1. Jarmolowski,A., Boelens,W.C., Izaurralde,E. and Mattaj,I.W. (1994)
Nuclear export of different classes of RNA is mediated by specific
factors. J. Cell Biol., 124, 627–635.
2. Ohno,M., Segref,A., Kuersten,S. and Mattaj,I.W. (2002) Identity
elements used in export of mRNAs. Mol. Cell, 9, 659–671.
3. Jin,L., Guzik,B.W., Bor,Y., Rekosh,D. and Hammarskjold,M.-L.
(2003) Tap and NXT promote translation of unspliced mRNA. Genes
Dev., 17, 3075–3086.
4. Wiegand,H.L., Lu,S. and Cullen,B.R. (2003) Exon junction
complexes mediate the enhancing effect of splicing on mRNA
expression. Proc. Natl Acad. Sci. USA, 100, 11327–11332.
5. Kuersten,S., Segal,S.P., Verheyden,J., LaMartina,S.M. and
Goodwin,E.B. (2004) NXF-2, REF-1, and REF-2 affect the choice of
nuclear export pathway for tra-2 mRNA in C. elegans. Mol. Cell, 14,
599–610.
6. Li,M.W., Sletten,A.C., Lee,J., Pyles,K.D., Matkovich,S.J., Ory,D.S.
and Schaffer,J.E. (2017) Nuclear export factor 3 regulates localization
of small nucleolar RNAs. J. Biol. Chem., 292, 20228–20239.
7. Lei,H., Dias,A.P. and Reed,R. (2011) Export and stability of
naturally intronless mRNAs require specific coding region sequences
and the TREX mRNA export complex. Proc. Natl Acad. Sci. USA,
108, 17985–17990.
8. Izaurralde,E., Lewis,J., McGuigan,C., Jankowska,M.,
Darzynkiewicz,E. and Mattaj,I.W. (1994) A nuclear cap binding
protein complex involved in pre-mRNA splicing. Cell, 78, 657–668.
9. Hamm,J. and Mattaj,I.W. (1990) Monomethylated cap structures
facilitate RNA export from the nucleus. Cell, 63, 109–118.
10. Ohno,M., Segref,A., Bachi,A., Wilm,M. and Mattaj,I.W. (2000)
PHAX, a mediator of U snRNA nuclear export whose activity is
regulated by phosphorylation. Cell, 101, 187–198.
11. Cheng,H., Dufu,K., Lee,C.-S., Hsu,J.L., Dias,A. and Reed,R. (2006)
Human mRNA export machinery recruited to the 5 end of mRNA.
Cell, 127, 1389–1400.
12. Huang,Y. and Steitz,J.A. (2005) SRprises along a messenger’s
journey. Mol. Cell, 17, 613–615.
13. Le Hir,H., Izaurralde,E., Maquat,L.E. and Moore,M.J. (2000) The
spliceosome deposits multiple proteins 20–24 nucleotides upstream of
mRNA exon–exon junctions. EMBO J., 19, 6860–6869.
14. Gruter,P.,
Tabernero,C., von Kobbe,C., Schmitt,C., Saavedra,C.,
Bachi,A., Wilm,M., Felber,B.K. and Izaurralde,E. (1998) TAP, the
human homolog of Mex67p, mediates CTE-dependent RNA export
from the nucleus. Mol. Cell, 1, 649–659.
Downloaded from https://academic.oup.com/nar/article/51/3/1393/6976059 by KYOTO UNIV. SURIKAISEKI-KEN TOSHO user on 25 January 2024
strengthens the RNA-binding activity of hnRNP C. RNA
binding of hnRNP C was previously shown to be weakened
by the phosphorylation of serine residues mainly within
the ACIDIC region (45–47). These findings suggested that
phosphorylation of the ACIDIC region induced the disassembly of the tetramer, thereby decreasing RNA binding. A previous study indicated that the hnRNP complex,
in which hnRNP C is a core component, was assembled
and disassembled during cell cycle progression as a result of mitosis-specific phosphorylation of hnRNP C (48).
