Emerin
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| Category | Antibiotics |
| Catalog number | BBF-01214 |
| CAS | 40581-18-8 |
| Molecular Weight | 316.35 |
| Molecular Formula | C20H16N2O2 |
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Description
It is produced by the strain of Aspergillus nidulans. Emerin is an antibiotic. Emerin is a protein that in humans is encoded by the EMD gene, also known as the STA gene. Mutations in emerin cause X-linked recessive Emery-Dreifuss muscular dystrophy, cardiac conduction abnormalities and dilated cardiomyopathy.
Specification
| Synonyms | Epurpurin C dimethyl ether; Emerin (Aspergillus); Butanedinitrile, bis((4-methoxyphenyl)methylene)-, (Z,Z)- |
| IUPAC Name | (2Z,3Z)-2,3-bis[(4-methoxyphenyl)methylidene]butanedinitrile |
| Canonical SMILES | COC1=CC=C(C=C1)C=C(C#N)C(=CC2=CC=C(C=C2)OC)C#N |
| InChI | InChI=1S/C20H16N2O2/c1-23-19-7-3-15(4-8-19)11-17(13-21)18(14-22)12-16-5-9-20(24-2)10-6-16/h3-12H,1-2H3/b17-11+,18-12+ |
| InChI Key | HCHFRAXBELVCGG-JYFOCSDGSA-N |
Properties
| Appearance | Greenish-Yellow Crystal |
| Boiling Point | 549.7 °C at 760 mmHg |
| Melting Point | 225-226 °C |
| Density | 1.186 g/cm3 |
| Solubility | Soluble in Acetone |
Reference Reading
1. Emerin regulation of nuclear stiffness is required for fast amoeboid migration in confined environments
Sandrine B Lavenus, Karl W Vosatka, Alexa P Caruso, Maria F Ullo, Ayesha Khan, Jeremy S Logue J Cell Sci. 2022 Apr 15;135(8):jcs259493. doi: 10.1242/jcs.259493. Epub 2022 May 3.
When metastasizing, tumor cells must traverse environments with diverse physicochemical properties. Recently, the cell nucleus has emerged as a major regulator of the transition from mesenchymal to fast amoeboid (leader bleb-based) migration. Here, we demonstrate that increasing nuclear stiffness through elevating lamin A, inhibits fast amoeboid migration in melanoma cells. Importantly, nuclei may respond to force through stiffening. A key factor in this process is the inner nuclear membrane (INM) protein emerin. Accordingly, we determined the role of emerin in regulating fast amoeboid migration. Strikingly, we found that both the up- and downregulation of emerin results in an inhibition of fast amoeboid migration. However, when key Src phosphorylation sites were removed, upregulation of emerin no longer inhibited fast amoeboid migration. Interestingly, as measured by using a Src biosensor, activity of Src was low in cells within a confined environment. Thus, the fast amoeboid migration of melanoma cells depends on the precise calibration of emerin activity.
2. Emerin interacts with histone methyltransferases to regulate repressive chromatin at the nuclear periphery
Nicholas Marano, James M Holaska Front Cell Dev Biol. 2022 Oct 6;10:1007120. doi: 10.3389/fcell.2022.1007120. eCollection 2022.
X-Linked Emery-Dreifuss muscular dystrophy is caused by mutations in the gene encoding emerin. Emerin is an inner nuclear membrane protein important for repressive chromatin organization at the nuclear periphery. Myogenic differentiation is a tightly regulated process characterized by genomic reorganization leading to coordinated temporal expression of key transcription factors, including MyoD, Pax7, and Myf5. Emerin was shown to interact with repressive histone modification machinery, including HDAC3 and EZH2. Using emerin-null myogenic progenitor cells we established several EDMD-causing emerin mutant lines in the effort to understand how the functional interaction of emerin with HDAC3 regulates histone methyltransferase localization or function to organize repressive chromatin at the nuclear periphery. We found that, in addition to its interaction with HDAC3, emerin interacts with the histone methyltransferases EZH2 and G9a in myogenic progenitor cells. Further, we show enhanced binding of emerin HDAC3-binding mutants S54F and Q133H to EZH2 and G9a. Treatment with small molecule inhibitors of EZH2 and G9a reduced H3K9me2 or H3K27me3 throughout differentiation. EZH2 and G9a inhibitors impaired cell cycle withdrawal, differentiation commitment, and myotube formation in wildtype progenitors, while they had no effect on emerin-null progenitors. Interestingly, these inhibitors exacerbated the impaired differentiation of emerin S54F and Q133H mutant progenitors. Collectively, these results suggest the functional interaction between emerin and HDAC3, EZH2, and G9a are important for myogenic differentiation.
3. Emerin self-assembly and nucleoskeletal coupling regulate nuclear envelope mechanics against stress
Anthony Fernandez, Markville Bautista, Liying Wu, Fabien Pinaud J Cell Sci. 2022 Mar 15;135(6):jcs258969. doi: 10.1242/jcs.258969. Epub 2022 Mar 30.
Emerin is an integral nuclear envelope protein that participates in the maintenance of nuclear shape. When mutated or absent, emerin causes X-linked Emery-Dreifuss muscular dystrophy (EDMD). To understand how emerin takes part in molecular --scaffolding at the nuclear envelope and helps protect the nucleus against mechanical stress, we established its nanoscale organization using single-molecule tracking and super-resolution microscopy. We show that emerin monomers form localized oligomeric nanoclusters stabilized by both lamin A/C and the SUN1-containing linker of nucleoskeleton and cytoskeleton (LINC) complex. Interactions of emerin with nuclear actin and BAF (also known as BANF1) additionally modulate its membrane mobility and its ability to oligomerize. In nuclei subjected to mechanical challenges, the mechanotransduction functions of emerin are coupled to changes in its oligomeric state, and the incremental self-assembly of emerin determines nuclear shape adaptation against mechanical forces. We also show that the abnormal nuclear envelope deformations induced by EDMD emerin mutants stem from improper formation of lamin A/C and LINC complex-stabilized emerin oligomers. These findings place emerin at the center of the molecular processes that regulate nuclear shape remodeling in response to mechanical challenges.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
