Fibroblast growth factor 2 (FGF-2) is a novel substrate for arginine methylation by PRMT5. (Q39904653)

15 September 2017

title

Fibroblast growth factor 2 (FGF-2) is a novel substrate for arginine methylation by PRMT5. (English)

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15 September 2017

author name string

Alexander-Francisco Bruns

series ordinal

1

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15 September 2017

Claudia Grothe

series ordinal

2

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15 September 2017

Peter Claus

series ordinal

3

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15 September 2017

publication date

1 January 2009

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15 September 2017

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15 September 2017

volume

390

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15 September 2017

issue

1

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15 September 2017

page(s)

59-65

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Protein arginine methyltransferases: from unicellular eukaryotes to humans

15 September 2017

cites work

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Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains

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The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies

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Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.

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PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins

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JMJD6 is a histone arginine demethylase

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Differential intranuclear localization of fibroblast growth factor-2 isoforms and specific interaction with the survival of motoneuron protein

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Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1

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A GR-motif functions in nuclear accumulation of the large FGF-2 isoforms and interferes with mitogenic signalling

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Nuclear localization of mouse fibroblast growth factor 2 requires N-terminal and C-terminal sequences

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Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN).

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SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets

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The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins

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Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes

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The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity

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The NH2-terminal extension of high molecular weight bFGF is a nuclear targeting signal

21 January 2018

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Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family

21 January 2018

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Nuclear and nucleolar localization of 18-kDa fibroblast growth factor-2 is controlled by C-terminal signals

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An amino-terminally extended and post-translationally modified form of a 25kD basic fibroblast growth factor

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Functional diversity of FGF-2 isoforms by intracellular sorting

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AS1411 alters the localization of a complex containing protein arginine methyltransferase 5 and nucleolin

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Fibroblast growth factor (FGF)-2 and FGF receptor 3 are required for the development of the substantia nigra, and FGF-2 plays a crucial role for the rescue of dopaminergic neurons after 6-hydroxydopamine lesion

21 January 2018

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Thrombin cleaves the high molecular weight forms of basic fibroblast growth factor (FGF-2): a novel mechanism for the control of FGF-2 and thrombin activity

21 January 2018

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Fibroblast growth factor-2(23) binds directly to the survival of motoneuron protein and is associated with small nuclear RNAs.

21 January 2018

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21 January 2018

Identifiers

DOI

10.1515/BC.2009.001

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15 September 2017

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