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Gene Review:

YTHDC1 - YTH domain containing 1

Homo sapiens

Synonyms: KIAA1966, YT521, YT521-B, YTH domain-containing protein 1

Wilkinson, F.L. et al., Imai, Y. et al., Rafalska, I. et al., Nayler, O. et al., Hartmann, A.M. et al.

Nayler, Hartmann, Stamm,

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Disease relevance of YTHDC1

Cloning of a gene, YT521, for a novel RNA splicing-related protein induced by hypoxia/reoxygenation [1].

High impact information on YTHDC1

Here, we show that the glutamic acid/arginine-rich domain protein YT521-B localizes to a novel subnuclear structure, the YT bodies [2].
On the basis of our experiments, we propose that YT521-B may participate in the assembly of genes into transcription centers, thereby allowing efficient regulation of gene expression [2].
Non-phosphorylated YT521-B changes alternative splice site selection of the IL-4 receptor, CD44 and SRp20, but phosphorylation of c-Abl minimizes this concentration dependent effect [3].
We show that YT521-B is tyrosine phosphorylated by c-Abl in the nucleus [3].
Tyrosine phosphorylation causes dispersion of YT521-B from YT bodies to the nucleoplasm [3].

Biological context of YTHDC1

YT521-B joins a growing list of candidates for a role in a gene expression model of the pathogenesis of EDMD [4].
A 'bipartite' binding site for YT521-B in emerin was identified using alanine substitution or disease-associated mutations in emerin [4].
Together, our data indicate that YT521-B and Sam68 may be part of a signal transduction pathway that influences splice site selection [5].
The YT521 cDNA is about 3200 bp long with an open reading frame encoding 712 amino acids [1].

Anatomical context of YTHDC1

Northern blot analysis revealed that YT521 mRNA expression was up-regulated in reoxygenated astrocytes [1].

Associations of YTHDC1 with chemical compounds

Induction of YT521 mRNA was mediated by endogenously generated reactive oxygen species, as it was suppressed by treatment of the cells with diphenyl iodonium which blocks oxygen-free radical formation by astrocytes [1].

Other interactions of YTHDC1

Inhibition by emerin of YT521-B-dependent splice site selection in vivo suggests that the interaction is physiologically significant [4].
Four out of five candidate interactors identified were nuclear proteins: lamin A, splicing factor YT521-B, proteasome subunit PA28 gamma and transcription factor vav-1 [4].
YT521-B is a ubiquitously expressed nuclear protein that changes alternative splice site usage in a concentration dependent manner [3].

References

Cloning of a gene, YT521, for a novel RNA splicing-related protein induced by hypoxia/reoxygenation. Imai, Y., Matsuo, N., Ogawa, S., Tohyama, M., Takagi, T. Brain Res. Mol. Brain Res. (1998) [Pubmed]
The ER repeat protein YT521-B localizes to a novel subnuclear compartment. Nayler, O., Hartmann, A.M., Stamm, S. J. Cell Biol. (2000) [Pubmed]
The intranuclear localization and function of YT521-B is regulated by tyrosine phosphorylation. Rafalska, I., Zhang, Z., Benderska, N., Wolff, H., Hartmann, A.M., Brack-Werner, R., Stamm, S. Hum. Mol. Genet. (2004) [Pubmed]
Emerin interacts in vitro with the splicing-associated factor, YT521-B. Wilkinson, F.L., Holaska, J.M., Zhang, Z., Sharma, A., Manilal, S., Holt, I., Stamm, S., Wilson, K.L., Morris, G.E. Eur. J. Biochem. (2003) [Pubmed]
The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn). Hartmann, A.M., Nayler, O., Schwaiger, F.W., Obermeier, A., Stamm, S. Mol. Biol. Cell (1999) [Pubmed]

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