The phosphorylation-induced disassembly of the hnRNP C
tetramer may explain hnRNP disassembly from mRNA.
1408 Nucleic Acids Research, 2023, Vol. 51, No. 3
36.
37.
38.
39.
40.
41.
42.
43.
44.
45.
46.
47.
48.
49.
50.
51.
52.
53.
54.
binding to RNA is a novel bZIP-like RNA binding domain. RNA, 2,
1139–1152.
Jiang,W., Guo,X. and Bhavanandan,V.P. (1998) Four distinct regions
in the auxiliary domain of heterogeneous nuclear ribonucleoprotein
C-related proteins. Biochim. Biophys. Acta, 1399, 229–233.
Barnett,S.F., Friedman,D.L. and LeStourgeon,W.M. (1989) The C
proteins of HeLa 40S nuclear ribonucleoprotein particles exist as
anisotropic tetramers of (C1)3 C2. Mol. Cell. Biol., 9, 492–498.
Whitson,S.R., LeStourgeon,W.M. and Krezel,A.M. (2005) Solution
structure of the symmetric coiled coil tetramer formed by the
oligomerization domain of hnRNP C: implications for biological
function. J. Mol. Biol., 350, 319–337.
Shahied,L., Braswell,E.H., LeStourgeon,W.M. and Krezel,A.M.
(2001) An antiparallel four-helix bundle orients the high-affinity
RNA binding sites in hnRNP C: a mechanism for RNA chaperonin
activity. J. Mol. Biol., 305, 817–828.
Kershaw,C.J. and O’Keefe,R.T. (2013) Splint ligation of RNA with
T4 DNA ligase. Methods Mol. Biol., 941, 257–269.
Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.
et al. (2012) Insights into RNA biology from an atlas of mammalian
mRNA-binding proteins. Cell, 149, 1393–1406.
Baltz,A.G., Munschauer,M., Schwanh¨ausser,B., Vasile,A.,
Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
Milek,M. et al. (2012) The mRNA-bound proteome and its global
occupancy profile on protein-coding transcripts. Mol. Cell, 46,
674–690.
Wang,D.O., Ninomiya,K., Mori,C., Koyama,A., Haan,M.,
Kitabatake,M., Hagiwara,M., Chida,K., Takahashi,S.-I., Ohno,M.
et al. (2017) Transport granules bound with nuclear cap binding
protein and exon junction complex are associated with microtubules
and spatially separated from eIF4E granules and P bodies in human
neuronal processes. Front. Mol. Biosci., 4, 93.
Barnett,S.F., LeStourgeon,W.M. and Friedman,D.L. (1988) Rapid
purification of native C protein from nuclear ribonucleoprotein
particles. J. Biochem. Biophys. Methods, 16, 87–97.
Stone,J.R., Maki,J.L. and Collins,T. (2003) Basal and hydrogen
peroxide stimulated sites of phosphorylation in heterogeneous nuclear
ribonucleoprotein C1/C2. Biochemistry, 42, 1301–1308.
Mayrand,S.H., Dwen,P. and Pederson,T. (1993) Serine/threonine
phosphorylation regulates binding of C hnRNP proteins to
pre-mRNA. Proc. Natl Acad. Sci. USA, 90, 7764–7768.
Kattapuram,T., Yang,S., Maki,J.L. and Stone,J.R. (2005) Protein
kinase CK1alpha regulates mRNA binding by heterogeneous nuclear
ribonucleoprotein C in response to physiologic levels of hydrogen
peroxide. J. Biol. Chem., 280, 15340–15347.
Pinol-Roma,S.
and Dreyfuss,G. (1993) Cell cycle-regulated
phosphorylation of the pre-mRNA-binding (heterogeneous nuclear
ribonucleoprotein) C proteins. Mol. Cell. Biol., 13, 5762–5770.
