Biology:Monoaminylation

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Short description: Post-translational modifications involving monoamines

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Monoaminylation
Post-translational modification in which monoamines are covalently attached to glutamine residues via reactions catalyzed by TGM2.
Biochemical Reaction
Part of Cell
Located Nucleus, Cytoplasm
Category Post-translational Modification
Central Functions
Modulation of Synaptic Activity
Neuroepigenetic & Neuroproteomic Regulation
Regulation of Circadian Rhythm & Vascular Tone
Placental Signaling & Embryonic Development
Key Enzymes
Known Substrates
Histone Protein H3
Rho GTPases (RhoA, Rac1, Cdc42)
Rab GTPases (Rab3a, Rab27a)
Ras, SERCA2a, GAPDH, mTOR, TPI1
Fibronectin, α-actinin
Discovered
1957 Heinrich Waelsch & Colleagues
Discover calcium-dependent transglutaminases (TGMs)
2003 Diego Walther & Colleagues
Discover protein serotonylation for the first time
2011 Diego Walther & Colleagues
Propose monoaminylation as a novel set of post-translational modifications
2012 Jakob Vowinckel & Colleagues'
Discover protein histaminylation as a novel post-translational modification
2019 Lorna Farrelly & Colleagues
Discover histone serotonylation as a novel post-translational modification
2020 Ashley Lepack & Colleagues
Discover histone dopaminylation as a novel post-translational modification
2025 Qingfei Zheng & Colleagues
Discover histone histaminylation as a novel post-translational modification

Protein monoaminylation refers to the post-translational modification in which monoamines (i.e., dopamine, serotonin, histamine) are covalently attached to glutamine residues via transamidation. Monoaminylation itself refers to the overall class of post-translational modifications involving monoamines; however, these reactions are further classified by the individual monoamine reactant they describe (i.e., dopaminylation, serotonylation, histaminylation).[1]

Monoaminylation has been reported for both histone and non-histone protein substrates, and thus represents a distinct neuroepigenetic and neuroproteomic regulatory mechanism with various implications in health and disease.[1] Recent studies have unveiled the critical role of monoaminylation in mediating a wide range of physiological processes, be that in the nervous system or beyond.[1][2]

Monoaminylation is known to contribute to several significant diseases, including schizophrenia and various cancers.[1][3][4] To date, notable protein monoaminylation substrates include a number of metabolic enzymes, signal transduction proteins, and cytoskeletal proteins, as well as histone H3.[1][2]

Monoaminylation has been reported in various cell types and tissues, including monoaminergic neurons,[5][6][7][8][9] mammary epithelial cells,[10] vascular smooth muscle,[11] cancer-associated fibroblasts,[12] enterochromaffin cells,[13][14] platelets,[15][16] neutrophils,[17] CD8+ T cells,[18] endothelial cells of the lung,[19] and pancreatic 𝛽-cells.[20] It is also known to influence both tumorigenesis and cancer metastasis, and has been associated with several forms of cancer, including colorectal cancer,[13][14] neuroendocrine prostate cancer,[17] pancreatic cancer,[21] hepatocellular carcinoma,[22][23] and ependymomas (brain cancer).[6]

Identification

Protein monoaminylation was first identified in 1957 by Heinrich Waelsch and colleagues at Columbia University. After discovering that primary amines could be covalently incorporated into proteins via transamidation at glutamine residues,[24] the group went on to uncover the enzyme catalyzing these reactions, effectively naming it "transglutaminase" after its function.[25][26]

Despite its discovery in the mid-twentieth century, protein monoaminylation was not investigated as a post-translational modification until 2003, when Diego Walther and colleagues at the Max-Planck-Institute for Molecular Genetics revealed that serotonylation of small GTPases mediates ⍺-granule release during the activation and aggregation of platelets.[16]

Notably, histone monoaminylation was not uncovered as an epigenetic regulatory mechanism until 2019, when Lorna Farrelly and colleagues at the Icahn School of Medicine reported the H3Q5-serotonylation (H3Q5ser) modification for the first time.[27] Later, in 2020, the H3Q5-dopaminylation (H3Q5dop) modification was identified in the striatum by Ashley Lepack and colleagues also at the Icahn School of Medicine.[28] Five years later, Qingfei Zheng and colleagues at Ohio State University discovered the H3Q5-histaminylation (H3Q5his) modification in histaminergic neurons.[9]

