RRBP1

Last update 23 Jan 2025

Basic Info

Synonyms

180 kDa ribosome receptor homolog, ES/130, ES/130-related protein

+ [8]

Introduction

Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane.

100 Clinical Results associated with RRBP1

100 Translational Medicine associated with RRBP1

0 Patents (Medical) associated with RRBP1

190

Literatures (Medical) associated with RRBP1

01 Mar 2025·Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids

Single-cell transcriptomic analysis and luteolin treatment reveal three adipogenic genes, including Aspn, Htra1 and Efemp1

Article

Author: Tao, Tao ; Xu, Yanting ; Zhang, Cheng-Hui ; Liu, Jian ; Zhang, Xian ; Chen, Juan

A comparative transcriptomic analysis in adipose stem and progenitor cells (ASPCs) between obese and lean mice might facilitate the identification of novel adipogenic genes. Here, we compare transcriptomic differences in the ASPCs of subcutaneous adipose tissue (SAT) between the mice fed on a high-fat-diet (HFD) and the chow diet (CD)-fed mice by analyzing three independent single-cell RNA sequencing datasets. Six differential genes, including three up-regulated genes Aspn, Rrbp1, Fbln2 and three down-regulated genes Htra1, Plpp3, Efemp1, are identified and confirmed in HFD-fed mice. Further, the expression of these genes is found to be significantly diminished in the differentiated 3T3-L1 cells. Treatment with luteolin, a dietary flavonoid known to inhibit 3T3-L1 adipogenesis, reverses the decreased expression of Aspn, Htra1 and Efemp1. Furthermore, knockdown of Aspn, Htra1 and Efemp1 significantly facilitates 3T3-L1 adipogenesis. Together, these genes not only are differential in ASPCs between obese and lean mice, but also are the adipogenic inhibitory genes that can be up-regulated by luteolin treatment.

01 Dec 2024·Neurobiology of Disease

Deciphering the alteration of MAP2 interactome caused by a schizophrenia-associated phosphorylation

Article

Author: Grubisha, Melanie J ; Grubisha, M.J. ; Lyu, J. ; Chou, Shinnyi ; Gilardi, Jordan ; Chou, S. ; Sweet, Robert A ; Buchwald, Serena C ; Buchwald, S.C. ; Lyu, Jiali ; Ruiz, Shelby ; MacDonald, Matthew L ; Ruiz, S. ; MacDonald, M.L. ; Gilardi, J. ; Sweet, R.A.

Microtubule-associated protein 2 (MAP2) is a crucial regulator of dendritic structure and neuronal function, orchestrating diverse protein interactions within the microtubule network. We have shown MAP2 is hyperphosphorylated at serine 1782 (S1782) in schizophrenia and phosphomimetic mutation of S1782 in mice (MAP2^S1782E) is sufficient to impair dendritic architecture. We sought to determine how this hyperphosphorylation affects the MAP2 interactome to provide insights into the disorder's mechanisms. We investigated the MAP2 interactome using co-immunoprecipitation and mass spectrometry in MAP2^S1782E and MAP2^WT mice. We found that S1782E MAP2 led to a substantial disruption of protein-protein interactions relative to WT MAP2. Reduced interactions with PDZ domain-containing proteins, calmodulin-binding proteins, ribosome proteins, and kinesin proteins may all contribute to dendritic impairments induced by S1782E, and may be linked to schizophrenia pathogenesis. Interestingly, novel gain-of-function interactions with PPM1L and KLHL8 nominated these as regulators of phosphoS1782 MAP2 abundance and potential therapeutic targets in schizophrenia.

01 Dec 2024·Cellular and Molecular Life Sciences

Stabilization of RRBP1 mRNA via an m6A-dependent manner in prostate cancer constitutes a therapeutic vulnerability amenable to small-peptide inhibition of METTL3

Article

Author: Tian, Yu ; Li, Zenghui ; Liu, Lu ; Xu, Hao ; Zhang, Dingxiao ; Feng, Yuqing ; Xu, Bin ; Xiong, Jiangling ; Shi, Junfeng ; Zou, Cheng ; He, Qinju ; Li, Wenjun ; Zhu, Jinwei

Mounting evidence has implicated the RNA m⁶A methylation catalyzed by METTL3 in a wide range of physiological and pathological processes, including tumorigenesis. The detailed m⁶A landscape and molecular mechanism of METTL3 in prostate cancer (PCa) remains ill-defined. We find that METTL3 is overexpressed in PCa and correlates with worse patient survival. Functional studies establish METTL3 as an oncoprotein dependent on its m⁶A enzymatic activity in both AR⁺ and AR^- PCa cells. To dissect the regulatory network of m⁶A pathway in PCa, we map the m⁶A landscape in clinical tumor samples using m⁶A-seq and identify genome-wide METTL3-binding transcripts via RIP-seq. Mechanistically, we discover RRBP1 as a direct METTL3 target in which METTL3 stabilizes RRBP1 mRNA in an m⁶A-dependent manner. RRBP1 positively correlates with METTL3 expression in PCa cohorts and exerts an oncogenic role in aggressive PCa cells. Leveraging the 3D structural protein-protein interaction between METTL3 and METTL14, we successfully develop two potential METTL3 peptide inhibitors (RM3 and RSM3) that effectively suppress cancer cell proliferation in vitro and tumor growth in vivo. Collectively, our study reveals a novel METTL3/m⁶A/RRBP1 axis in enhancing aggressive traits of PCa, which can be therapeutically targeted by small-peptide METTL3 antagonists.

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RRBP1

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