Acinus - Explore the Science & Experts | ideXlab

Scan Science and Technology

Contact Leading Edge Experts & Companies

Acinus

The Experts below are selected from a list of 5472 Experts worldwide ranked by ideXlab platform

Acinus – Free Register to Access Experts & Abstracts

Dianne Robert Soprano – One of the best experts on this subject based on the ideXlab platform.

  • Role of Acinus in regulating retinoic acid-responsive gene pre-mRNA splicing.
    Journal of cellular physiology, 2014
    Co-Authors: Fang Wang, Kenneth J. Soprano, Dianne Robert Soprano

    Abstract:

    Acinus-S’ is a corepressor for retinoic acid receptor (RAR)-dependent gene transcription and has been suggested to be involved in RNA processing. In this study, the role of Acinus isoforms in regulating pre-mRNA splicing was explored using in vivo splicing assays. Both Acinus-L and Acinus-S’, with the activity of Acinus-L higher than that of Acinus-S’, increase the splicing of a retinoic acid (RA)-responsive minigene containing a weak 5′ splice site but not a RA-responsive minigene containing a strong 5′ splice site. RA treatment further enhances the splicing of the weak 5′ splice site by Acinus in a dose- and time-dependent manner, suggesting a RA-dependent activity in addition to a RA-independent activity of Acinus. The RA-independent effect of Acinus occurs to varying degrees using minigene constructs containing several different promoters, while the RA-dependent splicing activity of Acinus is specific for transcripts derived from the minigene driven by a RA response element (RARE)-containing promoter. This suggests that the ligand-dependent splicing activity of Acinus is related to the RA-activated RAR bound to the RARE. The RRM domain is necessary for the RA-dependent splicing activity of Acinus and the RA-independent splicing activity of Acinus is repressed by RNPS1. Importantly, measurement of the splicing of endogenous human RARβ and Bcl-x in vivo demonstrates that Acinus stimulates the use of the weaker alternative 5′ splice site of these two genes in a RA-dependent manner for RARβ and a RA-independent manner for Bcl-x. Taken together, these studies demonstrate that Acinus functions in both RAR-dependent splicing and RAR-dependent transcription. J. Cell. Physiol. 230: 791–801, 2015. © 2014 Wiley Periodicals, Inc.

  • the sap motif and c terminal rs and rd e rich region influences the sub nuclear localization of Acinus isoforms
    Journal of Cellular Biochemistry, 2014
    Co-Authors: Fang Wang, Karen S. Wendling, Kenneth J. Soprano, Dianne Robert Soprano

    Abstract:

    Acinus has been reported to function in apoptosis, RNA processing and regulation of gene transcription including RA-dependent transcription. There are three different isoforms of Acinus termed Acinus-L, Acinus-S′ and Acinus-S. The isoforms of Acinus differ in their N-terminus while the C-terminus is consistent in all isoforms. The sub-nuclear localization of Acinus-L and Acinus-S′ was determined using fluorescence microscopy. Acinus-S′ colocalizes with SC35 in nuclear speckles while Acinus-L localizes diffusely throughout the nucleoplasm. RA treatment has little effect on the sub-nuclear localization of Acinus-L and Acinus-S′. The domains/regions necessary for the distinct sub-nuclear localization of Acinus-L and Acinus-S′ were identified. The speckled sub-nuclear localization of Acinus-S′ is dependent on its C-terminal RS- and RD/E-rich region but is independent of the phosphorylation status of Ser-453 and Ser-604 within this region. The unique N-terminal SAP-motif of Acinus-L is responsible for its diffuse localization in the nucleus. Moreover, the sub-nuclear localization of Acinus isoforms is affected by each other, which is determined by the combinatorial effect of the more potent SAP motif of Acinus-L and the C-terminal RS- and RD/E-rich region in all Acinus isoforms. The C-terminal RS- and RD/E-rich region of Acinus mediates the colocalization of Acinus isoforms as well as with its interacting protein RNPS1. In conclusion, the SAP motif is responsible for the difference in the nuclear localization between Acinus-L and Acinus-S′. This difference in the nuclear localization of Acinus-S′ and Acinus-L may suggest that these two isoforms have different functional roles.