Mechanism

Monoaminylation is catalyzed by transglutaminase 2 (TGM2) in a calcium-dependent manner, and relies upon the intracellular bioavailability of monoamine substrates.[2][29] Generally, protein monoaminylation occurs in the cytoplasm; however, histone monoaminylation only occurs within the nucleus.[1][29] Nevertheless, the mechanism for TGM2-catalyzed monoaminylation is identical for both histone and non-histone proteins.[1]

Structurally, Ca2+ binds directly to TGM2 itself and not to the substrate molecule.[29] Once Ca2+ binds to TGM2, a 4 nm relaxation about the major axis of the protein exposes the active site to available substrates.[29][30] The active site itself is composed of a well conserved catalytic triad (Cys277–His335–Asp358) situated within a substrate binding channel, which is bordered by two conserved residues (Trp241 and Trp332) that facilitate catalysis through stabilization of the transition state.[29][31] Once intracellular Ca2+ binds to TGM2 and exposes the substrate binding channel, the glutamine residue of a substrate protein (i.e., histone H3, RhoA) is free to enter the enzyme active site.[1][29] As a transamidation reaction, the mechanism for protein monoaminylation can be summarized in two parts: an initial thioester formation, followed by isopeptide bond formation.

Fig. 1 Mechanism for Protein Monoaminylation
Monoaminylation is a two step, Ca2+-dependent reaction in which TGM2 catalyzes the covalent attachment of a monoamine (ie., dopamine, serotonin, histamine) onto the glutamine residue of a substrate protein. (A) The catalytic cysteine residue (Cys277) of TGM2 facilitates an initial acyl transfer reaction, which is ultimately followed by isopeptide bond formation (B). Common substrate proteins include Histone H3, small GTPases (RhoA, Rab3a), and extracellular matrix proteins (fibronectin).

When intracellular Ca2+ and monoamine concentrations are sufficient, TGM2-catalyzed monoaminylation of substrate proteins can occur.[29] First, the catalytic cysteine residue (Cys277) within the TGM2 active site nucleophilically attacks the 𝛾-carboxamido group of the glutamine residue in an acyl transfer reaction (Fig. 1A), forming a thioester intermediate and releasing one molecule of ammonia (NH3) as a result.[1][29] Next, the deprotonated primary amine of the monoamine substrate nucleophilically attacks the 𝛾-thioester group of the intermediate, forming a stable isopeptide bond and ultimately releasing the enzyme (Fig. 1B).[1][29]

Functions

Histone Monoaminylation

With the discovery of histone monoaminylation in 2019, monoaminylation thus entered into the complex and ever-growing field of epigenetics, posing as a novel set of dynamic regulatory mechanisms.[1][27] To date, histone H3 is the only histone protein known to undergo monoaminylation modifications, and such modifications have only been reported for glutamine position 5 (Gln5) of histone H3 (hereafter referred to as H3Q5).[1] Thus, histone monoaminylation currently refers to the covalent addition of monoamines to glutamine at position 5 (Gln5) of histone H3.[1] Histone serotonylation remains the most widely reported histone monoaminylation modification to date,[1] though both histone dopaminylation and histone histaminylation have also been reported.[9][32]

