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Last update 08 May 2025

SERF2

Last update 08 May 2025

Basic Info

Synonyms

4F5REL, FAM2C, Gastric cancer-related protein VRG107

+ [5]

Introduction

Positive regulator of amyloid protein aggregation and proteotoxicity (PubMed:20723760). Induces conformational changes in amyloid proteins, such as HTT, driving them into compact formations preceding the formation of aggregates (PubMed:20723760).

Drugs associated with SERF2

CN118108828

Patent Mining

Target

SERF2

Mechanism-

Active Org.

Shanghai Zhongqi Biotechnology Co., Ltd.

Originator Org.

Shanghai Zhongqi Biotechnology Co., Ltd.

Active Indication

Nervous System Diseases

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with SERF2

100 Translational Medicine associated with SERF2

0 Patents (Medical) associated with SERF2

Literatures (Medical) associated with SERF2

01 Jun 2024·Biomolecular NMR Assignments

Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2

Article

Author: Sahoo, Bikash R ; Bardwell, James C A ; Subramanian, Vivekanandan

Human small EDRK-rich factor protein SERF2 is a cellular driver of protein amyloid formation, a process that has been linked to neurodegenerative diseases including Alzheimer's and Parkinson's disease. SERF2 is a 59 amino acid protein, highly charged, and well conserved whose structure and physiological function is unclear. SERF family proteins including human SERF2 have shown a tendency to form fuzzy complexes with misfolded proteins such as α-Synuclein which has been linked to Parkinson's disease. SERF family proteins have been recently identified to bind nucleic acids, but the binding mechanism(s) remain enigmatic. Here, using multidimensional solution NMR, we report the ¹H, ¹⁵N, and ¹³C chemical shift assignments (~ 86% of backbone resonance assignments) for human SERF2. TALOS-N predicted secondary structure of SERF2 showed three very short helices (3-4 residues long) in the N-terminal region of the protein and a long helix in the C-terminal region spanning residues 37-46 which is consistent with the helical content indicated by circular dichroism spectroscopy. Paramagnetic relaxation enhancement NMR analysis revealed that a short C-terminal region E53-K55 is in the proximity of the N-terminus. Having the backbone assignment of SERF2 allowed us to probe its interaction with α-Synuclein and to identify the residues in SERF2 binding interfaces that likely promote α-Synuclein aggregation.

01 Dec 2023·Arteriosclerosis, Thrombosis, & Vascular Biology

Clonal Proliferation Within Smooth Muscle Cells in Unstable Human Atherosclerotic Lesions

Article

Author: Shah, Palak ; Sato, Yu ; Mokry, Michal ; Fuller, Daniela T. ; Tanaka, Takamasa ; Mori, Masayuki ; Vozenilek, Aimee E. ; Finn, Aloke V. ; Xu, Weili ; Virmani, Renu ; Pasterkamp, Gerard ; Kawai, Kenji ; Guo, Liang ; Ghosh, Saikat Kumar B. ; Dhingra, Roma ; Konishi, Takao ; Kawakami, Rika ; Sakamoto, Atsushi ; Cornelissen, Anne

BACKGROUND:Studies in humans and mice using the expression of an X-linked gene or lineage tracing, respectively, have suggested that clones of smooth muscle cells (SMCs) exist in human atherosclerotic lesions but are limited by either spatial resolution or translatability of the model.METHODS:Phenotypic clonality can be detected by X-chromosome inactivation patterns. We investigated whether clones of SMCs exist in unstable human atheroma using RNA in situ hybridization (BaseScope) to identify a naturally occurring 24-nucleotide deletion in the 3′UTR of the X-linked BGN (biglycan) gene, a proteoglycan highly expressed by SMCs. BGN-specific BaseScope probes were designed to target the wild-type or deletion mRNA. Three different coronary artery plaque types (erosion, rupture, and adaptive intimal thickening) were selected from heterozygous females for the deletion BGN. Hybridization of target RNA-specific probes was used to visualize the spatial distribution of mutants. A clonality index was calculated from the percentage of each probe in each region of interest. Spatial transcriptomics were used to identify differentially expressed transcripts within clonal and nonclonal regions.RESULTS:Less than one-half of regions of interest in the intimal plaque were considered clonal with the mean percent regions of interest with clonality higher in the intimal plaque than in the media. This was consistent for all plaque types. The relationship of the dominant clone in the intimal plaque and media showed significant concordance. In comparison with the nonclonal lesions, the regions with SMC clonality had lower expression of genes encoding cell growth suppressors such as CD74, SERF-2 (small EDRK-rich factor 2), CTSB (cathepsin B), and HLA-DPA1 (major histocompatibility complex, class II, DP alpha 1), among others.CONCLUSIONS:Our novel approach to examine clonality suggests atherosclerosis is primarily a disease of polyclonally and to a lesser extent clonally expanded SMCs and may have implications for the development of antiatherosclerotic therapies.

01 Jul 2023·Life Science Alliance

Deletion of SERF2 in mice delays embryonic development and alters amyloid deposit structure in the brain

Article

Author: Marschall, Susan ; Foijer, Floris ; Youssef, Sameh A ; Hogewerf, Wytse ; Gailus-Durner, Valerie ; Fuchs, Helmut ; Stroo, Esther ; Harkema, Liesbeth ; Koster, Mirjam ; van Deursen, Jan ; Janssen, Leen ; Beschorner, Natalie ; Hrabe de Angelis, Martin ; van de Sluis, Bart ; Becker, Lore ; Garrett, Lilian ; Wolters, Anouk Hg ; Thathiah, Amantha ; Nollen, Ellen Aa ; Sin, Olga ; de Bruin, Alain ; Wurst, Wolfgang ; Jucker, Matthias ; Bakker, Bjorn ; Hoelter, Sabine M

In age-related neurodegenerative diseases, like Alzheimer’s and Parkinson’s, disease-specific proteins become aggregation-prone and form amyloid-like deposits. Depletion of SERF proteins ameliorates this toxic process in worm and human cell models for diseases. Whether SERF modifies amyloid pathology in mammalian brain, however, has remained unknown. Here, we generated conditionalSerf2knockout mice and found that full-body deletion ofSerf2delayed embryonic development, causing premature birth and perinatal lethality. Brain-specificSerf2knockout mice, on the other hand, were viable, and showed no major behavioral or cognitive abnormalities. In a mouse model for amyloid-β aggregation, brain depletion ofSerf2altered the binding of structure-specific amyloid dyes, previously used to distinguish amyloid polymorphisms in the human brain. These results suggest thatSerf2depletion changed the structure of amyloid deposits, which was further supported by scanning transmission electron microscopy, but further study will be required to confirm this observation. Altogether, our data reveal the pleiotropic functions of SERF2 in embryonic development and in the brain and support the existence of modifying factors of amyloid deposition in mammalian brain, which offer possibilities for polymorphism-based interventions.

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SERF2

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