Dephosphorylated NSSR1 Is Induced by Androgen in Mouse Epididymis and Phosphorylated NSSR1 Is Increased during Sperm Maturation

Xiao, Peipei; Peng, Zheng Yu; Huang, Lu; Li, Ya; Chen, Xian Hua

doi:10.1371/journal.pone.0025667

Cited by 5 publications

(6 citation statements)

References 37 publications

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“…This cytosolic localization persists in testicular cancer, and is also seen in liver, endometrial and urothelial cancers (Uhlen et al 2015). Dephosphorylation of SRSF10 is induced by androgen in mouse epididymis and phosphorylated SRSF10 expression is increased during sperm maturation (Xiao et al 2011). 9.…”

Section: Heart Developmentmentioning

confidence: 97%

SRSF10: an atypical splicing regulator with critical roles in stress response, organ development, and viral replication

Shkreta

Aurélie

Salvetti

et al. 2021

RNA

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Serine/Arginine Splicing Factor 10 (SRSF10) is a member of the family of mammalian splicing regulators known as SR proteins. Like several of its SR siblings, the SRSF10 protein is composed of an RNA binding domain (RRM) and of arginine and serine-rich auxiliary domains (RS) that guide interactions with other proteins. The phosphorylation status of SRSF10 is of paramount importance for its activity and is subjected to changes during mitosis, heat-shock and DNA damage. SRSF10 overexpression has functional consequences in a growing list of cancers. By controlling the alternative splicing of specific transcripts, SRSF10 has also been implicated in glucose, fat and cholesterol metabolism, in the development of the embryonic heart and in neurological processes. SRSF10 is also important for the proper expression and processing of HIV-1 and other viral transcripts. We discuss how SRSF10 could become a potentially appealing therapeutic target to combat cancer and viral infections.

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Section: Heart Developmentmentioning

confidence: 97%

SRSF10: an atypical splicing regulator with critical roles in stress response, organ development, and viral replication

Shkreta

Aurélie

Salvetti

et al. 2021

RNA

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“…At 1 or 12 hr after vector injection or 4-6 hr after nocodazole injection (16-18 hr after viral injection), animals received an overdose of pentobarbital (100 mg/kg intraperitoneally) and were perfused transcardially with ice-cold 100 mM sodium PBS (pH 7.4), followed by 4% PFA in phosphate buffer (PB) (pH 7.4). After tissues were postfixed for 24 hr at 4°C in PFA, 34 10-20 lm coronal sections were cut using a cyrosection microtome and then the slides were directly sealed with mounting medium (Prolong Antifade Gold with DAPI [4¢,6¢-diamidino-2-phenylindole]; Molecular Probes).…”

Section: Animal Studiesmentioning

confidence: 99%

Disruption of Microtubules Post-Virus Entry Enhances Adeno-Associated Virus Vector Transduction

Xiao

Mitchell

et al. 2016

Human Gene Therapy

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Perinuclear retention of viral particles is a poorly understood phenomenon observed during many virus infections. In this study, we investigated whether perinuclear accumulation acts as a barrier to limit recombinant adeno-associated virus (rAAV) transduction. After nocodazole treatment to disrupt microtubules at microtubule-organization center (MT-MTOC) after virus entry, we observed higher rAAV transduction. To elucidate the role of MT-MTOC in rAAV infection and study its underlying mechanisms, we demonstrated that rAAV's perinuclear localization was retained by MT-MTOC with fluorescent analysis, and enhanced rAAV transduction from MT-MTOC disruption was dependent on the rAAV capsid's nuclear import signals. Interestingly, after knocking down RhoA or inhibiting its downstream effectors (ROCK and Actin), MT-MTOC disruption failed to increase rAAV transduction or nuclear entry. These data suggest that enhancement of rAAV transduction is the result of increased trafficking to the nucleus via the RhoA-ROCK-Actin pathway. Ten-fold higher rAAV transduction was also observed by disrupting MT-MTOC in brain, liver, and tumor in vivo. In summary, this study indicates that virus perinuclear accumulation at MT-MTOC is a barrier-limiting parameter for effective rAAV transduction and defines a novel defense mechanism by which host cells restrain viral invasion.

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“…Heat shockinduced NSSR1 dephosphorylation was found to display splicing thermotolerance mediated by the Hsp27 protein (Shi et al, 2011). Recently, we found that NSSR1 is expressed in mouse reproductive tissues such as the uterus and epididymis and, more interestingly, that the level of de-phosphorylated NSSR1 proteins in the mouse caput is upregulated during the first 3 weeks after birth, and was induced by androgen in the mouse epididymis Xiao et al, 2011), indicating the potential roles that dephosphorylated NSSR1 protein might play during development of the epididymis and sperm maturation. It therefore appears that dephosphorylated NSSR1 proteins are involved in multiple aspects of physiological functions in different tissues and cells, including splicing, and that more functions need to be assigned to dephosphorylated NSSR1.…”

Section: Introductionmentioning

confidence: 96%

Dephosphorylation of NSSR1 regulates alternative splicing of the GluR-B minigene

Zhang

Chen

et al. 2014

Genet. Mol. Res.

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ABSTRACT. Neural salient serine/arginine-rich protein 1 (NSSR1, alternatively SRp38) is an important splicing factor that can repress pre-mRNA alternative splicing in cells during heat shock and mitosis. We show here that NSSR1 protein is dephosphorylated when cells are heat shocked or incubated with kinase inhibitor K252a. Both heat shock and K252a treatment increase the truncated splicing isoform of the GluR-B minigene pre-mRNA. We also investigated the roles of the RRM motif and three RS domains of NSSR1 in in vivo pre-mRNA splicing. The results show that deletion of the RRM motif did not affect GluR-B minigene pre-mRNA splicing, but deletion of any one of the three RS domains increases the truncated splicing isoform of the GluR-B minigene. We further show that an SRSRSK sequence in the RS3 domain may play an important role in the function of NSSR1 in pre-mRNA splicing.

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Dephosphorylated NSSR1 Is Induced by Androgen in Mouse Epididymis and Phosphorylated NSSR1 Is Increased during Sperm Maturation

Cited by 5 publications

References 37 publications

SRSF10: an atypical splicing regulator with critical roles in stress response, organ development, and viral replication

SRSF10: an atypical splicing regulator with critical roles in stress response, organ development, and viral replication

Disruption of Microtubules Post-Virus Entry Enhances Adeno-Associated Virus Vector Transduction

Dephosphorylation of NSSR1 regulates alternative splicing of the GluR-B minigene

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