Ford,L.P., Suh,J.M., Wright,W.E. and Shay,J.W. (2000)
Heterogeneous nuclear ribonucleoproteins C1 and C2 associate with
the RNA component of human telomerase. Mol. Cell. Biol., 20,
9084–9091.
Hallais,M., Pontvianne,F., Andersen,P.R., Clerici,M., Lener,D.,
Benbahouche,N.E.H., Gostan,T., Vandermoere,F., Robert,M.-C.,
Cusack,S. et al. (2013) CBC–ARS2 stimulates 3 -end maturation of
multiple RNA families and favors cap-proximal processing. Nat.
Struct. Mol. Biol., 20, 1358–1366.
Gruber,J.J., Zatechka,D.S., Sabin,L.R., Yong,J., Lum,J.J., Kong,M.,
Zong,W.-X., Zhang,Z., Lau,C.-K., Rawlings,J. et al. (2009) Ars2 links
the nuclear cap-binding complex to RNA interference and cell
proliferation. Cell, 138, 328–339.
Gruber,J.J., Olejniczak,S.H., Yong,J., La Rocca,G., Dreyfuss,G. and
Thompson,C.B. (2012) Ars2 promotes proper replication-dependent
histone mRNA 3 end formation. Mol. Cell, 45, 87–98.
Giacometti,S., Benbahouche,N.E.H., Domanski,M., Robert,M.-C.,
Meola,N., Lubas,M., Bukenborg,J., Andersen,J.S., Schulze,W.M.,
Verheggen,C. et al. (2017) Mutually exclusive CBC-containing
complexes contribute to RNA fate. Cell Rep., 18, 2635–2650.
Schulze,W.M., Stein,F., Rettel,M., Nanao,M. and Cusack,S. (2018)
Structural analysis of human ARS2 as a platform for
co-transcriptional RNA sorting. Nat. Commun., 9, 1701.
Downloaded from https://academic.oup.com/nar/article/51/3/1393/6976059 by KYOTO UNIV. SURIKAISEKI-KEN TOSHO user on 25 January 2024
15. Le Hir,H., Gatfield,D., Izaurralde,E. and Moore,M.J. (2001) The
exon–exon junction complex provides a binding platform for factors
involved in mRNA export and nonsense-mediated mRNA decay.
EMBO J., 20, 4987–4997.
16. Masuyama,K., Taniguchi,I., Kataoka,N. and Ohno,M. (2004) RNA
length defines RNA export pathway. Genes Dev., 18, 2074–2085.
17. Fuke,H. and Ohno,M. (2008) Role of poly (A) tail as an identity
element for mRNA nuclear export. Nucleic Acids Res., 36, 1037–1049.
18. McCloskey,A., Taniguchi,I., Shinmyozu,K. and Ohno,M. (2012)
hnRNP C tetramer measures RNA length to classify RNA
polymerase II transcripts for export. Science, 335, 1643–1646.
19. Choi,Y.D. and Dreyfuss,G. (1984) Isolation of the heterogeneous
nuclear RNA–ribonucleoprotein complex (hnRNP): a unique
supramolecular assembly. Proc. Natl Acad. Sci. USA, 81, 7471–7475.
20. Samakina,O.P., Lukanidin,E.M., Molnar,J. and Georgiev,G.P. (1968)
Structural organization of nuclear complexes containing DNA-like
RNA. J. Mol. Biol., 33, 251–263.
21. Beyer,A.L., Christensen,M.E., Walker,B.W. and LeStourgeon,W.M.
(1977) Identification and characterization of the packaging proteins
of core 40S hnRNP particles. Cell, 11, 127–138.
22. Karn,J., Vidali,G., Boffa,L.C. and Allfrey,V.G. (1977)
Characterization of the non-histone nuclear proteins associated with
rapidly labeled heterogeneous nuclear RNA. J. Biol. Chem., 252,
7307–7322.
