). "Mutations in MEGF10, a regulator of satellite cell myogenesis, cause early onset myopathy, areflexia, respiratory distress and dysphagia (EMARDD)". Nature Genetics. 43 (12): 1189–92. doi:10.1038/ng.995. PMID   22101682. S2CID   5536249.
  8. Kay JN, Chu MW, Sanes JR (March 2012). "MEGF10 and MEGF11 mediate homotypic interactions required for mosaic spacing of retinal neurons". Nature. 483 (7390): 465–9. Bibcode:2012Natur.483..465K. doi:10.1038/nature10877. PMC   3310952 . PMID   22407321.

Further reading