Biology:RNF144A

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

RNF144A is an E3 ubiquitin ligase belonging to the RING-between RING (RBR) family of ubiquitin ligases, whose specific members have been shown to function as RING-HECT hybrid E3 ligases.[1][2][3] RNF144A is most closely related to RNF144B at the protein level, and the two proteins together comprise a subdomain within the RBR family of proteins.[4][5][6] The ubiquitin ligase activity of RNF144A catalyzes ubiquitin linkages at the K6-, K11- and K48- positions of ubiquitin in vitro, and is regulated by self-association through its transmembrane domain.[7][8]

The biological functions of RNF144A is/are relatively unknown beyond its intrinsic enzymatic activity. Somatic mutations of RNF144A have been catalogued in cancer genetic databases in several primary human tumors, including breast, stomach, lymphoma, glioblastoma, uterine and lung cancers. Other members of the RBR family have been associated with neurological and immunological diseases, most notably parkin, HOIL-1L and HOIP(RNF31).[9][10][11][12]

Current known substrates of RNF144A targeted for degradation are proteins involved in DNA repair, heatshock/chaperone function and signalling, consistent with the predominant association of this protein with cancer, and include (DNA-PKcs), PARP1, HSPA2, BMI1, and RAF1.[13][14][15][16][17]

See also

References

  1. ↑ "UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids". Nature 474 (7349): 105–8. June 2011. doi:10.1038/nature09966. PMID 21532592. 
  2. ↑ "RNF144A ring finger protein 144A [Homo sapiens (human) - Gene - NCBI"]. National Center for Biotechnology Information, U.S. National Library of Medicine. https://www.ncbi.nlm.nih.gov/gene/9781. 
  3. ↑ "RNF144A - E3 ubiquitin-protein ligase RNF144A - Homo sapiens (Human) - RNF144A gene & protein". UniProt. https://www.uniprot.org/uniprot/P50876. 
  4. ↑ "RING-Between-RING E3 Ligases: Emerging Themes amid the Variations". Journal of Molecular Biology 429 (22): 3363–3375. November 2017. doi:10.1016/j.jmb.2017.08.008. PMID 28827147. 
  5. ↑ "RBR E3 ubiquitin ligases: new structures, new insights, new questions". The Biochemical Journal 458 (3): 421–37. March 2014. doi:10.1042/BJ20140006. PMID 24576094. PMC 3940038. https://portlandpress.com/biochemj/article/458/3/421-437/46554. 
  6. ↑ "The ring between ring fingers (RBR) protein family". Genome Biology 8 (3): 209. 2007. doi:10.1186/gb-2007-8-3-209. PMID 17367545. 
  7. ↑ "Ubiquitin Linkage-Specific Affimers Reveal Insights into K6-Linked Ubiquitin Signaling". Molecular Cell 68 (1): 233–246.e5. October 2017. doi:10.1016/j.molcel.2017.08.020. PMID 28943312. 
  8. ↑ "Regulation of RNF144A E3 Ubiquitin Ligase Activity by Self-association through Its Transmembrane Domain". The Journal of Biological Chemistry 290 (38): 23026–38. September 2015. doi:10.1074/jbc.M115.645499. PMID 26216882. 
  9. ↑ "The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease". Neuron 85 (2): 257–73. January 2015. doi:10.1016/j.neuron.2014.12.007. PMID 25611507. 
  10. ↑ "Second Case of HOIP Deficiency Expands Clinical Features and Defines Inflammatory Transcriptome Regulated by LUBAC". Frontiers in Immunology 10: 479. 2019-03-18. doi:10.3389/fimmu.2019.00479. PMID 30936877. 
  11. ↑ "Human HOIP and LUBAC deficiency underlies autoinflammation, immunodeficiency, amylopectinosis, and lymphangiectasia". The Journal of Experimental Medicine 212 (6): 939–51. June 2015. doi:10.1084/jem.20141130. PMID 26008899. 
  12. ↑ "Immunodeficiency, autoinflammation and amylopectinosis in humans with inherited HOIL-1 and LUBAC deficiency". Nature Immunology 13 (12): 1178–86. December 2012. doi:10.1038/ni.2457. PMID 23104095. 
  13. ↑ "RNF144A, an E3 ubiquitin ligase for DNA-PKcs, promotes apoptosis during DNA damage". Proceedings of the National Academy of Sciences of the United States of America 111 (26): E2646-55. July 2014. doi:10.1073/pnas.1323107111. PMID 24979766. Bibcode: 2014PNAS..111E2646H. 
  14. ↑ "RBR-type E3 ubiquitin ligase RNF144A targets PARP1 for ubiquitin-dependent degradation and regulates PARP inhibitor sensitivity in breast cancer cells". Oncotarget 8 (55): 94505–94518. November 2017. doi:10.18632/oncotarget.21784. PMID 29212245. 
  15. ↑ "RNF144A functions as a tumor suppressor in breast cancer through ubiquitin ligase activity-dependent regulation of stability and oncogenic functions of HSPA2". Cell Death and Differentiation 27 (3): 1105–1118. August 2019. doi:10.1038/s41418-019-0400-z. PMID 31406303. 
  16. ↑ "Targeting glioma stem cells through combined BMI1 and EZH2 inhibition". Nature Medicine 23 (11): 1352–1361. November 2017. doi:10.1038/nm.4415. PMID 29035367. 
  17. ↑ RNF144A shapes the hierarchy of cytokine signaling to provide protective immunity against influenza. 2019-09-26. doi:10.1101/782680. 



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