SRRM2

Last update 08 May 2025

Basic Info

Synonyms

300 kDa nuclear matrix antigen, Cwc21, KIAA0324

+ [11]

Introduction

Required for pre-mRNA splicing as component of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable).

100 Clinical Results associated with SRRM2

100 Translational Medicine associated with SRRM2

0 Patents (Medical) associated with SRRM2

Literatures (Medical) associated with SRRM2

01 Jul 2025·Cytokine

LINC00426 promotes the progression of atherosclerosis by regulating miR-873-5p/SRRM2 axis

Article

Author: Gan, Lu ; Zhou, Bo ; Tang, Fang ; Jin, Peng ; Zhou, Pimo ; Jin, Ping ; Yang, Tai ; Chen, Jiulin

BACKGROUNDAtherosclerosis (AS) is a disease that occurs in the great arteries and is the main cause of cardiovascular disease and death.OBJECTIVETo investigate the clinical significance of LINC00426 in AS and to investigate that LINC00426 regulates PDGF-BB-induced proliferation, migration, invasion and inflammatory response of vascular smooth muscle cells (VSMCs) by modulating miR-873-5p/SRRM2 axis.METHODSThe expression of LINC00426 was detected using RT-qPCR. The diagnostic role of LINC00426 in AS was analyzed with ROC curves. CCK-8 assay was used to measure cell proliferation, and transwell assay was used to measure cell migration and invasion ability. The targeted binding relationship between LINC00426 and miR-873-5p, miR-873-5p and SRRM2 was detected using dual-luciferase reporter gene assay. The concentration of proinflammatory factors was detected by using ELISA kit.RESULTThe expression of LINC00426 was increased in patients with AS, and LINC00426 had a diagnostic role in AS. In addition, LINC00426 regulated PDGF-BB-induced proliferation, migration, invasion, and inflammation of VSMCs by regulating miR-873-5p/SRRM2 axis.CONCLUSIONLINC00426 may function as a biomarker for the diagnosis and treatment of AS.

01 Apr 2025·Molecular Cell

Phosphorylation-dependent charge blocks regulate the relaxation of nuclear speckle networks

Article

Author: Liang, Yuhang ; Zhang, Mengjun ; Fang, Ning ; Chen, Junlin ; Ge, Yifan ; Shu, Li ; Sun, Yingtian ; Qu, Qingming ; Zhong, Chuan-Qi ; Huang, Shaohui ; Dong, Yichen ; Ma, Suibin ; Chen, Zhongwen ; Zhang, Xin ; Wang, Bo ; Gu, Zhuang ; Guo, Jierui

Nuclear speckles (NSs) are viscoelastic network fluids formed via phase separation coupled to percolation (PSCP). Intermolecular crosslinks of SRRM2 lead to the emergence of system-spanning networks, although the physicochemical grammar governing SRRM2 PSCP remains poorly decoded. Here, we demonstrate that SRRM2 is extensively phosphorylated within the intrinsically disordered region (IDR), creating alternating charge blocks. We show that this specific charge pattern does not markedly alter the condensation threshold of SRRM2 in cells. Instead, SRRM2 charge blocks intensify intra-network molecular interactions to modulate the material properties of mesoscopic SRRM2 condensates. We further identify casein kinase 2 (CK2) as the upstream enzyme to catalyze SRRM2 phosphorylation. Phosphorylation of SRRM2 IDR by CK2 facilitates NS relaxation, which is associated with enhanced efficiency of mRNA splicing to safeguard genome stability during DNA damage. Our findings reveal important regulatory mechanisms of charge blocks in modulating the material properties and functions of biomolecular condensates in human cells.

01 Jan 2025·Advances in Protein Chemistry and Structural Biology

Nuclear Tau accumulation in Alzheimer’s disease

Review

Author: Suresh, Swathi ; Chinnathambi, Subashchandrabose ; Velmurugan, Gowshika ; Chandrashekar, Madhura ; Adithyan, Anusree

Tau is a well-known microtubule-associated protein and is located in the cytoplasm of neurons, which play a crucial role in Alzheimer's diseases. Due to its preferred binding to DNA sequences found in the nucleolus and pericentromeric heterochromatin, Tau has been found within the cell nucleus, where it may be a nucleic acid-associated protein. Tau has the ability to directly interact with nuclear pore complex nucleoporins, influencing both their structural and functional integrity. The interaction between Tau and NUPs highlights a potential mechanism underlying NPC dysfunction in AD pathogenesis. Pathological Tau hinders the import and export of nucleus through RAN mediated cascades. Nuclear Tau aggregates colocalize with membrane less organelles called nuclear speckles, which are involved in pre-mRNA splicing, and modify their dynamics, composition, and structure. Additionally, SRRM2 and other nuclear speckle proteins including MSUT2 and PABPN1 mislocalize to cytosolic Tau aggregates, and causes propagation of Tau aggregates. Research highlights, Extracellular Tau Oligomers induce significant nuclear invagination. They act as a key player in the transformation of healthy neurons into sick neurons in AD. The mechanism behind this phenomenon depends on intracellular Tau and is linked to changes in chromatin structure, nucleocytoplasmic transport, and gene transcription. This review highlights the vital roles of nuclear Tau protein in the context of nuclear pore complex functioning and, modulation of nuclear speckles in Alzheimer's diseases. Addressing these pathways is essential for formulating focused therapeutics intended to alleviate Tau-induced neurodegeneration.

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SRRM2

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