2023
DOI: 10.1016/j.apsb.2022.11.025
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HBXIP blocks myosin-IIA assembly by phosphorylating and interacting with NMHC-IIA in breast cancer metastasis

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Cited by 4 publications
(1 citation statement)
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“…Unlike the ubiquitin-proteasome pathway, HBXIP mainly regulates the acetylation of target proteins by modulating acetylases. For example, tissue chip technology showed that HBXIP expression in tumor cells was related to HOXB13 and STEM20 like kinase1 (MST1) ( 62 , 63 ); further research into the mechanism found that HBXIP can change the acetylation levels of HOXB13 and tumor suppressor proteinMST1 via the acetylase P300 and Histone deacetylase 6 (HDAC6) to regulate chaperone-mediated autophagy HBXIP also recruits protein kinase CβII to stimulate phosphorylation of non-muscle heavy chain myosin IIA, thereby enhancing breast cancer invasion ( 64 ).…”
Section: Hbxip and Tumorsmentioning
confidence: 99%
“…Unlike the ubiquitin-proteasome pathway, HBXIP mainly regulates the acetylation of target proteins by modulating acetylases. For example, tissue chip technology showed that HBXIP expression in tumor cells was related to HOXB13 and STEM20 like kinase1 (MST1) ( 62 , 63 ); further research into the mechanism found that HBXIP can change the acetylation levels of HOXB13 and tumor suppressor proteinMST1 via the acetylase P300 and Histone deacetylase 6 (HDAC6) to regulate chaperone-mediated autophagy HBXIP also recruits protein kinase CβII to stimulate phosphorylation of non-muscle heavy chain myosin IIA, thereby enhancing breast cancer invasion ( 64 ).…”
Section: Hbxip and Tumorsmentioning
confidence: 99%