Histone monoaminylation modifications are associated with a number of regulatory effects, no two of which appear to be the same. H3Q5-serotonylation (H3Q5ser) has been reported in a wide range of tissues and cell types, including serotonergic neurons of the dorsal raphe nucleus,[5] astrocytes of the olfactory bulb,[33][34] the inferior alveolar nerve (ie., of the lip and lower jaw),[35] placenta,[36] ependymomas (brain cancers),[6] pancreatic ductal adenocarcinoma (PDAC) tissues,[21] cancer-associated fibroblasts,[12] hepatocellular carcinoma (HCC),[22][23] and neutrophils.[17] By comparison, H3Q5-dopaminylation (H3Q5dop) has remained a far less explored topic since its discovery in 2020.[28] Nevertheless, H3Q5dop has been reported in dopaminergic neurons of the nucleus accumbens,[7] the ventral tegmental area (VTA),[8] and the amygdala.[32] H3Q5-histaminylation (H3Q5his) remains the most recent (ie., 2025) and thus least reported histone monoaminylation of all, which has been observed within histaminergic neurons of the posterior hypothalamic tuberomammillary nucleus (TMN),[9] and experimentally in vitro using HeLa cells.[9] Data as to the effects of H3Q5ser, H3Q5dop, and H3Q5his are all displayed in detail within the table below:

Monoaminylation Tissue (or Cell) Type Modification Biological Function References
Serotonylation Dorsal Raphe Nucleus
(Serotonergic neurons)		 H3K4me3Q5ser High levels induce chronic stress-related gene expression programs and attenuate behavioral resilience to stressful stimuli (Al-Kachak et al., 2024)[5]
Serotonylation Olfactory bulb
(Astrocytes)		 H3Q5ser Regulates olfactory sensory processing by promoting astrocytic GABA release (Sardar et al., 2023)[33]
Serotonylation Inferior Alveolar Nerve
(ie., of the lip and lower jaw)		 H3Q5ser Promotes sensory neuron regeneration after inferior alveolar nerve transection, enhancing sensory recovery (Mao et al., 2025)[35]
Serotonylation Placenta H3Q5ser Significantly contributes to developmental gene expression programs in placenta, impacting key neurodevelopmental transcriptional networks in the offspring brain (Chan et al., 2024)[36]
Serotonylation Ependymomas
(Serotonergic neurons)		 H3Q5ser Promotes ependymoma tumorigenesis by dysregulating the expression of a core set of developmental transcription factors (Chen et al., 2024)[6]
Serotonylation Pancreatic Ductal Adenocarcinoma (PDAC) Tissues H3K4me3Q5ser Promotes pancreatic cancer progression by upregulating SCD and remodeling lipid metabolism (Lin et al., 2025)[21]
Serotonylation Cancer-associated fibroblasts (CAFs) H3Q5ser Enhances colorectal cancer (CRC) proliferation and invasiveness by triggering a pro-inflammatory phenotype in CAFs (Ling et al., 2024)[12]
Serotonylation Hepatocellular Carcinoma (HCC) H3Q5ser Promotes HCC tumor progression by increasing chromatin accessibility, leading to increased MYC transcriptional activity (Dong et al., 2025)[23]
Serotonylation Neutrophils H3Q5ser Induces the formation of neutrophil extracellular traps (NETs) in the liver, leading to metastases in neuroendocrine (NE) cancers (Liu et al., 2025)[17]
Serotonylation Rostral Ventrolateral Medulla (RVLM), Raphe Nuclei H3K4me3Q5ser Delays ejaculation by recruiting MZF1 to the DRD4 promoter, upregulating DRD4 expression (Gao et al., 2023)[37]
Dopaminylation Nucleus Accumbens (NAc) H3Q5dop Promotes cocaine-seeking behavior and regulates cocaine-induced gene expression programs (Stewart et al., 2023)[7]
Dopaminylation Ventral Tegmental Area (VTA) H3Q5dop Promotes heroin-seeking behavior and regulates gene expression programs associated with heroin abstinence (Fulton et al., 2022)
Dopaminylation Amygdala H3Q5dop Modification was identified following early-life stressful social experience (SSE) in rat pups (Rajan et al., 2023)[32]
Histaminylation Posterior Hypothalamic Tuberomammillary Nucleus (TMN) H3Q5his Diurnally rhythmic expression in the brain contributes to circadian gene expression and behavior (Zheng et al., 2025)[9]

