Reactome | NUDT21 dimerizes

NUDT21 dimerizes

Stable Identifier

R-HSA-9968762

Type

Reaction [binding]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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NUDT21 (CPSF5, also known as CFIm25), a Nudix hydrolase superfamily member, forms a head-to-tail homodimer that constitutes the structural core of the cleavage factor I (CF I, CFIm) complex (Kim et al. 2010; Yang et al. 2011). Each monomer contributes an antiparallel β-strand interface that stabilizes the dimer and creates two symmetric RNA-binding surfaces recognizing UGUA motifs upstream of poly(A) sites (PASs). The NUDT21 homodimer scaffolds a homo- or heterodimer of CPSF6 (CFIm68) and/or CPSF7 (CFIm59), forming the functional CF I heterotetramer that loops RNA and promotes distal PAS usage (Yang et al. 2011). Loss or depletion of NUDT21 shortens 3′ UTRs and alters gene regulation in many cell types, highlighting its role in alternative polyadenylation and tumor suppression (Kubo et al., 2006; Masamha et al., 2014; Li et al., 2015; Brumbaugh et al. 2017; reviewed in Xiao et al., 2023).

Literature References

PubMed ID	Title	Journal	Year
20695905	Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation Kim, S, Yamamoto, J, Chen, Y, Aida, M, Wada, T, Handa, H, Yamaguchi, Y	Genes Cells	2010
21295486	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 Yang, Q, Coseno, M, Gilmartin, GM, Doublié, S	Structure	2011