Keywords
Last Name

Vyacheslav Labunskyy, PhD

TitleAssistant Professor
InstitutionBoston University School of Medicine
DepartmentDermatology
Address609 Albany Street
Boston MA 02118
Phone(617) 638-5551
 Research Expertise & Professional Interests
The primary research focus of our lab is the biology of aging and understanding the basic mechanisms that underlie the pathogenesis of age-related diseases. We are particularly interested in studying the nature of senescence factors and understanding how stress response signaling regulates aging. In our work we utilize ribosome profiling and next-generation sequencing, and a combination of molecular and biochemical approaches to look at transcriptional and translational changes that are associated with the aging process as well as the mechanisms of such regulation in eukaryotic cells. A second major focus of the laboratory is synthetic biology and developing new bioengineering approaches that can be used to study complex traits, such as longevity, using yeast S. cerevisiae as a model organism.

We hope that our studies will provide a better understanding of the mechanisms that regulate aging and will help to identify new targets for therapeutic intervention for age-related diseases.

 Self-Described Keywords
  • Molecular Mechanisms of Skin Aging
  • Functional Genomics
  • Stress Signaling
  • Synthetic Biology
 Publications
Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
List All   |   Timeline
  1. Beaupere C, Wasko BM, Lorusso J, Kennedy BK, Kaeberlein M, Labunskyy VM. CAN1 Arginine Permease Deficiency Extends Yeast Replicative Lifespan via Translational Activation of Stress Response Genes. Cell Rep. 2017 Feb 21; 18(8):1884-1892. PMID: 28228255.
    View in: PubMed
  2. Gao J, Barroso C, Zhang P, Kim HM, Li S, Labrador L, Lightfoot J, Gerashchenko MV, Labunskyy VM, Dong MQ, Martinez-Perez E, Colaiácovo MP. N-terminal acetylation promotes synaptonemal complex assembly in C. elegans. Genes Dev. 2016 Nov 01; 30(21):2404-2416. PMID: 27881602.
    View in: PubMed
  3. Labunskyy VM, Hatfield DL, Gladyshev VN. Selenoproteins: molecular pathways and physiological roles. Physiol Rev. 2014 Jul; 94(3):739-77. PMID: 24987004.
    View in: PubMed
  4. Labunskyy VM, Suzuki Y, Hanly TJ, Murao A, Roth FP, Gladyshev VN. The insertion Green Monster (iGM) method for expression of multiple exogenous genes in yeast. G3 (Bethesda). 2014 Jul; 4(7):1183-91. PMID: 24776987.
    View in: PubMed
  5. Labunskyy VM, Gerashchenko MV, Delaney JR, Kaya A, Kennedy BK, Kaeberlein M, Gladyshev VN. Lifespan extension conferred by endoplasmic reticulum secretory pathway deficiency requires induction of the unfolded protein response. PLoS Genet. 2014 Jan; 10(1):e1004019. PMID: 24391512.
    View in: PubMed
  6. Labunskyy VM, Gladyshev VN. Role of reactive oxygen species-mediated signaling in aging. Antioxid Redox Signal. 2013 Oct 20; 19(12):1362-72. PMID: 22901002.
    View in: PubMed
  7. Kasaikina MV, Fomenko DE, Labunskyy VM, Lachke SA, Qiu W, Moncaster JA, Zhang J, Wojnarowicz MW, Natarajan SK, Malinouski M, Schweizer U, Tsuji PA, Carlson BA, Maas RL, Lou MF, Goldstein LE, Hatfield DL, Gladyshev VN. Roles of the 15-kDa selenoprotein (Sep15) in redox homeostasis and cataract development revealed by the analysis of Sep 15 knockout mice. J Biol Chem. 2011 Sep 23; 286(38):33203-12. PMID: 21768092.
    View in: PubMed
  8. Labunskyy VM, Lee BC, Handy DE, Loscalzo J, Hatfield DL, Gladyshev VN. Both maximal expression of selenoproteins and selenoprotein deficiency can promote development of type 2 diabetes-like phenotype in mice. Antioxid Redox Signal. 2011 Jun 15; 14(12):2327-36. PMID: 21194350.
    View in: PubMed
  9. Suzuki Y, St Onge RP, Mani R, King OD, Heilbut A, Labunskyy VM, Chen W, Pham L, Zhang LV, Tong AH, Nislow C, Giaever G, Gladyshev VN, Vidal M, Schow P, Lehár J, Roth FP. Knocking out multigene redundancies via cycles of sexual assortment and fluorescence selection. Nat Methods. 2011 Feb; 8(2):159-64. PMID: 21217751.
    View in: PubMed
  10. Shchedrina VA, Zhang Y, Labunskyy VM, Hatfield DL, Gladyshev VN. Structure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins. Antioxid Redox Signal. 2010 Apr 1; 12(7):839-49. PMID: 19747065.
    View in: PubMed
  11. Sengupta A, Carlson BA, Labunskyy VM, Gladyshev VN, Hatfield DL. Selenoprotein T deficiency alters cell adhesion and elevates selenoprotein W expression in murine fibroblast cells. Biochem Cell Biol. 2009 Dec; 87(6):953-61. PMID: 19935881.
    View in: PubMed
  12. Labunskyy VM, Yoo MH, Hatfield DL, Gladyshev VN. Sep15, a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses. Biochemistry. 2009 Sep 8; 48(35):8458-65. PMID: 19650649.
    View in: PubMed
  13. Kehr S, Malinouski M, Finney L, Vogt S, Labunskyy VM, Kasaikina MV, Carlson BA, Zhou Y, Hatfield DL, Gladyshev VN. X-ray fluorescence microscopy reveals the role of selenium in spermatogenesis. J Mol Biol. 2009 Jun 26; 389(5):808-18. PMID: 19379757.
    View in: PubMed
  14. Labunskyy VM, Hatfield DL, Gladyshev VN. The Sep15 protein family: roles in disulfide bond formation and quality control in the endoplasmic reticulum. IUBMB Life. 2007 Jan; 59(1):1-5. PMID: 17365173.
    View in: PubMed
  15. Novoselov SV, Calvisi DF, Labunskyy VM, Factor VM, Carlson BA, Fomenko DE, Moustafa ME, Hatfield DL, Gladyshev VN. Selenoprotein deficiency and high levels of selenium compounds can effectively inhibit hepatocarcinogenesis in transgenic mice. Oncogene. 2005 Dec 1; 24(54):8003-11. PMID: 16170372.
    View in: PubMed
  16. Ferguson AD, Labunskyy VM, Fomenko DE, Araç D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J. NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. J Biol Chem. 2006 Feb 10; 281(6):3536-43. PMID: 16319061.
    View in: PubMed
  17. Labunskyy VM, Ferguson AD, Fomenko DE, Chelliah Y, Hatfield DL, Gladyshev VN. A novel cysteine-rich domain of Sep15 mediates the interaction with UDP-glucose:glycoprotein glucosyltransferase. J Biol Chem. 2005 Nov 11; 280(45):37839-45. PMID: 16129668.
    View in: PubMed
  18. Shostak K, Labunskyy V, Dmitrenko V, Malisheva T, Shamayev M, Rozumenko V, Zozulya Y, Zehetner G, Kavsan V. HC gp-39 gene is upregulated in glioblastomas. Cancer Lett. 2003 Aug 20; 198(2):203-10. PMID: 12957359.
    View in: PubMed
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