Combinatory effects between monoaminylation and other histone modifications have been reported.[5] Herein, low levels of trimethylation and serotonylation of histone H3 at lysine position 4 (H3K4) and glutamine position 5 (H3Q5), respectively (ie., H3K4me3Q5ser), in the dorsal raphe nucleus led to depressive symptoms in both male and female mice exposed to chronic stress.[5] Behavioral outcomes associated with H3K4me3Q5ser depletion were corrected by treatment with serotonin-associated antidepressants, thus evidencing such antidepressants as sufficient to attenuate stress-mediated gene expression and behavioral dysregulation.[5] Interestingly, corresponding patterns of H3K4me3Q5ser depletion were observed in the brains of major depressive disorder (MDD) patients on vs. off antidepressants at their time of death, thus evidencing a neurotransmission-independent role for serotonin in mediating both stress-associated and anti-depressant-associated transcriptional plasticity and behavioral outcomes.[5]

Similarly, low levels of trimethylation and dopaminylation of histone H3 at lysine position 4 (H3K4) and glutamine position 5 (H3Q5) in the amygdala led to failure in novel odor recognition for rat pups undergoing novel odor preference testing.[32] However, the authors of this study omit whether such modifications were in fact detected concurrently (ie., H3K4me3Q5dop). Nevertheless, scent recognition testing serves as a critical methodology for evaluating memory, cognitive function, and sensory perception in rodent models, and thus represents an important mechanism for evaluating changes in neurotransmission and epigenetic regulation in response to environmental conditions such as stress.[32][38] Herein, failure to recognize novel odor was reportedly linked to increased dopamine transmission, decreased levels of TGM2, and increased histone trimethylation (H3K4me3) and dopaminylation (H3Q5dop) in the amygdala following exposure to early-life stressful social experience (SSE).[32] It remains unclear whether the reported fluctuations in TGM2 levels could be attributed to changes in TGM2 expression levels or changes in TGM2 activity levels.[32] Ambiguity aside, this data provides useful insight, as early-life adversity paradigms appear sufficient for reconfiguration of epigenetic signatures within the limbic system, thereby establishing stable, differential epigenetic programs which may contribute to lifelong susceptibility for affective psychopathologies (ie., major depressive disorder, bipolar disorder, anxiety disorders).[1][32]

