SAP30BP

Last update 23 Jan 2025

Basic Info

Synonyms

HCNGP, HTRG, HTRP

+ [4]

Introduction

Plays a role in transcriptional repression by promoting histone deacetylase activity, leading to deacetylation of histone H3 (PubMed:21221920). May be involved in the regulation of beta-2-microglobulin genes (By similarity). (Microbial infection) Involved in transcriptional repression of HHV-1 genes TK and gC.

100 Clinical Results associated with SAP30BP

100 Translational Medicine associated with SAP30BP

0 Patents (Medical) associated with SAP30BP

Literatures (Medical) associated with SAP30BP

01 Dec 2024·Biochemical and Biophysical Research Communications

BioID proximity mapping reveals novel SAP18 interactions in the prespliceosomal complex

Article

Author: Adhikary, Ankita ; Kumari, Sweta ; Singh, Kusum Kumari

SAP18 protein was originally discovered in association with the SIN3 transcriptional repressor complex. Subsequent biochemical fractionation studies identified SAP18 as a component of another distinct trimeric complex termed as the apoptosis- and splicing-associated protein (ASAP) complex. The existence of SAP18 in distinct complexes highlights its dual role in transcriptional and splicing regulation. In our study, we aim to define the in vivo interactome of SAP18 using proximity-dependent biotin identification (BioID). Mass spectrometry analysis of streptavidin-purified biotinylated proteins revealed new SIN3-associated interactors, including RBBP4 and SAP30BP. Notably, we identified 72 spliceosomal proteins as highly enriched interactors. Additionally, a complementary immunoprecipitation assay validated novel interactions of SAP18 with the prespliceosomal components SNRNP70, SNRPA, SF3B1, U2AF1, and the SR protein SRSF1. Mutational analysis using a C-terminal SAP18 double point mutant, which is known to be deficient in ASAP-interaction, demonstrated a debilitated interaction with the prespliceosomal proteins. Altogether, our results present a refined understanding of the SAP18 interactome, uncovering its association with the prespliceosome in conjugation with ASAP components.

11 Dec 2023·The EMBO Journal

CDK11 requires a critical activator SAP30BP to regulate pre‐mRNA splicing

Article

Author: Zhou, Yu ; Cheng, Hong ; Yun, Hao ; Liu, Hui ; Xu, Lin ; Fan, Jing ; Wang, Changshou ; Wang, Keyun ; Ye, Mingliang ; Du, Chen

AbstractCDK11 is an emerging druggable target for cancer therapy due to its prevalent roles in phosphorylating critical transcription and splicing factors and in facilitating cell cycle progression in cancer cells. Like other cyclin‐dependent kinases, CDK11 requires its cognate cyclin, cyclin L1 or cyclin L2, for activation. However, little is known about how CDK11 activities might be modulated by other regulators. In this study, we show that CDK11 forms a tight complex with cyclins L1/L2 and SAP30BP, the latter of which is a poorly characterized factor. Acute degradation of SAP30BP mirrors that of CDK11 in causing widespread and strong defects in pre‐mRNA splicing. Furthermore, we demonstrate that SAP30BP facilitates CDK11 kinase activities in vitro and in vivo, through ensuring the stabilities and the assembly of cyclins L1/L2 with CDK11. Together, these findings uncover SAP30BP as a critical CDK11 activator that regulates global pre‐mRNA splicing.

01 Dec 2023·Cell Reports

SAP30BP interacts with RBM17/SPF45 to promote splicing in a subset of human short introns

Article

Author: Fukumura, Kazuhiro ; Mayeda, Akila ; Sattler, Michael ; Seuß, Stefanie ; Kang, Hyun-Seo ; Yoshimoto, Rei ; Sperotto, Luca

Human pre-mRNA splicing requires the removal of introns with highly variable lengths, from tens to over a million nucleotides. Therefore, mechanisms of intron recognition and splicing are likely not universal. Recently, we reported that splicing in a subset of human short introns with truncated polypyrimidine tracts depends on RBM17 (SPF45), instead of the canonical splicing factor U2 auxiliary factor (U2AF) heterodimer. Here, we demonstrate that SAP30BP, a factor previously implicated in transcriptional control, is an essential splicing cofactor for RBM17. In vitro binding and nuclear magnetic resonance analyses demonstrate that a U2AF-homology motif (UHM) in RBM17 binds directly to a newly identified UHM-ligand motif in SAP30BP. We show that this RBM17-SAP30BP interaction is required to specifically recruit RBM17 to phosphorylated SF3B1 (SF3b155), a U2 small nuclear ribonucleoprotein (U2 snRNP) component in active spliceosomes. We propose a mechanism for splicing in a subset of short introns, in which SAP30BP guides RBM17 in the assembly of active spliceosomes.

Analysis

Perform a panoramic analysis of this field.

view full example data

Chat with Hiro

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

SAP30BP

Basic Info

Related

Analysis