  • The SAP Motif and C‐Terminal RS‐ and RD/E‐Rich Region Influences the Sub‐Nuclear Localization of Acinus Isoforms
    Journal of cellular biochemistry, 2014
    Co-Authors: Fang Wang, Karen S. Wendling, Kenneth J. Soprano, Dianne Robert Soprano

    Abstract:

    Acinus has been reported to function in apoptosis, RNA processing and regulation of gene transcription including RA-dependent transcription. There are three different isoforms of Acinus termed Acinus-L, Acinus-S′ and Acinus-S. The isoforms of Acinus differ in their N-terminus while the C-terminus is consistent in all isoforms. The sub-nuclear localization of Acinus-L and Acinus-S′ was determined using fluorescence microscopy. Acinus-S′ colocalizes with SC35 in nuclear speckles while Acinus-L localizes diffusely throughout the nucleoplasm. RA treatment has little effect on the sub-nuclear localization of Acinus-L and Acinus-S′. The domains/regions necessary for the distinct sub-nuclear localization of Acinus-L and Acinus-S′ were identified. The speckled sub-nuclear localization of Acinus-S′ is dependent on its C-terminal RS- and RD/E-rich region but is independent of the phosphorylation status of Ser-453 and Ser-604 within this region. The unique N-terminal SAP-motif of Acinus-L is responsible for its diffuse localization in the nucleus. Moreover, the sub-nuclear localization of Acinus isoforms is affected by each other, which is determined by the combinatorial effect of the more potent SAP motif of Acinus-L and the C-terminal RS- and RD/E-rich region in all Acinus isoforms. The C-terminal RS- and RD/E-rich region of Acinus mediates the colocalization of Acinus isoforms as well as with its interacting protein RNPS1. In conclusion, the SAP motif is responsible for the difference in the nuclear localization between Acinus-L and Acinus-S′. This difference in the nuclear localization of Acinus-S′ and Acinus-L may suggest that these two isoforms have different functional roles.

Fang Wang – One of the best experts on this subject based on the ideXlab platform.

  • Role of Acinus in regulating retinoic acid-responsive gene pre-mRNA splicing.
    Journal of cellular physiology, 2014
    Co-Authors: Fang Wang, Kenneth J. Soprano, Dianne Robert Soprano

    Abstract:

    Acinus-S’ is a corepressor for retinoic acid receptor (RAR)-dependent gene transcription and has been suggested to be involved in RNA processing. In this study, the role of Acinus isoforms in regulating pre-mRNA splicing was explored using in vivo splicing assays. Both Acinus-L and Acinus-S’, with the activity of Acinus-L higher than that of Acinus-S’, increase the splicing of a retinoic acid (RA)-responsive minigene containing a weak 5′ splice site but not a RA-responsive minigene containing a strong 5′ splice site. RA treatment further enhances the splicing of the weak 5′ splice site by Acinus in a dose- and time-dependent manner, suggesting a RA-dependent activity in addition to a RA-independent activity of Acinus. The RA-independent effect of Acinus occurs to varying degrees using minigene constructs containing several different promoters, while the RA-dependent splicing activity of Acinus is specific for transcripts derived from the minigene driven by a RA response element (RARE)-containing promoter. This suggests that the ligand-dependent splicing activity of Acinus is related to the RA-activated RAR bound to the RARE. The RRM domain is necessary for the RA-dependent splicing activity of Acinus and the RA-independent splicing activity of Acinus is repressed by RNPS1. Importantly, measurement of the splicing of endogenous human RARβ and Bcl-x in vivo demonstrates that Acinus stimulates the use of the weaker alternative 5′ splice site of these two genes in a RA-dependent manner for RARβ and a RA-independent manner for Bcl-x. Taken together, these studies demonstrate that Acinus functions in both RAR-dependent splicing and RAR-dependent transcription. J. Cell. Physiol. 230: 791–801, 2015. © 2014 Wiley Periodicals, Inc.

  • the sap motif and c terminal rs and rd e rich region influences the sub nuclear localization of Acinus isoforms
    Journal of Cellular Biochemistry, 2014
    Co-Authors: Fang Wang, Karen S. Wendling, Kenneth J. Soprano, Dianne Robert Soprano

    Abstract:

