biology

Jun dimerization protein 2

Jun dimerization protein 2 is a biology topic covered in the lgStudy science library. This page brings together a partial reference excerpt, illustrations, worked examples, real-world applications and a short study plan, so you can understand Jun dimerization protein 2 rather than just read about it. In short: Jun dimerization protein 2 (JUNDM2) is a protein that in humans is encoded by the JDP2 gene. The Jun dimerization protein is a member of the AP-1 family of transcription factors.

Key takeaways

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Reference excerpt

Jun dimerization protein 2 (JUNDM2) is a protein that in humans is encoded by the JDP2 gene. The Jun dimerization protein is a member of the AP-1 family of transcription factors. JDP 2 was found by a Sos-recruitment system, to dimerize with c-Jun to repress AP-1-mediated activation. It was later identified by the yeast-two hybrid system to bind to activating transcription factor 2 (ATF2) to repress ATF-mediated transcriptional activation. JDP2 regulates 12-O-tetradecanoylphorbol-13-acetate (TPA) response element (TRE)- and cAMP-responsive element (CRE)-dependent transcription. The JDP2 gene is located on human chromosome 14q24.3 (46.4 kb, 75,427,715 bp to 75,474,111 bp) and mouse chromosome 12 (39 kb, 85,599,105 bp to 85,639,878 bp), which is located at about 250 kbp in the Fos-JDP2-BATF locus. Alternative splicing of JDP2 generates at least two isoforms. The protein JDP2 has 163 amino acids, belongs to the family of basic leucine zipper (bZIP), and shows high homology with the ATF3 bZIP domain. The bZIP domain includes the amino acids from position 72 to 135, the basic motif from position 74 to 96, and the leucine zipper from 100 to 128. The molecular weight of the canonical JDP2 is 18,704 Da. The histone-binding region is located from position 35 to 72 and the inhibition of the histone acetyltransferase (INHAT) region is from position 35 to 135, which is located before the DNA-binding domain. JDP2 is expressed ubiquitously but is detected mainly in the cerebellum, brain, lung, and testis. A JDP2 single nucleotide polymorphism (SNP) was detected in Japanese, Korean, and Dutch cohorts, and is associated with an increased risk of intracranial aneurysms.

Posttranscriptional and post translational modifications Phosphorylation of the threonine (Thr) residue at position 148 is mediated by c-Jun N-terminal kinase (MAPK8; JNK1) and p38 MAPK. Phosphorylated ATF2 inhibits the formation with JDP2 in vitro while phosphorylated JDP2 undergoes proteosomal degradation. It contains putative SUMO modification of lysine (Lys) residue at position 65, and recruits interferon regulatory factor 2 binding protein 1 (IRF2BP1), which acts as an E3 ligase. Phosphorylation of Thr at position 148 is detected in response to various stress conditions such as UV irradiation, oxidative stress, and anisomycin treatment or JDP2 is also regulated by other kinases such as p38 MAPK and doublecortin like protein kinase. Polyubiquitination of JDP2 protein is induced by IRF2BP1. JDP2 displays histone-binding and histone-chaperone activity. and inhibition of p300/CBP induced histone acetylation (INHAT). JDP2 recruits histone deacetylases HDAC1 and HDAC2, HDAC6 and HDAC3. JDP2 has INHAT activity and inhibits histone methylation in vitro.

Function

Phenotypes of gene knockout and transgenic mice Gene knockout mice have a shorter tail, are smaller, have low neutrophil count. and cell proliferation, and commit to cell cycle arrest because of AP-1 repression. TransgenicJDP2 mice display atrial dilation and myocardial hypertrophy.

Dimer formation and interacting molecules JDP2 functions as a transcription activator or repressor depending on the leucine zipper protein member it is associated with. JDP2 forms a homodimer or heterodimer with c-Jun, JUNB, JUND, Fra2, ATF2. and acts as a general repressor. On the other hand, JDP2 form a stable heterodimer with CHOP10 to enhance TRE- but not CRE-dependent transcription. In addition, JDP2 has been shown to directly associate with the progesterone receptor (PR) and functionally acts as a coactivator of progesterone-dependent PR-mediated gene transcription. Other proteins such as interferon regulatory factor-2-binding protein-1 (IRF2BP1). CCAAT/enhancer-binding protein gamma (C/EBPγ), HDAC3 and HDAC6 have also been demonstrated to associate with JDP2.

