JMY

Official Full Name

junction mediating and regulatory protein, p53 cofactor

Organism

Homo sapiens

GeneID

133746

Background

Enables microtubule binding activity. Involved in cellular response to starvation. Located in autophagosome membrane; cell leading edge; and cytoplasmic vesicle. [provided by Alliance of Genome Resources, Feb 2025]

Synonyms

WHAMM2; WHDC1L3;

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Detailed Information

Recent Research

The role of JMY in embryo development before implantation

JMY is unique because it has a dual role. Ligation-mediated and regulatory proteins (JMY) are regulators of transcription and actin filament assembly. JMY, as a transcriptional regulator, binds to p300 and promotes p53-mediated transcriptional responses. At the same time, JMY, as a key nucleation promoting factor (NPF), is involved in the development of pig embryos by regulating the NPF-Arp2-actin pathway. Pig embryos express JMY mRNA and protein, and JMY protein is transferred from cytoplasm to nuclear development stage in the late embryo. Knockout of JMY by RNA interference significantly reduced the rate of blastocyst development and verified its role in porcine embryo development. Injection of JMY dsRNA also impairs actin and Arp2 expression and co-injection of actin and Arp2 mRNA partially rescued blastocyst development.

JMY binds and activates the Arp2 / 3 complex, which is involved in cell migration. The region of JMY is responsible for its actin nucleation activity and interaction with the Arp2/3 complex located in the C-terminal WWWCA region, consisting of three tandemly composed actin monomer binding sequences (Wiskott-Aldrich syndrome protein homology 2 [WH2] domain) and Arp2 / 3 binding center and acidic (CA) region. JMY is one of the essential components of asymmetrical splitting of oocytes in mice and pigs. The Arp2 / 3 complex and various NPFs, including WAVE2 and JMY, are important for early mouse embryogenesis. However, the exact role and function of JMY in early pig embryo development is not well understood.

The role of JMY in asymmetrically splitting pig oocytes

Porcine oocytes express JMY mRNA and protein, and mRNA expression levels decrease during oocyte maturation. JMY knockdown also down-regulated the mRNA and protein levels of actin and Arp2/3. Furthermore, JMY accumulates in the nucleus in response to DNA damage, and JMY knockdown inhibits DNA damage mediated p53 activation. In conclusion, as a regulator of actin nucleation promoting factor and DNA activator during DNA damage in DNA oocytes, JMY plays an important role in oocyte maturation.

Roles of JMY in cytoskeletal remodeling and actin assembly

The C-terminus of JMY comprises a canonical VCA-module, the sequence signature of Arp2/3 complex activators. In addition, tandem repeats of three WH2 (V or most recently W) domains enabled JMY to perform Arp2 / 3 independent actin assembly. The motility of cytoplasmic function of JMY is abolished by DNA damage and nuclear translocation of JMY. By mass spectrometry, it was found that JMY localizes to the dynamic vesicle-tubular structure throughout the cytoplasm, which is modified with actin and Arp2/3 complexes. In addition, the JMY moiety co-localizes and interacts with VAP-A, which participates in vesicle-based trafficking. Finally, overexpression of JMY causes the Golgi to diffuse through the loss of cross-site and affect VSV-G transport. This suggests that it is different from other Arp2 / 3 activators involved in the vesicle trafficking process, such as related WHAMM or WASH. JMY drives vesicle trafficking in the trans-Golgi region and the ER-membrane contact site (MCS).

The role of JMY in tumor suppression

JMY is a dual-function p300-binding protein: by enhancing P53 transcription in the nucleus, it plays an important role in the response of cells to DNA damage, while promoting actin filament assembly in the cytoplasm; it induces cell movement in vitro. Researchers believe that JMY may act as a tumor suppressor or oncogene. It has been reported that JMY is expressed in normal tissues, heterogeneously expressed in different tumor types, and closely related to cytoplasmic and nuclear expression. Most notably, expression is absent in certain invasive carcinomas compared to normal tissues and breast carcinoma in situ, which is consistent with putative inhibition. However, as in lymph node metastasis, JMY expression is higher than primary colorectal cancer and head and neck cancer, which may also have carcinogenic properties depending on the cellular environment, by increasing motility and metastatic potential.

References:

Schlüter K, et al. JMY is involved in anterograde vesicle trafficking from the trans-Golgi network. European Journal of Cell Biology, 2014, 93(5-6):194-204.
Adighibe O, et al. JMY protein, a regulator of P53 and cytoplasmic actin filaments, is expressed in normal and neoplastic tissues. Virchows Archiv, 2014, 465(6):715-722.
Lin Z, et al. JMY Functions as Actin Nucleation-Promoting Factor and Mediator for p53-Mediated DNA Damage in Porcine Oocytes. Plos One, 2014, 9(10):e109385.
Lin Z, et al. JMY Functions as Actin Nucleation-Promoting Factor and Mediator for p53-Mediated DNA Damage in Porcine Oocytes. Plos One, 2014, 9(10):e109385.

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