See also

References

  1. ↑ 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 Zhao, Yiqi; Zhang, Hongli; Yang, Yating; Chen, Wei-Dong; Wang, Yan-Dong (March 2026). "Monoaminylation in Human Health and Disease: State of the Field, Challenges, and Emerging Directions". Advanced Science (Weinheim, Baden-Wurttemberg, Germany) 13 (16). doi:10.1002/advs.202520653. ISSN 2198-3844. PMID 41662496. Bibcode: 2026AdvSc..1320653Z. 
  2. ↑ 2.0 2.1 2.2 Walther, Diego J.; Stahlberg, Silke; Vowinckel, Jakob (December 2011). "Novel roles for biogenic monoamines: from monoamines in transglutaminase-mediated post-translational protein modification to monoaminylation deregulation diseases". The FEBS Journal 278 (24): 4740–4755. doi:10.1111/j.1742-4658.2011.08347.x. ISSN 1742-4658. PMID 21923757. 
  3. ↑ Chen, Yun-Zhou; Zhu, Xiu-Mei; Lv, Peng; Hou, Xi-Kai; Pan, Ying; Li, Ang; Du, Zhe; Xuan, Jin-Feng et al. (June 2024). "Association of histone modification with the development of schizophrenia". Biomedicine & Pharmacotherapy = Biomedecine & Pharmacotherapie 175. doi:10.1016/j.biopha.2024.116747. ISSN 1950-6007. PMID 38744217. 
  4. ↑ Li, Huapeng; Wu, Jinghua; Zhang, Nan; Zheng, Qingfei (2024-08-28). "Transglutaminase 2-mediated histone monoaminylation and its role in cancer". Bioscience Reports 44 (8). doi:10.1042/BSR20240493. ISSN 1573-4935. PMID 39115570. 
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 Al-Kachak, Amni; Di Salvo, Giuseppina; Fulton, Sasha L.; Chan, Jennifer C.; Farrelly, Lorna A.; Lepack, Ashley E.; Bastle, Ryan M.; Kong, Lingchun et al. (2024-06-13). "Histone serotonylation in dorsal raphe nucleus contributes to stress- and antidepressant-mediated gene expression and behavior" (in en). Nature Communications 15 (1): 5042. doi:10.1038/s41467-024-49336-4. ISSN 2041-1723. PMID 38871707. Bibcode: 2024NatCo..15.5042A. 
  6. ↑ 6.0 6.1 6.2 6.3 Chen, Hsiao-Chi; He, Peihao; McDonald, Malcolm; Williamson, Michael R.; Varadharajan, Srinidhi; Lozzi, Brittney; Woo, Junsung; Choi, Dong-Joo et al. (August 2024). "Histone serotonylation regulates ependymoma tumorigenesis" (in en). Nature 632 (8026): 903–910. doi:10.1038/s41586-024-07751-z. ISSN 1476-4687. PMID 39085609. Bibcode: 2024Natur.632..903C. 
  7. ↑ 7.0 7.1 7.2 Stewart, Andrew F.; Lepack, Ashley E.; Fulton, Sasha L.; Safovich, Polina; Maze, Ian (June 2023). "Histone H3 dopaminylation in nucleus accumbens, but not medial prefrontal cortex, contributes to cocaine-seeking following prolonged abstinence". Molecular and Cellular Neurosciences 125. doi:10.1016/j.mcn.2023.103824. ISSN 1095-9327. PMID 36842545. 
  8. ↑ 8.0 8.1 Fulton, Sasha L.; Mitra, Swarup; Lepack, Ashley E.; Martin, Jennifer A.; Stewart, Andrew F.; Converse, Jacob; Hochstetler, Mason; Dietz, David M. et al. (September 2022). "Histone H3 dopaminylation in ventral tegmental area underlies heroin-induced transcriptional and behavioral plasticity in male rats". Neuropsychopharmacology: Official Publication of the American College of Neuropsychopharmacology 47 (10): 1776–1783. doi:10.1038/s41386-022-01279-4. ISSN 1740-634X. PMID 35094023. 
  9. ↑ 9.0 9.1 9.2 9.3 9.4 9.5 Zheng, Qingfei; Weekley, Benjamin H.; Vinson, David A.; Zhao, Shuai; Bastle, Ryan M.; Thompson, Robert E.; Stransky, Stephanie; Ramakrishnan, Aarthi et al. (January 2025). "Bidirectional histone monoaminylation dynamics regulate neural rhythmicity". Nature 637 (8047): 974–982. doi:10.1038/s41586-024-08371-3. ISSN 1476-4687. PMID 39779849. Bibcode: 2025Natur.637..974Z. 