23. Huang,M., Rech,J.E., Northington,S.J., Flicker,P.F., Mayeda,A.,
Krainer,A.R. and LeStourgeon,W.M. (1994) The C-protein tetramer
binds 230 to 240 nucleotides of pre-mRNA and nucleates the
assembly of 40S heterogeneous nuclear ribonucleoprotein particles.
Mol. Cell. Biol., 14, 518–533.
24. Venables,J.P., Koh,C.-S., Froehlich,U., Lapointe,E., Couture,S.,
Inkel,L., Bramard,A., Paquet,E.R., Watier,V., Durand,M. et al.
(2008) Multiple and specific mRNA processing targets for the major
human hnRNP proteins. Mol. Cell. Biol., 28, 6033–6043.
25. Choi,Y.D., Grabowski,P.J., Sharp,P.A. and Dreyfuss,G. (1986)
Heterogeneous nuclear ribonucleoproteins: role in RNA splicing.
Science, 231, 1534–1539.
26. Zarnack,K., Konig,J.,
Tajnik,M., Martincorena,I., Eustermann,S.,
St´evant,I., Reyes,A., Anders,S., Luscombe,N.M. and Ule,J. (2013)
Direct competition between hnRNP C and U2AF65 protects the
transcriptome from the exonization of Alu elements. Cell, 152,
453–466.
27. Merrill,B.M., Barnett,S.F., LeStourgeon,W.M. and Williams,K.R.
(1989) Primary structure differences between proteins C1 and C2 of
HeLa 40S nuclear ribonucleoprotein particles. Nucleic Acids Res., 17,
8441–8449.
28. Dreyfuss,G., Matunis,M.J., Pinol-Roma,S.
and Burd,C.G. (1993)
hnRNP proteins and the biogenesis of mRNA. Annu. Rev. Biochem.,
62, 289–321.
29. Swanson,M.S., Nakagawa,T.Y., LeVan,K. and Dreyfuss,G. (1987)
Primary structure of human nuclear ribonucleoprotein particle C
proteins: conservation of sequence and domain structures in
heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding
proteins. Mol. Cell. Biol., 7, 1731–1739.
30. Konig,J.,
Zarnack,K., Rot,G., Curk,T., Kayikci,M., Zupan,B.,
Turner,D.J., Luscombe,N.M. and Ule,J. (2010) iCLIP reveals the
function of hnRNP particles in splicing at individual nucleotide
resolution. Nat. Struct. Mol. Biol., 17, 909–915.
31. Cienikov´a,Z., Jayne,S., Damberger,F.F., Allain,F.H.-T. and Maris,C.
(2015) Evidence for cooperative tandem binding of hnRNP C RRMs
in mRNA processing. RNA, 21, 1931–1942.
32. Gorlach,M.,
Wittekind,M., Beckman,R.A., Mueller,L. and
Dreyfuss,G. (1992) Interaction of the RNA-binding domain of the
hnRNP C proteins with RNA. EMBO J., 11, 3289–3295.
33. Soltaninassab,S.R., McAfee,J.G., Shahied-Milam,L. and
LeStourgeon,W.M. (1998) Oligonucleotide binding specificities of the
hnRNP C protein tetramer. Nucleic Acids Res., 26, 3410–3417.
34. McAfee,J.G., Soltaninassab,S.R., Lindsay,M.E. and
LeStourgeon,W.M. (1996) Proteins C1 and C2 of heterogeneous
nuclear ribonucleoprotein complexes bind RNA in a highly
cooperative fashion: support for their contiguous deposition on
pre-mRNA during transcription. Biochemistry, 35, 1212–1222.
35. McAfee,J.G., Shahied-Milam,L., Soltaninassab,S.R. and
LeStourgeon,W.M. (1996) A major determinant of hnRNP C protein
...
論文の公開元へ
