RBM42

Last update 08 May 2025

Basic Info

Synonyms

MGC10433, RBM42, RNA binding motif protein 42

+ [2]

Introduction

Binds (via the RRM domain) to the 3'-untranslated region (UTR) of CDKN1A mRNA.

100 Clinical Results associated with RBM42

100 Translational Medicine associated with RBM42

0 Patents (Medical) associated with RBM42

Literatures (Medical) associated with RBM42

01 Mar 2025·Nature Cell Biology

Functional screen identifies RBM42 as a mediator of oncogenic mRNA translation specificity

Article

Author: Subramanyam, Vishvak ; Miglani, Sohit ; Slota, Macey ; Oses-Prieto, Juan A ; Yiakis, Kaylee ; Kim, Grace E ; Ruggero, Davide ; Goodarzi, Hani ; Hernandez, Grace ; Wen, Kwun Wah ; Perera, Rushika M ; Liu, Isabelle ; Rademaker, Gilles ; Kovalski, Joanna R ; Sarioglu, Goksu ; Mohan, Nimmy ; Burlingame, Alma L

Oncogenic protein dosage is tightly regulated to enable cancer formation but how this is regulated by translational control remains unknown. The Myc oncogene is a paradigm of an exquisitely regulated oncogene and a driver of pancreatic ductal adenocarcinoma (PDAC). Here we use a CRISPR interference screen in PDAC cells to identify activators of selective MYC translation. The top hit, the RNA-binding protein RBM42, is highly expressed in PDAC and predicts poor survival. We show that RBM42 binds and selectively regulates the translation of MYC and a precise suite of pro-oncogenic transcripts, including JUN and EGFR. Mechanistically, we find that RBM42 binds and remodels the MYC 5' untranslated region structure, facilitating the formation of the translation pre-initiation complex. Importantly, RBM42 is necessary for PDAC tumorigenesis in a Myc-dependent manner in vivo. This work transforms the understanding of the translational code in cancer and illuminates therapeutic openings to target the expression of oncogenes.

03 Jan 2024·Protein & Cell

Biallelic variants in RBM42 cause a multisystem disorder with neurological, facial, cardiac, and musculoskeletal involvement

Article

Author: Shi, Weihui ; Yang, Zhenhua ; Wang, Li ; Wang, Jian ; Huang, He-Feng ; Pan, Nina ; Chen, Yiyao ; Wang, Yanlin ; Tan, Yajing ; Zhang, Xiaoyu Merlin ; Yang, Bingxin ; Wang, Minhui ; Li, Jinsong ; Hu, Liya ; Xing, Qinghe ; Zhang, Jinglan ; Ma, Zhonghua ; Chen, Songchang ; Xu, Chenming ; Li, Shuyuan

AbstractHere, we report a previously unrecognized syndromic neurodevelopmental disorder associated with biallelic loss-of-function variants in the RBM42 gene. The patient is a 2-year-old female with severe central nervous system (CNS) abnormalities, hypotonia, hearing loss, congenital heart defects, and dysmorphic facial features. Familial whole-exome sequencing (WES) reveals that the patient has two compound heterozygous variants, c.304C>T (p.R102*) and c.1312G>A (p.A438T), in the RBM42 gene which encodes an integral component of splicing complex in the RNA-binding motif protein family. The p.A438T variant is in the RRM domain which impairs RBM42 protein stability in vivo. Additionally, p.A438T disrupts the interaction of RBM42 with hnRNP K, which is the causative gene for Au-Kline syndrome with overlapping disease characteristics seen in the index patient. The human R102* or A438T mutant protein failed to fully rescue the growth defects of RBM42 ortholog knockout ΔFgRbp1 in Fusarium while it was rescued by the wild-type (WT) human RBM42. A mouse model carrying Rbm42 compound heterozygous variants, c.280C>T (p.Q94*) and c.1306_1308delinsACA (p.A436T), demonstrated gross fetal developmental defects and most of the double mutant animals died by E13.5. RNA-seq data confirmed that Rbm42 was involved in neurological and myocardial functions with an essential role in alternative splicing (AS). Overall, we present clinical, genetic, and functional data to demonstrate that defects in RBM42 constitute the underlying etiology of a new neurodevelopmental disease which links the dysregulation of global AS to abnormal embryonic development.

23 May 2023·Journal of ovarian research

Extracellular vesicle-microRNAs mediated response of bovine ovaries to seasonal environmental changes.

Article

Author: Rojas, Camila Santos ; Gad, Ahmed ; Gonella-Diaza, Angela ; Heredia, Daniella ; Tesfaye, Dawit ; Joyce, Kamryn ; Menjivar, Nico Graham

BACKGROUNDAmong the various seasonal environmental changes, elevated ambient temperature during the summer season is a main cause of stress in dairy and beef cows, leading to impaired reproductive function and fertility. Follicular fluid extracellular vesicles (FF-EVs) play an important role in intrafollicular cellular communication by, in part, mediating the deleterious effects of heat stress (HS). Here we aimed to investigate the changes in FF-EV miRNA cargoes in beef cows in response to seasonal changes: summer (SUM) compared to the winter (WIN) season using high throughput sequencing of FF-EV-coupled miRNAs. In addition to their biological relevance, the potential mechanisms involved in the packaging and release of those miRNAs as a response to environmental HS were elucidated.RESULTSSequencing analysis revealed that an average of 6.6% of the EV-RNA mapped reads were annotated to bovine miRNAs. Interestingly, miR-148a, miR-99a-5p, miR-10b, and miR-143 were the top four miRNAs in both groups accounting for approximately 52 and 62% of the total miRNA sequence reads in the SUM and WIN groups, respectively. A group of 16 miRNAs was up-regulated and 8 miRNAs were down-regulated in the SUM compared to the WIN group. Five DE-miRNAs (miR-10a, miR-10b, miR-26a, let-7f, and miR-1246) were among the top 20 expressed miRNA lists. Sequence motif analysis revealed the appearance of two specific motifs in 13 out of the 16 upregulated miRNAs under HS conditions. Both motifs were found to be potentially bonded by specific RNA binding proteins including Y-box binding proteins (YBX1 and YBX2) and RBM42.CONCLUSIONOur findings indicate that FF EV-coupled miRNA profile varies under seasonal changes. These miRNAs could be a good indicator of the cellular mechanism in mediating HS response and the potential interplay between miRNA motifs and RNA binding proteins can be one of the mechanisms governing the packaging and release of miRNAs via EVs to facilitate cellular survival.

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RBM42

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