  10. ↑ Sheftel, Celeste M.; Hernandez, Laura L. (2020). "Serotonin stimulated parathyroid hormone related protein induction in the mammary epithelia by transglutaminase-dependent serotonylation". PLOS ONE 15 (10). doi:10.1371/journal.pone.0241192. ISSN 1932-6203. PMID 33095824. Bibcode: 2020PLoSO..1541192S. 
  11. ↑ Watts, Stephanie W.; Priestley, Jessica R. C.; Thompson, Janice M. (2009-05-25). "Serotonylation of vascular proteins important to contraction". PLOS ONE 4 (5). doi:10.1371/journal.pone.0005682. ISSN 1932-6203. PMID 19479059. Bibcode: 2009PLoSO...4.5682W. 
  12. ↑ 12.0 12.1 12.2 Ling, Tianlong; Dai, Zhanghan; Wang, Houming; Kien, Tran Trung; Cui, Rong; Yu, Tachung; Chen, Jianjun (2024-09-28). "Serotonylation in tumor-associated fibroblasts contributes to the tumor-promoting roles of serotonin in colorectal cancer". Cancer Letters 600. doi:10.1016/j.canlet.2024.217150. ISSN 1872-7980. PMID 39097134. 
  13. ↑ 13.0 13.1 Ye, Di; Xu, Huanji; Xia, Hongwei; Zhang, Chenliang; Tang, Qiulin; Bi, Feng (2021-05-18). "Targeting SERT promotes tryptophan metabolism: mechanisms and implications in colon cancer treatment". Journal of Experimental & Clinical Cancer Research: CR 40 (1): 173. doi:10.1186/s13046-021-01971-1. ISSN 1756-9966. PMID 34006301. 
  14. ↑ 14.0 14.1 Yu, Huangfei; Qu, Tianyin; Yang, Jinlan; Dai, Qing (2023-04-12). "Serotonin acts through YAP to promote cell proliferation: mechanism and implication in colorectal cancer progression". Cell Communication and Signaling: CCS 21 (1): 75. doi:10.1186/s12964-023-01096-2. ISSN 1478-811X. PMID 37046308. 
  15. ↑ Guilluy, Christophe; Eddahibi, Saadia; Agard, Christian; Guignabert, Christophe; Izikki, Mohamed; Tu, Ly; Savale, Laurent; Humbert, Marc et al. (2009-06-15). "RhoA and Rho kinase activation in human pulmonary hypertension: role of 5-HT signaling". American Journal of Respiratory and Critical Care Medicine 179 (12): 1151–1158. doi:10.1164/rccm.200805-691OC. ISSN 1535-4970. PMID 19299501. 
  16. ↑ 16.0 16.1 Walther, Diego J.; Peter, Jens-Uwe; Winter, Sandra; Höltje, Markus; Paulmann, Nils; Grohmann, Maik; Vowinckel, Jakob; Alamo-Bethencourt, Victor et al. (2003-12-26). "Serotonylation of Small GTPases Is a Signal Transduction Pathway that Triggers Platelet α-Granule Release" (in English). Cell 115 (7): 851–862. doi:10.1016/S0092-8674(03)01014-6. ISSN 0092-8674. PMID 14697203. https://www.cell.com/cell/abstract/S0092-8674(03)01014-6. 
  17. ↑ 17.0 17.1 17.2 17.3 Liu, Kaiyuan; Zhang, Yingchao; Du, Genyu; Chen, Xinyu; Xiao, Lingling; Jiang, Luyao; Jing, Na; Xu, Penghui et al. (2025-04-15). "5-HT orchestrates histone serotonylation and citrullination to drive neutrophil extracellular traps and liver metastasis". The Journal of Clinical Investigation 135 (8). doi:10.1172/JCI183544. ISSN 1558-8238. PMID 39903533. 
  18. ↑ Wang, Xu; Fu, Sheng-Qiao; Yuan, Xiao; Yu, Feng; Ji, Qian; Tang, Hao-Wen; Li, Rong-Kun; Huang, Shan et al. (2024-02-15). "A GAPDH serotonylation system couples CD8+ T cell glycolytic metabolism to antitumor immunity". Molecular Cell 84 (4): 760–775.e7. doi:10.1016/j.molcel.2023.12.015. ISSN 1097-4164. PMID 38215751. 
  19. ↑ Mo, Chunheng; Li, Hui; Yan, Mengli; Xu, Shiyu; Wu, Jinyan; Li, Jiachen; Yang, Xinchun; Li, Yuanyuan et al. (2024-08-06). "Dopaminylation of endothelial TPI1 suppresses ferroptotic angiocrine signals to promote lung regeneration over fibrosis". Cell Metabolism 36 (8): 1839–1857.e12. doi:10.1016/j.cmet.2024.07.008. ISSN 1932-7420. PMID 39111287. 
