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Cleavage and polyadenylation specificity factor subunit 6

Definition:

Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery. Plays a role in mRNA export.; (Microbial infection) Binds HIV-1 capsid-nucleocapsid (HIV-1 CA-NC) complexes and might thereby promote the integration of the virus in the nucleus of dividing cells (in vitro).

References:

[1]. Andreas R Gruber, et al. Cleavage factor Im is a key regulator of 3' UTR length. RNA Biol. 2012 Dec;9(12):1405-12. [Content Brief]

[2]. Kirk M Brown, et al. A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im. Mol Cell. 2003 Dec;12(6):1467-76. [Content Brief]

[3]. Yong Zhu, et al. Molecular Mechanisms for CFIm-Mediated Regulation of mRNA Alternative Polyadenylation. Mol Cell. 2018 Jan 4;69(1):62-74.e4. [Content Brief]

[4]. Marc-David Ruepp, et al. Mammalian pre-mRNA 3' end processing factor CF I m 68 functions in mRNA export. Mol Biol Cell. 2009 Dec;20(24):5211-23. [Content Brief]

[5]. Sol Kim, et al. Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation. Genes Cells. 2010 Sep 1;15(9):1003-13. [Content Brief]

[6]. U Rüegsegger, et al. Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits. Mol Cell. 1998 Jan;1(2):243-53. [Content Brief]

[7]. U Rüegsegger, et al. Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors. J Biol Chem. 1996 Mar 15;271(11):6107-13. [Content Brief]

[8]. Qin Yang, et al. Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping. Structure. 2011 Mar 9;19(3):368-77. [Content Brief]

[9]. Kenneth A Matreyek, et al. Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity. PLoS Pathog. 2013;9(10):e1003693. [Content Brief]

[10]. Sabine Dettwiler, et al. Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization. J Biol Chem. 2004 Aug 20;279(34):35788-97. [Content Brief]

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