factor interacting with PAPOLA and CPSF1
Dernière mise à jour 5 Jul 2022
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La FIP1L1 gene provides instructions for making part of a protein complex named cleavage and polyadenylation specificity factor (CPSF). This complex of proteins plays an important role in processing molecules called messenger RNAs (mRNAs), which serve as the genetic blueprints for making proteins. The CPSF protein complex helps add a string of the RNA building block adenine to the mRNA, creating a polyadenine tail or poly(A) tail. The poly(A) tail is important for stability of the mRNA and for protein production from the blueprint.
Normal function
La FIP1L1 gene provides instructions for making part of a protein complex named cleavage and polyadenylation specificity factor (CPSF). This complex of proteins plays an important role in processing molecules called messenger RNAs (mRNAs), which serve as the genetic blueprints for making proteins. The CPSF protein complex helps add a string of the RNA building block adenine to the mRNA, creating a polyadenine tail or poly(A) tail. The poly(A) tail is important for stability of the mRNA and for protein production from the blueprint.
Conditions referring to this gene or chromosome
Other names
FIP1-like 1 protein
FIP1_HUMAN
hFip1
pre-mRNA 3'-end-processing factor FIP1
Rhe
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Lectures complémentaires et références
- factor interacting with PAPOLA and CPSF1; MedlinePlus, National Library of Medicine.
- Bain BJ. Relationship between idiopathic hypereosinophilic syndrome, eosinophilic leukemia, and systemic mastocytosis. Am J Hematol. 2004 Sep;77(1):82-5. doi: 10.1002/ajh.20088.
- Buitenhuis M, Verhagen LP, Cools J, Coffer PJ. Molecular mechanisms underlying FIP1L1-PDGFRA-mediated myeloproliferation. Cancer Res. 2007 Apr 15;67(8):3759-66. doi: 10.1158/0008-5472.CAN-06-4183.
- Cools J, DeAngelo DJ, Gotlib J, Stover EH, Legare RD, Cortes J, Kutok J, Clark J, Galinsky I, Griffin JD, Cross NC, Tefferi A, Malone J, Alam R, Schrier SL, Schmid J, Rose M, Vandenberghe P, Verhoef G, Boogaerts M, Wlodarska I, Kantarjian H, Marynen P, Coutre SE, Stone R, Gilliland DG. A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as a therapeutic target of imatinib in idiopathic hypereosinophilic syndrome. N Engl J Med. 2003 Mar 27;348(13):1201-14. doi: 10.1056/NEJMoa025217.
- Fukushima K, Matsumura I, Ezoe S, Tokunaga M, Yasumi M, Satoh Y, Shibayama H, Tanaka H, Iwama A, Kanakura Y. FIP1L1-PDGFRalpha imposes eosinophil lineage commitment on hematopoietic stem/progenitor cells. J Biol Chem. 2009 Mar 20;284(12):7719-32. doi: 10.1074/jbc.M807489200. Epub 2009 Jan 14.
- Kaufmann I, Martin G, Friedlein A, Langen H, Keller W. Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase. EMBO J. 2004 Feb 11;23(3):616-26. doi: 10.1038/sj.emboj.7600070. Epub 2004 Jan 29.
- Roufosse FE, Goldman M, Cogan E. Hypereosinophilic syndromes. Orphanet J Rare Dis. 2007 Sep 11;2:37. doi: 10.1186/1750-1172-2-37.
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