  20. ↑ Yoo, Yeong-Min; Joo, Seong Soo (2024-06-21). "Serotonin Influences Insulin Secretion in Rat Insulinoma INS-1E Cells". International Journal of Molecular Sciences 25 (13): 6828. doi:10.3390/ijms25136828. ISSN 1422-0067. PMID 38999937. 
  21. ↑ 21.0 21.1 21.2 Lin, Sang; Tan, Sheng; Peng, Yonglin; Tulamaiti, Aziguli; Du, Wenfei; Ding, Keshuo; Chen, Changyu; Wu, Jun et al. (2025-07-01). "Histone serotonylation promotes pancreatic cancer development via lipid metabolism remodeling" (in en). Nature Communications 16 (1): 5947. doi:10.1038/s41467-025-61197-z. ISSN 2041-1723. PMID 40593695. Bibcode: 2025NatCo..16.5947L. 
  22. ↑ 22.0 22.1 Navarro-Corcuera, Amaia; Martínez-Chantar, María L. (July 2025). "Histone serotonylation in HCC: Decoding the impact of "happy" histones on liver cancer progression". Journal of Hepatology 83 (1): 18–20. doi:10.1016/j.jhep.2025.02.020. ISSN 1600-0641. PMID 40023196. 
  23. ↑ 23.0 23.1 23.2 Dong, Renshun; Wang, Tianci; Dong, Wei; Zhang, Haoquan; Li, Yani; Tao, Ran; Liu, Qiumeng; Liang, Huifang et al. (July 2025). "TGM2-mediated histone serotonylation promotes HCC progression via MYC signalling pathway". Journal of Hepatology 83 (1): 105–118. doi:10.1016/j.jhep.2024.12.038. ISSN 1600-0641. PMID 39788430. 
  24. ↑ Sarkar, N. K.; Clarke, D. D.; Waelsch, H. (August 1957). "An enzymically catalyzed incorporation of amines into proteins". Biochimica et Biophysica Acta 25 (2): 451–452. doi:10.1016/0006-3002(57)90512-7. ISSN 0006-3002. PMID 13471608. 
  25. ↑ Mycek, M. J.; Clarke, D. D.; Neidle, A.; Waelsch, H. (1959-10-01). "Amine incorporation into insulin as catalyzed by transglutaminase". Archives of Biochemistry and Biophysics 84 (2): 528–540. doi:10.1016/0003-9861(59)90613-7. ISSN 0003-9861. PMID 14425580. 
  26. ↑ Bader, Michael (2019). "Serotonylation: Serotonin Signaling and Epigenetics". Frontiers in Molecular Neuroscience 12. doi:10.3389/fnmol.2019.00288. ISSN 1662-5099. PMID 31824263. 
  27. ↑ 27.0 27.1 Farrelly, Lorna A.; Thompson, Robert E.; Zhao, Shuai; Lepack, Ashley E.; Lyu, Yang; Bhanu, Natarajan V.; Zhang, Baichao; Loh, Yong-Hwee E. et al. (March 2019). "Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3". Nature 567 (7749): 535–539. doi:10.1038/s41586-019-1024-7. ISSN 1476-4687. PMID 30867594. Bibcode: 2019Natur.567..535F. 
  28. ↑ 28.0 28.1 Lepack, Ashley E.; Werner, Craig T.; Stewart, Andrew F.; Fulton, Sasha L.; Zhong, Ping; Farrelly, Lorna A.; Smith, Alexander C. W.; Ramakrishnan, Aarthi et al. (2020-04-10). "Dopaminylation of histone H3 in ventral tegmental area regulates cocaine seeking". Science (New York, N.Y.) 368 (6487): 197–201. doi:10.1126/science.aaw8806. ISSN 1095-9203. PMID 32273471. Bibcode: 2020Sci...368..197L. 
  29. ↑ 29.0 29.1 29.2 29.3 29.4 29.5 29.6 29.7 29.8 Király, Róbert; Demény, MátéÁ.; Fésüs, László (2011-11-21). "Protein transamidation by transglutaminase 2 in cells: a disputed Ca2+-dependent action of a multifunctional protein" (in en). The FEBS Journal 278 (24): 4717–4739. doi:10.1111/j.1742-4658.2011.08345.x. ISSN 1742-464X. PMID 21902809. https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2011.08345.x. 
  30. ↑ Di Venere, A.; Rossi, A.; De Matteis, F.; Rosato, N.; Agrò, A. F.; Mei, G. (2000-02-11). "Opposite effects of Ca(2+) and GTP binding on tissue transglutaminase tertiary structure". The Journal of Biological Chemistry 275 (6): 3915–3921. doi:10.1074/jbc.275.6.3915. ISSN 0021-9258. PMID 10660544. 
  31. ↑ Iismaa, Siiri E.; Holman, Sara; Wouters, Merridee A.; Lorand, Laszlo; Graham, Robert M.; Husain, Ahsan (2003-10-28). "Evolutionary specialization of a tryptophan indole group for transition-state stabilization by eukaryotic transglutaminases". Proceedings of the National Academy of Sciences of the United States of America 100 (22): 12636–12641. doi:10.1073/pnas.1635052100. ISSN 0027-8424. PMID 14566064. Bibcode: 2003PNAS..10012636I. 
  32. ↑ 32.0 32.1 32.2 32.3 32.4 32.5 32.6 32.7 Rajan, Koilmani Emmanuvel; Karen, Christopher; Dhivakar, Selvavinayagam (2023-07-13). "Early-life stressful social experience (SSE) alters ultrasound vocalizations and impairs novel odor preference: Influence of histone dopaminylation". Neuroscience Letters 809. doi:10.1016/j.neulet.2023.137304. ISSN 0304-3940. PMID 37225119. https://www.sciencedirect.com/science/article/pii/S030439402300263X. 
  33. ↑ 33.0 33.1 Sardar, Debosmita; Cheng, Yi-Ting; Woo, Junsung; Choi, Dong-Joo; Lee, Zhung-Fu; Kwon, Wookbong; Chen, Hsiao-Chi; Lozzi, Brittney et al. (2023-06-16). "Induction of astrocytic Slc22a3 regulates sensory processing through histone serotonylation". Science (New York, N.Y.) 380 (6650). doi:10.1126/science.ade0027. ISSN 1095-9203. PMID 37319217. 
  34. ↑ Sardar, Debosmita; Cheng, Yi-Ting; Woo, Junsung; Choi, Dong-Joo; Lee, Zhung-Fu; Kwon, Wookbong; Chen, Hsiao-Chi; Lozzi, Brittney; Cervantes, Alexis; Rajendran, Kavitha; Huang, Teng-Wei; Jain, Antrix; Arenkiel, Benjamin; Maze, Ian; Deneen, Benjamin (2023-02-27). "Activity-dependent induction of astrocytic Slc22a3 regulates sensory processing through histone serotonylation". pp. 2023.02.24.529904. bioRxiv 10.1101/2023.02.24.529904.
  35. ↑ 35.0 35.1 Mao, Suning; Zhang, Gaowei; Ma, Pingchuan; Ma, Zhongkai; Li, Chunjie; Ye, Li (2025-10-01). "Serotonin promotes lip sensory recovery after inferior alveolar nerve transection via histone serotonylation". Journal of Dental Sciences 20 (4): 2363–2374. doi:10.1016/j.jds.2025.04.001. ISSN 1991-7902. PMID 41040553. 
  36. ↑ 36.0 36.1 Chan, Jennifer C.; Alenina, Natalia; Cunningham, Ashley M.; Ramakrishnan, Aarthi; Shen, Li; Bader, Michael; Maze, Ian (2024-04-01). "Serotonin Transporter-dependent Histone Serotonylation in Placenta Contributes to the Neurodevelopmental Transcriptome". Journal of Molecular Biology. Interpreting Combinatorial Epigenetic Modifications for Biological Meaning 436 (7). doi:10.1016/j.jmb.2024.168454. ISSN 0022-2836. PMID 38266980. 
  37. ↑ Gao, Pan; Liu, Xi; Zhu, Tianle; Gao, Rui; Gao, Jingjing; Zhang, Yao; Jiang, Hui; Huang, Houbao et al. (September 2023). "Vital function of DRD4 in dapoxetine medicated premature ejaculation treatment" (in en). Andrology 11 (6): 1175–1187. doi:10.1111/andr.13390. ISSN 2047-2919. PMID 36746766. https://onlinelibrary.wiley.com/doi/10.1111/andr.13390. 
  38. ↑ Saak, Tiana M.; Zhang, Renjie; Spence, Matthew D.A.; Devanand, Davangere P.; Overdevest, Jonathan B.; Motter, Jeffrey N. (December 2025). "Performance on a novel odor recognition memory test preferentially associates with specific cognitive measures and psychophysical characteristics" (in en). Alzheimer's & Dementia 21 (S3). doi:10.1002/alz70857_106541. ISSN 1552-5260. 



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