Cell differentiation JDP2 plays a role in cell differentiation in several systems. Ectopic expression of JDP2 inhibits the retinoic acid-induced differentiation of F9 cells and adipocyte differentiation. By contrast, JDP2 induces terminal muscle cell differentiation in C2 myoblasts and reduces the tumorigenicity of rhabdomyosarcoma cells and restored their ability to differentiate into myotubes. It is also reported that JDP2 plays an important role in the RANK-mediated osteoclast differentiation. Further, JDP2 is involved in neutrophil differentiation and transcription factor Tbx3-mediated osteoclastogenesis for host defense and bone homeostasis. Methylome mapping suggests that JDP2 plays a role in cell progenitor differentiation of megakaryocytes.

Regulation of cell cycle and p53 signaling JDP2 induces cell cycle arrest through cyclin D, p53, and cyclin A transcription, by increasing JUNB, JUND, and Fra2, and by decreasing c-JUN through the loss of p27Kip1. JDP2 downregulates p53 transcription, which promotes leukemogenesis. Mouse p53 protein negatively regulates the JDP2 promoter in F9 cells as part of the JDP2˗p53 autoregulatory circuit. By contrast, JDP2-knockout mice exhibit in downregulation of p53 and p21 proteins.

Apoptosis and senescence JDP2 appears to be involved in the inhibition of apoptosis. Depletion of JDP2 induces cell death similar to apoptosis. A study also demonstrated that UV irradiation induces JDP2 expression, which in turn down-regulates expression of p53 and thereby protects cells from UV-mediated programmed cell death. Heart-specific JDP2 overexpression protects cardiomyocytes against hypertrophic growth and TGFβ–induced apoptosis. In other settings, JDP2 has been shown to play an important role in the regulation of cellular senescence. JDP2-deficient mouse embryonic fibroblasts are resistant to replicative senescence by recruiting polycomb-repressive complexes (PRC1 and PRC2) to the promoters at the p16Ink4a locus.

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Illustrations

Worked examples

Example 1 — a first encounter with Jun dimerization protein 2

Start with the simplest possible case. Write down what Jun dimerization protein 2 claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In biology, the smallest case is usually a single object, a single equation or a single measurement. Check that every symbol or term in your sentence has a meaning in that case.

Example 2 — changing one variable

Take the situation from Example 1 and change exactly one quantity: double it, halve it, or set it to zero. Predict what should happen to Jun dimerization protein 2 before you calculate. Comparing your prediction with the result is the fastest way to find out whether you understand the idea or only the words.

Example 3 — an exam-style question

Typical questions about Jun dimerization protein 2 ask you to (a) state it precisely, (b) apply it to given data, and (c) explain a limitation. Practise writing all three answers in under five minutes; the third part is what separates a full-mark answer from an average one.

Applications of Jun dimerization protein 2

In research: Jun dimerization protein 2 appears in biology research whenever the underlying quantities have to be modelled precisely. Papers usually cite it as a starting assumption and then explore where it breaks down.
In technology and industry: Engineering practice reuses Jun dimerization protein 2 in design rules, simulations and safety margins. Knowing the idea lets you read a specification sheet and understand why the numbers look the way they do.
In the classroom: Jun dimerization protein 2 is common in secondary-school and first-year university syllabi. It links to neighbouring topics Genes on human chromosome 14, Transcription factors, Wikipedia articles with corresponding academic peer reviewed articles, so understanding it makes those chapters shorter.
In everyday life: Look for Jun dimerization protein 2 outside the textbook — in sport, cooking, traffic, electronics or the sky above you. An example you found yourself is remembered far longer than one you were given.

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How to study Jun dimerization protein 2 in 20 minutes

Read the reference excerpt below once, without taking notes.
Close the page and write down what Jun dimerization protein 2 means in your own words.
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Frequently asked questions

What is Jun dimerization protein 2 in simple terms?

Jun dimerization protein 2 (JUNDM2) is a protein that in humans is encoded by the JDP2 gene. The Jun dimerization protein is a member of the AP-1 family of transcription factors.

Why does Jun dimerization protein 2 matter?

Because it connects several biology ideas at once: it gives you a definition you can apply, a quantity you can calculate, and a way to check whether a result is plausible.

How should I study Jun dimerization protein 2?

Read the excerpt, restate it from memory, then work through the examples and applications listed on this page. The five-step study plan above takes about twenty minutes.

What does this page cover?

It gives you a compact reference excerpt plus original lgStudy explanations, examples, applications and study material on Jun dimerization protein 2.