The Sever Laboratory

 Basic Scientific Research With Clinical Relevance


Why do we study molecular mechanisms of kidney diseases?

Despite hundreds of millions of people losing kidney function world-wide every year, no kidney-specific therapeutics exist. The current treatments for kidney loss, dialysis and transplant, significantly diminish quality of life and life span. The goal of our research is to elucidate the molecular mechanisms of kidney diseases to identify druggable pathways and develop new therapeutics. We primarily focus on the role of the GTPase dynamin in regulating actin cytoskeleton dynamics and clathrin-mediated endocytosis. Disregulation of both of these processes has been implicated in the loss of kidney-specific cells called podocytes that are required for kidney function. Gaining a better understanding of podocyte pathobiology will lay the groundwork to cure kidney disease.

Why study dynamin?

Dyamin is a founding member of a superfamily of large GTPases that exist in multiple oligomerization states. Dynamin is best known for its role in clathrin-mediated endocytosis. Its ability to self-assemble into helices on lipid templates in vitro has led to the paradigm that dynamin directly executes the fission reaction in which coated pits are freed from the plasma membrane. We have identified regulation of the actin cytoskeleton as an additional and distinct role for dynamin oligomerization in podocytes and other cell types. By using classic cell biology, biochemistry, single molecule imaging, and animal models, we are establishing novel paradigms for dynamin function, the actin cytoskeleton, and endocytosis in healthy and injured kidney cells.

Why join the Sever laboratory?

The Sever lab is a welcoming and highly interactive environment. Post-doctoral fellows and research technicians share expertise, reagents, and ideas to reach their common goal of understanding how dynamin regulates the actin cytoskeleton in healthy and diseased tissue. We are always looking for energetic and accomplished post-doctoral fellows with expertise in molecular biology, biochemistry, and/or biophysics.


The establishment of distinct, cell-type specific, cellular features, including cell polarity, involve signaling cascades, membrane trafficking, and cytoskeletal dynamics, all of which need to be highly coordinated and regulated.  We seek to understand the role of the GTPase dynamin as one of the major coordinators of multiple cellular processes including endocytosis, actin cytoskeleton dynamics, as well as microtubule dynamics, in healthy and injured cells. 

Regulation of the actin cytoskeleton

In 2010 we identified direct interactions between dynamin and actin filaments and we have since shown that the dynamin oligomerization cycle plays a direct role in regulating actin polymerization and crosslinking of actin filaments. These interactions have since been implicated in highly diverse cellular processes including endocytosis, the formation of lamellipodia, filopodia invadopodia, and growth cones in neuronal cells. All these processes are driven by the association of distinct actin structures with the plasma membrane. We now seek to identify the molecular mechanisms by which dynamin establishes such diverse cellular processes. Utilizing biochemical and cell biology assays, and total internal reflection fluorescence (TIRF) single-molecule imaging, we plan to elucidate the mechanism by which dynamin regulates actin and microtubule dynamics.  We use kidney specific cells named podocytes as an experimental model system to study the role of dynamin with regard to endocytosis, the actin cytoskeleton, and microtubule dynamics. Podocytes are terminally differentiated cells that form the filtration barrier in the kidney. Damage or loss of podocytes is an early symptom of many kidney diseases as structural integrity of the podocyte actin and microtubule cytoskeleton is critical for its proper function. Better understanding podocyte pathobiology has lead to the establishment of novel paradigms with regard to role of dynamin in the cell and has the potential to pave the way for developing a cure for kidney diseases. 

This photo shows the structure of podocytes in mice expressing dynamin mutant R725A, which increases dynamin’s propensity to oligomerize into higher-order structures such as rings. Dynamin oligomerization has been implicated in clathrin-mediated endocytosis, but here we show for the first time that its oligomerization plays an essential physiological role by directly regulating the actin cytoskeleton. This, in turn, drives the formation of foot processes that are significantly longer than those in wild-type animals as well as those in animals before Doxycycline treatment (used to drive expression of DynR725A). It is very rare to see such a dramatic effect on the length of the foot processes (FPs) since dominant-negative mutations of diverse proteins expressed in podocytes typically result in the loss of FPs. It should be noted that this particular dynamin mutant (DynR725A) has been published by Dr. Sever back in 1999 in Nature (Sever et al, Nature 1999). This mutant suggested that dynamin is a regulatory GTPase and not a pinchase. As you can see, this mutant has a long history.

Clathrin Mediated Endocytosis

We are also interested in the role of dynamin in clathrin-mediated endocytosis. The classical view of dynamin holds that it acts as a mechanochemical enzyme or "pinchase," severing vesicles from the plasma membrane. Our work suggests an alternative model in which dynamin is a regulatory GTPase, orchestrating formation of clathrin-coated vesicles. In this view unoligomerized dynamin recruits additional proteins that drive formation of fully invaginated coated pits and subsequent budding of free vesicles. Our latest studies suggest that dynamin oligomerization may play an indirect but global role in endocytosis through regulation of actin. 

This image shows localization of dynamin (labeled with black dots) on clathrin coated vesicles (labeled 'V') in foot processes of mice.

