Ordered Multi-site Phosphorylation of the Splicing Factor ASF/SF2 By SRPK1

Ma, Chen‐Ting; Velazquez-Dones, Adolfo; Hagopian, Jonathan C.; Ghosh, Gourisankar; Fu, Xiang‐Dong; Adams, Joseph A.

doi:10.1016/j.jmb.2007.08.029

Cited by 49 publications

(109 citation statements)

References 30 publications

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“…SRSF1 is required for 5 0 splice site selection, cleavage, and subsequent lariat formation and has been shown to recruit U1 snRNP to 5 0 splice sites and participate in the bridging of 5 0 and 3 0 splice sites [73][74][75]. Phosphorylation of SRSF1 by a specific SR protein kinase, SRPK1, enhances SRSF1 alternative splicing activity via promotion of the use of intron proximal sites while hindering intron distal site usage [76][77][78]. SRSF1 also mediates post-splicing activities including mRNA nuclear export, nonsense-mediated decay (NMD), and translation [71].…”

Section: P32 Sfsf1 and Alternative Splicingmentioning

confidence: 99%

Alteration of splice site selection in the LMNA gene and inhibition of progerin production via AMPK activation

Finley¹

2014

Medical Hypotheses

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Section: P32 Sfsf1 and Alternative Splicingmentioning

confidence: 99%

Alteration of splice site selection in the LMNA gene and inhibition of progerin production via AMPK activation

Finley¹

2014

Medical Hypotheses

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“…An RS dipeptide stretch at the C-terminus is the phosphorylation site of mammalian SRPKs and is the site where ASF/SF2 binds with other proteins [29,30]. In this study, we detected phosphorylation of purified truncated ASF/SF2 fusion proteins Trx-DSR and Trx-RS (Fig.…”

Section: Psrpk Can Phosphorylate the Sr Protein Asf/sf2mentioning

confidence: 66%

“…All SRPKs specifically act on the RS domain of the SR protein in an ordered, multisite phosphorylation manner [29,30]. Similar to human SRPK1 and SRPK2, mouse mSRPK1 and mSRPK2, yeast Dsk1p and Sky1p, PSRPK can also phosphorylate human SR protein ASF/SF2 [1 -7,13], demonstrating that ASF/SF2 is a common substrate of SRPKs.…”

Section: Discussionmentioning

confidence: 99%

A novel <italic>Physarum polycephalum</italic> SR protein kinase specifically phosphorylates the RS domain of the human SR protein, ASF/SF2

Liu¹,

Kang²,

Zhang³

et al. 2009

ABBS

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A 1591-bp cDNA of a serine-rich protein kinase (SRPK)-like protein has been identified in Physarum polycephalum (GenBank accession No. DQ140379). The cDNA contains two repeat sequences at bp 1 -153 and bp 395 -547. The encoding sequence is 56% homologous to human SRPK1 and is named Physarum SRPK (PSRPK). Consistent with other SRPKs, the consensus motifs of PSRPK are within the two conserved domains (CDs). However, divergent motifs between the N-terminal and CDs are much shorter than the corresponding sequences of other SRPKs. To study the structure and function of this protein, we performed co-expression experiment in Escherichia coli and in vitro phosphorylation assay to investigate the phosphorylation effect of recombinant PSRPK on the human SR protein, ASF/SF2. Western blot analysis showed that PSRPK could phosphorylate ASF/SF2 in E. coli cells. Autoradiographic examination showed that both recombinant PSRPK and a truncated form of PSRPK with a 28-aa deletion at the N-terminus could phosphorylate ASF/SF2 and a truncated form of ASF/SF2 that contains the RS domain. However, these two forms of PSRPK could not phosphorylate a truncated form ASF/SF2 that lacks the RS domain. A truncated form of PSRPK that lacks either of CDs does not have any phosphorylation activity. These results indicated that, like other SRPKs, the phosphorylation site in PSRPK is located within the RS domain of the SR protein and that its phosphorylation activity is closely associated with the two CDs. This study on the structure and function of PSRPK demonstrates that it is a new member of the SRPK family.

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“…The gene encoding SFRS protein kinase 1, a serine/arginine (SR) protein kinase specific for the SR-rich domain family of splicing factors was massively upregulated (33-fold) at D13 and moderately upregulated at the other time points (fourfold to eightfold). It is thought to play a role in the regulation of both constitutive and alternative splicing by regulating phosphorylation and intracellular localization of splicing factors (Ma et al 2008). The gene for eukaryotic translation elongation factor 1B2, which participates in the elongation cycle of protein biosynthesis, was only moderately affected.…”

Section: Discussionmentioning

confidence: 99%

Effect of Early Introduction of Microencapsulated Diet to Larval Atlantic Halibut, Hippoglossus hippoglossus L. Assessed by Microarray Analysis

et al. 2009

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Effect of early introduction of microencapsulated diet to larvalAbstract An experimental microdiet prepared using an internal gelation method was used to partially replace the traditional live feed (Artemia) for larval Atlantic halibut, Hippoglossus hippoglossus L. Three trials were conducted with microdiet introduced at 20, 32, and 43 days post first feeding and larvae were sampled at approximately 2, 13, 23, and 33 days after microdiet introduction in each trial. The success of feeding was assessed by morphometrics and histological analysis of gut contents. Microdiet particles were readily consumed after a period of adaptation and provided an adequate source of nutrients with no significant increase in mortality in the microdiet-fed group compared to the control group. However, growth was limited and there was an increased incidence of malpigmentation of the eye and skin. Subtle changes in underlying digestive and developmental physiology were revealed by microarray analysis of RNA from control and experimental fish given microdiet from day20 post first feeding. Fifty-eight genes were differentially expressed over the four sampling times in the course of the trial and the 28 genes with annotated functions fell into five major categories: metabolism and biosynthesis, cell division and proliferation, protein trafficking, cell structure, and stress. Interestingly, several of these genes were involved in pigmentation and eye development, in agreement with the phenotypic abnormalities seen in the larvae.

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Ordered Multi-site Phosphorylation of the Splicing Factor ASF/SF2 By SRPK1

Cited by 49 publications

References 30 publications

Alteration of splice site selection in the LMNA gene and inhibition of progerin production via AMPK activation

Alteration of splice site selection in the LMNA gene and inhibition of progerin production via AMPK activation

A novel <italic>Physarum polycephalum</italic> SR protein kinase specifically phosphorylates the RS domain of the human SR protein, ASF/SF2

Effect of Early Introduction of Microencapsulated Diet to Larval Atlantic Halibut, Hippoglossus hippoglossus L. Assessed by Microarray Analysis

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Ordered Multi-site Phosphorylation of the Splicing Factor ASF/SF2 By SRPK1

Cited by 49 publications

References 30 publications

Alteration of splice site selection in the LMNA gene and inhibition of progerin production via AMPK activation

Alteration of splice site selection in the LMNA gene and inhibition of progerin production via AMPK activation

A novel &lt;italic&gt;Physarum polycephalum&lt;/italic&gt; SR protein kinase specifically phosphorylates the RS domain of the human SR protein, ASF/SF2

Effect of Early Introduction of Microencapsulated Diet to Larval Atlantic Halibut, Hippoglossus hippoglossus L. Assessed by Microarray Analysis

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A novel <italic>Physarum polycephalum</italic> SR protein kinase specifically phosphorylates the RS domain of the human SR protein, ASF/SF2