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Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions. Additionally we are shipping Junction Mediating and Regulatory Protein, P53 Cofactor Antibodies (64) and and many more products for this protein.
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In autophagosomes, the integrity of the WH2 domains allows JMY to promote actin nucleation, which is required for efficient autophagosome formation.
JMY was expressed in normal tissues and heterogeneously in different tumor types, with close correlation between cytoplasmic and nuclear expression.
JARID1A, JMY, and PTGER4 polymorphisms are related to ankylosing spondylitis in Chinese Han patients.
JMY is related to the severity of AS in Chinese Han patients.
actin assembly regulates nuclear import of JMY in response to DNA damage.
JMY is expressed at high levels in brain tissue, and in various cell lines JMY is predominantly cytoplasmic, with a minor fraction in the nucleus.
results establish the interplay between JMY and HIF-1alpha (show HIF1A Proteins) as a new mechanism that controls cell motility under hypoxic stress
Data demonstrate a pathway that links the cytoskeleton with the p53 (show TP53 Proteins) response, and further suggest that the ability of JMY to regulate actin and cadherin is instrumental in coordinating cell motility with the p53 (show TP53 Proteins) response.
JMY represents a new class of multifunctional actin assembly factor whose activity is regulated, at least in part, by sequestration in the nucleus.
JMY drives vesicular trafficking in the trans-Golgi region and at ER-membrane contact sites, distinct from other Arp2 (show AICDA Proteins)/3 activators involved in vesicle transport processes such as the related WHAMM (show WHAMM Proteins) or WASH.
Results of the present study show that the nucleation-promoting factors JMY and WAVE2 (show WASF2 Proteins) are critical for cytokinesis during development of mouse embryos.
JMY is required for spindle migration, asymmetric division and cytokinesis during mouse oocyte maturation.
The protein and messenger RNA levels of JMY were decreased in aged oocytes, but the levels were normal in caffeine-treated aged oocytes.
JMY is a modulator of neuritogenesis
These results define a new functional relationship between the p53 (show TP53 Proteins) cofactor JMY and Mdm2 (show MDM2 Proteins), and indicate that transcription cofactors that facilitate p53 (show TP53 Proteins) activity are important targets for Mdm2 (show MDM2 Proteins) in suppressing the p53 (show TP53 Proteins) response.
Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions. In nucleus, acts as a cofactor that increases p53/TP53 response. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor for both branched and unbranched actin filaments. Activates the Arp2/3 complex to induce branched actin filament networks. Also catalyzes actin polymerization in the absence of Arp2/3, creating unbranched filaments. Contributes to cell motility by controlling actin dynamics.
junction mediating and regulatory protein, p53 cofactor
, junction-mediating and regulatory protein
, junction-mediating and -regulatory protein
, WAS protein homology region 2 domain containing 1-like 3
, p300 transcriptional cofactor JMY