    Acinus has been reported to function in apoptosis, RNA processing and regulation of gene transcription including RA-dependent transcription. There are three different isoforms of Acinus termed Acinus-L, Acinus-S′ and Acinus-S. The isoforms of Acinus differ in their N-terminus while the C-terminus is consistent in all isoforms. The sub-nuclear localization of Acinus-L and Acinus-S′ was determined using fluorescence microscopy. Acinus-S′ colocalizes with SC35 in nuclear speckles while Acinus-L localizes diffusely throughout the nucleoplasm. RA treatment has little effect on the sub-nuclear localization of Acinus-L and Acinus-S′. The domains/regions necessary for the distinct sub-nuclear localization of Acinus-L and Acinus-S′ were identified. The speckled sub-nuclear localization of Acinus-S′ is dependent on its C-terminal RS- and RD/E-rich region but is independent of the phosphorylation status of Ser-453 and Ser-604 within this region. The unique N-terminal SAP-motif of Acinus-L is responsible for its diffuse localization in the nucleus. Moreover, the sub-nuclear localization of Acinus isoforms is affected by each other, which is determined by the combinatorial effect of the more potent SAP motif of Acinus-L and the C-terminal RS- and RD/E-rich region in all Acinus isoforms. The C-terminal RS- and RD/E-rich region of Acinus mediates the colocalization of Acinus isoforms as well as with its interacting protein RNPS1. In conclusion, the SAP motif is responsible for the difference in the nuclear localization between Acinus-L and Acinus-S′. This difference in the nuclear localization of Acinus-S′ and Acinus-L may suggest that these two isoforms have different functional roles.

  • The SAP Motif and C‐Terminal RS‐ and RD/E‐Rich Region Influences the Sub‐Nuclear Localization of Acinus Isoforms
    Journal of cellular biochemistry, 2014
    Co-Authors: Fang Wang, Karen S. Wendling, Kenneth J. Soprano, Dianne Robert Soprano

    Abstract:

    Acinus has been reported to function in apoptosis, RNA processing and regulation of gene transcription including RA-dependent transcription. There are three different isoforms of Acinus termed Acinus-L, Acinus-S′ and Acinus-S. The isoforms of Acinus differ in their N-terminus while the C-terminus is consistent in all isoforms. The sub-nuclear localization of Acinus-L and Acinus-S′ was determined using fluorescence microscopy. Acinus-S′ colocalizes with SC35 in nuclear speckles while Acinus-L localizes diffusely throughout the nucleoplasm. RA treatment has little effect on the sub-nuclear localization of Acinus-L and Acinus-S′. The domains/regions necessary for the distinct sub-nuclear localization of Acinus-L and Acinus-S′ were identified. The speckled sub-nuclear localization of Acinus-S′ is dependent on its C-terminal RS- and RD/E-rich region but is independent of the phosphorylation status of Ser-453 and Ser-604 within this region. The unique N-terminal SAP-motif of Acinus-L is responsible for its diffuse localization in the nucleus. Moreover, the sub-nuclear localization of Acinus isoforms is affected by each other, which is determined by the combinatorial effect of the more potent SAP motif of Acinus-L and the C-terminal RS- and RD/E-rich region in all Acinus isoforms. The C-terminal RS- and RD/E-rich region of Acinus mediates the colocalization of Acinus isoforms as well as with its interacting protein RNPS1. In conclusion, the SAP motif is responsible for the difference in the nuclear localization between Acinus-L and Acinus-S′. This difference in the nuclear localization of Acinus-S′ and Acinus-L may suggest that these two isoforms have different functional roles.

Kenneth J. Soprano – One of the best experts on this subject based on the ideXlab platform.

  • Role of Acinus in regulating retinoic acid-responsive gene pre-mRNA splicing.
    Journal of cellular physiology, 2014
    Co-Authors: Fang Wang, Kenneth J. Soprano, Dianne Robert Soprano

    Abstract:

    Acinus-S’ is a corepressor for retinoic acid receptor (RAR)-dependent gene transcription and has been suggested to be involved in RNA processing. In this study, the role of Acinus isoforms in regulating pre-mRNA splicing was explored using in vivo splicing assays. Both Acinus-L and Acinus-S’, with the activity of Acinus-L higher than that of Acinus-S’, increase the splicing of a retinoic acid (RA)-responsive minigene containing a weak 5′ splice site but not a RA-responsive minigene containing a strong 5′ splice site. RA treatment further enhances the splicing of the weak 5′ splice site by Acinus in a dose- and time-dependent manner, suggesting a RA-dependent activity in addition to a RA-independent activity of Acinus. The RA-independent effect of Acinus occurs to varying degrees using minigene constructs containing several different promoters, while the RA-dependent splicing activity of Acinus is specific for transcripts derived from the minigene driven by a RA response element (RARE)-containing promoter. This suggests that the ligand-dependent splicing activity of Acinus is related to the RA-activated RAR bound to the RARE. The RRM domain is necessary for the RA-dependent splicing activity of Acinus and the RA-independent splicing activity of Acinus is repressed by RNPS1. Importantly, measurement of the splicing of endogenous human RARβ and Bcl-x in vivo demonstrates that Acinus stimulates the use of the weaker alternative 5′ splice site of these two genes in a RA-dependent manner for RARβ and a RA-independent manner for Bcl-x. Taken together, these studies demonstrate that Acinus functions in both RAR-dependent splicing and RAR-dependent transcription. J. Cell. Physiol. 230: 791–801, 2015. © 2014 Wiley Periodicals, Inc.