Molecular mechanisms of kidney diseases

Chronic kidney disease, which is loss of kidney function over time, affects hundreds of millions of people worldwide. It is often associated with the appearance of significant amounts of high-molecular-weight plasma proteins such as albumin in the urine (termed proteinuria), a symptom of a compromised glomerular filtration barrier.  Chronic kidney disease can occur due to genetic mutations in “house keeping genes” such as a-actinin 4, or more often as a secondary effect of diabetes and hypertension. Irrespective of genetic or disease-based causes, podocyte injury underlies loss of kidney function.  Podocytes are terminally differentiated cells of the glomerulus, which consist of a cell body, primary microtubule-driven membrane extensions, as well as secondary actin-based membrane extensions called foot processes. Sustained dis-regulation of the actin cytoskeleton in foot processes ultimately leads to podocyte loss.  We have shown that pharmacological targeting of actin-dependent dynamin oligomerization ameliorates chronic kidney disease in diverse animal models. Our study established the first successful targeting of the actin cytoskeleton dynamics in foot processes and in the whole organism. Current research in the lab focuses on interplay between actin, microtubule dynamics, and endocytosis, and the role of dynamin in coordinating these processes in podocytes. We are also examining role of these processes in polarized epithelial cells of renal tubules. Cells of the renal tubules are often injured during anti-cancer therapies, resulting in acute loss of kidney function. The immerging view of kidney disease is that regardless of the injury (diabetes, hypertension, anti-cancer drugs, genetics), the whole organ is somehow affected. Our current challenge is to establish comprehensive understanding of the kidney injury as a whole organ, instead of focusing only on distinct cell types within the organ (podocytes vs epithelial cells).

This image shows dynamin (green) localization at actin filaments and focal adhesions in cultured differentiated mouse podocytes. The actin filaments and focal adhesions are labeled in red.

Florescence lifetime image microscopy (FLIM) was used to identify localization of dynamin oligomers in cultured podocytes (red signal).

Molecular Mechanisms of neurodegenerative diseases

As is the case with kidney diseases, the identification of therapeutic targets based on novel mechanistic studies is urgently needed for neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, and prion diseases. Given our insights regarding the role of the actin cytoskeleton and dynamin in the kidney, we are currently testing our hypothesis that targeting the actin cytoskeleton of dendritic spines may preserve and even reverse early signs of neurodegeneration. The Sever laboratory is striving to establish a unique environment with MGH and HMS where focusing on the basic cellular processes such as dynamin, actin, microtubules ,and endocytosis, we can elucidate common and cell type specific molecular mechanisms that govern highly diverse diseases.

Actin based foot processes of podocytes (left image) are structurally similar to actin based dendritic spines in neurons (right image).


  1. The D2D3 form of uPAR acts as an immunotoxin and may cause diabetes and kidney disease. (Sci Transl Med 2023)
    Zhu, K, Mukherjee, K, Wei, C, Hayek, SS, Collins, A, Gu, C, Corapi, K, Altintas, MM, Wang, Y, Waikar, SS, Bianco, AC, Koch, A, Tacke, F, Reiser, J, Sever, S

  2. The small GTPase regulatory protein Rac1 drives podocyte injury independent of cationic channel protein TRPC5. (Kidney Int 2023)
    Polat, OK, Isaeva, E, Sudhini, YR, Knott, B, Zhu, K, Noben, M, Suresh Kumar, V, Endlich, N, Mangos, S, Reddy, TV, Samelko, B, Wei, C, Altintas, MM, Dryer, SE, Sever, S, Staruschenko, A, Reiser, J

  3. Simultaneous stabilization of actin cytoskeleton in multiple nephron-specific cells protects the kidney from diverse injury. (Nat Commun 2022)
    Mukherjee, K, Gu, C, Collins, A, Mettlen, M, Samelko, B, Altintas, MM, Sudhini, YR, Wang, X, Bouley, R, Brown, D, Pedro, BP, Bane, SL, Gupta, V, Brinkkoetter, PT, Hagmann, H, Reiser, J, Sever, S

  4. A Novel Fluorogenic Assay for the Detection of Nephrotoxin-Induced Oxidative Stress in Live Cells and Renal Tissue. (ACS Sens 2021)
    Mukherjee, K, Chio, TI, Gu, H, Sackett, DL, Bane, SL, Sever, S

  5. Role of actin cytoskeleton in podocytes. (Pediatr Nephrol 2021)
    Sever, S

  6. Soluble Urokinase Receptor and Acute Kidney Injury. (N Engl J Med 2020)
    Hayek, SS, Leaf, DE, Samman Tahhan, A, Raad, M, Sharma, S, Waikar, SS, Sever, S, Camacho, A, Wang, X, Dande, RR, Ibrahim, NE, Baron, RM, Altintas, MM, Wei, C, Sheikh-Hamad, D, Pan, JS, Holliday, MW Jr, Januzzi, JL, Weisbord, SD, Quyyumi, AA, Reiser, J

  7. uPAR isoform 2 forms a dimer and induces severe kidney disease in mice. (J Clin Invest 2019)
    Wei, C, Li, J, Adair, BD, Zhu, K, Cai, J, Merchant, M, Samelko, B, Liao, Z, Koh, KH, Tardi, NJ, Dande, RR, Liu, S, