About

Yuliya Skorobogatko is an Assistant Adjunct Professor in the Department of Medicine at UC San Diego. Her research focuses on various aspects of cell biology and biochemistry, including the regulation of energy storage in adipocytes, the role of neutrophils in sympathetic activation of white adipose tissue, and mechanisms of glucose homeostasis involving RalA in brown fat. She has contributed to understanding the molecular pathways involved in energy expenditure, inflammation, and neurodegeneration, with notable work on O-GlcNAc modifications and their impact on tau protein stability and neurodegenerative processes. Her research also explores the genetic and molecular basis of gastrointestinal stromal tumors and the therapeutic implications of KIT mutations. Skorobogatko's work is characterized by a focus on cellular signaling, protein modifications, and their relevance to metabolic and neurodegenerative diseases.

Research topics

• Biology
• Neuroscience
• Genetics
• Chemistry
• Internal medicine
• Medicine
• Endocrinology

Selected publications

• Limiting De Novo Lipogenesis Unlocks the Thermogenic Potential of Glucose in Brown Fat

  Research Square · 2026-02-23

  preprintOpen access1st authorCorresponding
  PublisherOA PDFDOI

• Sympathetic activation of white adipose tissue recruits neutrophils to limit energy expenditure

  Research Square · 2025-04-15 · 1 citations

  preprintOpen access
  PublisherOA PDFDOI

• Neutrophils preserve energy storage in sympathetically activated adipocytes

  Nature · 2025-12-10 · 2 citations

  articleOpen access
  PublisherOA PDFDOI

• 1674-P: Increased Glucose Uptake in Brown Fat Promotes Energy Expenditure

  Diabetes · 2023

  • Internal medicine
  • Endocrinology
  • Chemistry

  Brown and beige fat dissipate energy as heat in response to β3-adrenergic receptor (β3AR) stimulation. Strategies to facilitate this response may be employed to promote weight loss and improve health in patients with metabolic disease. Previously, we discovered that GTPase RalA and its GAP complex RalGAP regulate exocytosis of glucose transporter GLUT4. We demonstrated in vivo, that adipose-tissue specific knockout of RalGAP subunit RalGAPB activates RalA and increases glucose uptake 7 times in brown fat (BAT), leading to improved glucose handling on high fat diet (HFD). Here we seek to test the effect of increased glucose uptake in BAT on energy expenditure (EE), using mice with BAT-specific knockout of RalGAPB (the KO mice). After 8 weeks on 45% HFD, the KO mice and control littermates (Ctr) were injected with β3AR agonist CL-316,243 (CL) or PBS for 8 days. Mice assigned to CL were placed in metabolic cages. Respiratory quotient was increased in the KO mice, indicating increased glucose oxidation (likely by BAT, due to increased glucose uptake). EE at room temperature was elevated in the KO mice. This was compensated by increased food uptake, explaining similar body weights between the KO and Ctr mice. CL injections, as expected, induced spikes in EE. Acute response to CL (arbitrarily defined as EE during 2 hours after CL injection) was consistent between daily CL injections in Ctr mice, and was increased twice in the KO mice compared to Ctr. In Ctr mice, 1st CL injection increased average day and night EE; this response gradually declined with consecutive CL injections. In the KO mice, 1st CL injection elicited similar to Ctr mice increase in average day and night EE; and the response to consecutive CL injections was preserved. As anticipated, CL reduced adiposity in Ctr mice, which was further augmented in the KO mice, consistent with finding on EE. We will further test the role of increased glucose uptake by BAT in EE of the KO mice, and will determine the mechanism of sustained CL responsiveness in the KO mice. Disclosure F.Rezayat: None. J.A.Resnick: None. I.M.Farah: None. Y.Skorobogatko: None. A.Saltiel: Board Member; Elgia Therapeutics. Funding National Institutes of Health (P30DK063491)

  PublisherDOI

• Bi-allelic Variants in RALGAPA1 Cause Profound Neurodevelopmental Disability, Muscular Hypotonia, Infantile Spasms, and Feeding Abnormalities

  The American Journal of Human Genetics · 2020 · 35 citations

  • Biology
  • Neuroscience
  • Genetics
  PublisherOA PDFDOI

• TBK1 at the Crossroads of Inflammation and Energy Homeostasis in Adipose Tissue

  Cell · 2018-02-01 · 258 citations

  articleOpen access
  PublisherOA PDFDOI

• RalA controls glucose homeostasis by regulating glucose uptake in brown fat

  Proceedings of the National Academy of Sciences · 2018-06-18 · 51 citations

  articleOpen access1st author

  Insulin increases glucose uptake into adipose tissue and muscle by increasing trafficking of the glucose transporter Glut4. In cultured adipocytes, the exocytosis of Glut4 relies on activation of the small G protein RalA by insulin, via inhibition of its GTPase activating complex RalGAP. Here, we evaluate the role of RalA in glucose uptake in vivo with specific chemical inhibitors and by generation of mice with adipocyte-specific knockout of RalGAPB. RalA was profoundly activated in brown adipose tissue after feeding, and its inhibition prevented Glut4 exocytosis. RalGAPB knockout mice with diet-induced obesity were protected from the development of metabolic disease due to increased glucose uptake into brown fat. Thus, RalA plays a crucial role in glucose transport in adipose tissue in vivo.

  PublisherOA PDFDOI

• Post-translational modification of brain proteins with O-linked N-acetyl-D-glucosamine

  2013-02-01

  dissertationOpen accessSenior author

  This work contributes to understanding how post-translational modifications of proteins modulate synaptic function. Modification of synaptic proteins with the regulatory intracellular carbohydrate 0-linked N-acetylglucosamine (0-G1cNAc) is the focus of this study, which resulted in mapping of the first 0-G1cNAc sites on human brain proteins and established that modification of the synaptic protein, synapsin I, with 0-G1cNAc modulates synaptic plasticity (a property of neurons to modulate the strength of communication between synapses which is indispensible for learning and memory). Previously we found that pharmacological elevation of 0-G1cNAc in mouse brain facilitates synaptic plasticity. This facilitation is in part due to a presynaptic mechanism. One of the important presynaptic mechanisms of synaptic plasticity is generation and mobilization of a so called "reserve pool" of synaptic vesicles, which is used in addition to a "readily releasable pool" to maintain neurotransmitter release during times of high neuronal activity. Synapsin I, which is extensively modified by 0-G1cNAc, is a key synaptic vesicle binding protein that regulates the size and release of the reserve pool. Disruption of synapsin I function compromises the reserve pool of synaptic vesicles, leading to epilepsy and memory deficits. We addressed the role of synapsin I 0- GIcNAcylation in synaptic plasticity using a combination of biochemical tools, molecular biology, and imaging in primary hippocampal neurons. Based on our findings we propose a model where O-GlcNAcylation of synapsin I disrupts its association with synaptic vesicles and promotes trafficking of synaptic vesicles from the reserve pool to the readily releasable pool, thus facilitating synaptic plasticity. A single 0-GleNAc site, Thr87 which is crucial for regulating synapsin I, is located within the amphipathic lipid-packing sensor (ALPS) motif, which is responsible for preferential association of synapsin I with synaptic vesicles vs. the cell membrane. Thus, Thr87 0-GIcNAcylation decreases the affinity of synapsin I to synaptic vesicles likely through the disruption of the ALPS motif function. Since we found that synapsin 0-GleNAcylation is increased during synapse maturation, we propose that the regulation of synapsin I by 0-GIcNAc is important during synaptogenesis. Meanwhile the regulation of synapsin I O-GlcNAcylation during neurotransmission remains to be investigated.

  PublisherDOI

• O-Linked β-N-Acetylglucosamine (O-GlcNAc) Site Thr-87 Regulates Synapsin I Localization to Synapses and Size of the Reserve Pool of Synaptic Vesicles

  Journal of Biological Chemistry · 2013-11-27 · 59 citations

  articleOpen access1st authorCorresponding

  O-GlcNAc is a carbohydrate modification found on cytosolic and nuclear proteins. Our previous findings implicated O-GlcNAc in hippocampal presynaptic plasticity. An important mechanism in presynaptic plasticity is the establishment of the reserve pool of synaptic vesicles (RPSV). Dynamic association of synapsin I with synaptic vesicles (SVs) regulates the size and release of RPSV. Disruption of synapsin I function results in reduced size of the RPSV, increased synaptic depression, memory deficits, and epilepsy. Here, we investigate whether O-GlcNAc directly regulates synapsin I function in presynaptic plasticity. We found that synapsin I is modified by O-GlcNAc during hippocampal synaptogenesis in the rat. We identified three novel O-GlcNAc sites on synapsin I, two of which are known Ca(2+)/calmodulin-dependent protein kinase II phosphorylation sites. All O-GlcNAc sites mapped within the regulatory regions on synapsin I. Expression of synapsin I where a single O-GlcNAc site Thr-87 was mutated to alanine in primary hippocampal neurons dramatically increased localization of synapsin I to synapses, increased density of SV clusters along axons, and the size of the RPSV, suggesting that O-GlcNAcylation of synapsin I at Thr-87 may be a mechanism to modulate presynaptic plasticity. Thr-87 is located within an amphipathic lipid-packing sensor (ALPS) motif, which participates in targeting of synapsin I to synapses by contributing to the binding of synapsin I to SVs. We discuss the possibility that O-GlcNAcylation of Thr-87 interferes with folding of the ALPS motif, providing a means for regulating the association of synapsin I with SVs as a mechanism contributing to synapsin I localization and RPSV generation.

  PublisherOA PDFDOI

• Swi1 Associates with Chromatin through the DDT Domain and Recruits Swi3 to Preserve Genomic Integrity

  PLoS ONE · 2012-08-30 · 14 citations

  articleOpen access

  Swi1 and Swi3 form the replication fork protection complex and play critical roles in proper activation of the replication checkpoint and stabilization of replication forks in the fission yeast Schizosaccharomyces pombe. However, the mechanisms by which the Swi1-Swi3 complex regulates these processes are not well understood. Here, we report functional analyses of the Swi1-Swi3 complex in fission yeast. Swi1 possesses the DDT domain, a putative DNA binding domain found in a variety of chromatin remodeling factors. Consistently, the DDT domain-containing region of Swi1 interacts with DNA in vitro, and mutations in the DDT domain eliminate the association of Swi1 with chromatin in S. pombe cells. DDT domain mutations also render cells highly sensitive to S-phase stressing agents and induce strong accumulation of Rad22-DNA repair foci, indicating that the DDT domain is involved in the activity of the Swi1-Swi3 complex. Interestingly, DDT domain mutations also abolish Swi1's ability to interact with Swi3 in cells. Furthermore, we show that Swi1 is required for efficient chromatin association of Swi3 and that the Swi1 C-terminal domain directly interacts with Swi3. These results indicate that Swi1 associates with chromatin through its DDT domain and recruits Swi3 to function together as the replication fork protection complex.

  PublisherOA PDFDOI

Frequent coauthors

• Andrew V. Kossenkov

  37 shared

• Andrew K. Godwin

  35 shared

• Margaret von Mehren

  35 shared

• Burton Eisenberg

  Hoag Memorial Hospital Presbyterian

  35 shared

• Martin G. Belinsky

  33 shared

• Lori Rink

  33 shared

• Michael F. Ochs

  32 shared

• Thomas F. Pajak

  Sidney Kimmel Cancer Center

  16 shared