In today's world, Y box binding protein 1 is a relevant topic that has captured the attention of millions of people around the world. Whether due to its impact on society, its influence on popular culture or its importance in academia, Y box binding protein 1 has become a topic of general interest that has generated heated discussions and passionate debates. From its emergence to its evolution today, Y box binding protein 1 has left an indelible mark on history, making it a topic worth exploring in depth to understand its true scope and meaning in today's world.
Y box binding protein 1 also known as Y-box transcription factor or nuclease-sensitive element-binding protein 1 is a protein that in humans is encoded by the YBX1gene.[5] YBX1 is an RNA binding protein[6] that stabilises messenger RNAs modified with N6-methyladenosine.[7]
Clinical significance
YBX1 is a potential drug target in cancer therapy.[8] YB-1 helps the replication of adenovirus type 5, a commonly used vector in gene therapy.[8] Thus, YB-1 can cause an "oncolytic" effect in YB-1 positive cancer cells treated with adenoviruses.
DNA repair
The mitochondria of human cells possess a repair pathway for DNAbase pair mismatches that is distinct from the DNA mismatch repair pathway of the nucleus.[9] This mitochondrial pathway includes participation of Y box binding protein 1 (designated YB-1 or YBX1), that likely acts in the mismatch binding and recognition steps of mismatch repair.[9]
Interactions
Y box binding protein 1 has been shown to interact with:
^ abKojic S, Medeot E, Guccione E, Krmac H, Zara I, Martinelli V, et al. (May 2004). "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle". Journal of Molecular Biology. 339 (2): 313–325. doi:10.1016/j.jmb.2004.03.071. PMID15136035.
^Ise T, Nagatani G, Imamura T, Kato K, Takano H, Nomoto M, et al. (January 1999). "Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with proliferating cell nuclear antigen". Cancer Research. 59 (2): 342–346. PMID9927044.
^Chibi M, Meyer M, Skepu A, G Rees DJ, Moolman-Smook JC, Pugh DJ (December 2008). "RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1". Journal of Molecular Biology. 384 (4): 908–916. doi:10.1016/j.jmb.2008.09.060. PMID18851979.
Sakura H, Maekawa T, Imamoto F, Yasuda K, Ishii S (December 1988). "Two human genes isolated by a novel method encode DNA-binding proteins containing a common region of homology". Gene. 73 (2): 499–507. doi:10.1016/0378-1119(88)90514-8. PMID2977358.
Kudo S, Mattei MG, Fukuda M (July 1995). "Characterization of the gene for dbpA, a family member of the nucleic-acid-binding proteins containing a cold-shock domain". European Journal of Biochemistry. 231 (1): 72–82. doi:10.1111/j.1432-1033.1995.tb20672.x (inactive 13 November 2025). PMID7628487.{{cite journal}}: CS1 maint: DOI inactive as of November 2025 (link)
Ise T, Nagatani G, Imamura T, Kato K, Takano H, Nomoto M, et al. (January 1999). "Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with proliferating cell nuclear antigen". Cancer Research. 59 (2): 342–346. PMID9927044.
1h95: SOLUTION STRUCTURE OF THE SINGLE-STRANDED DNA-BINDING COLD SHOCK DOMAIN (CSD) OF HUMAN Y-BOX PROTEIN 1 (YB1) DETERMINED BY NMR (10 LOWEST ENERGY STRUCTURES)