  • the sap motif and c terminal rs and rd e rich region influences the sub nuclear localization of Acinus isoforms
    Journal of Cellular Biochemistry, 2014
    Co-Authors: Fang Wang, Karen S. Wendling, Kenneth J. Soprano, Dianne Robert Soprano

    Abstract:

    Acinus has been reported to function in apoptosis, RNA processing and regulation of gene transcription including RA-dependent transcription. There are three different isoforms of Acinus termed Acinus-L, Acinus-S′ and Acinus-S. The isoforms of Acinus differ in their N-terminus while the C-terminus is consistent in all isoforms. The sub-nuclear localization of Acinus-L and Acinus-S′ was determined using fluorescence microscopy. Acinus-S′ colocalizes with SC35 in nuclear speckles while Acinus-L localizes diffusely throughout the nucleoplasm. RA treatment has little effect on the sub-nuclear localization of Acinus-L and Acinus-S′. The domains/regions necessary for the distinct sub-nuclear localization of Acinus-L and Acinus-S′ were identified. The speckled sub-nuclear localization of Acinus-S′ is dependent on its C-terminal RS- and RD/E-rich region but is independent of the phosphorylation status of Ser-453 and Ser-604 within this region. The unique N-terminal SAP-motif of Acinus-L is responsible for its diffuse localization in the nucleus. Moreover, the sub-nuclear localization of Acinus isoforms is affected by each other, which is determined by the combinatorial effect of the more potent SAP motif of Acinus-L and the C-terminal RS- and RD/E-rich region in all Acinus isoforms. The C-terminal RS- and RD/E-rich region of Acinus mediates the colocalization of Acinus isoforms as well as with its interacting protein RNPS1. In conclusion, the SAP motif is responsible for the difference in the nuclear localization between Acinus-L and Acinus-S′. This difference in the nuclear localization of Acinus-S′ and Acinus-L may suggest that these two isoforms have different functional roles.

  • The SAP Motif and C‐Terminal RS‐ and RD/E‐Rich Region Influences the Sub‐Nuclear Localization of Acinus Isoforms
    Journal of cellular biochemistry, 2014
    Co-Authors: Fang Wang, Karen S. Wendling, Kenneth J. Soprano, Dianne Robert Soprano

    Abstract:

    Acinus has been reported to function in apoptosis, RNA processing and regulation of gene transcription including RA-dependent transcription. There are three different isoforms of Acinus termed Acinus-L, Acinus-S′ and Acinus-S. The isoforms of Acinus differ in their N-terminus while the C-terminus is consistent in all isoforms. The sub-nuclear localization of Acinus-L and Acinus-S′ was determined using fluorescence microscopy. Acinus-S′ colocalizes with SC35 in nuclear speckles while Acinus-L localizes diffusely throughout the nucleoplasm. RA treatment has little effect on the sub-nuclear localization of Acinus-L and Acinus-S′. The domains/regions necessary for the distinct sub-nuclear localization of Acinus-L and Acinus-S′ were identified. The speckled sub-nuclear localization of Acinus-S′ is dependent on its C-terminal RS- and RD/E-rich region but is independent of the phosphorylation status of Ser-453 and Ser-604 within this region. The unique N-terminal SAP-motif of Acinus-L is responsible for its diffuse localization in the nucleus. Moreover, the sub-nuclear localization of Acinus isoforms is affected by each other, which is determined by the combinatorial effect of the more potent SAP motif of Acinus-L and the C-terminal RS- and RD/E-rich region in all Acinus isoforms. The C-terminal RS- and RD/E-rich region of Acinus mediates the colocalization of Acinus isoforms as well as with its interacting protein RNPS1. In conclusion, the SAP motif is responsible for the difference in the nuclear localization between Acinus-L and Acinus-S′. This difference in the nuclear localization of Acinus-S′ and Acinus-L may suggest that these two isoforms have different functional roles.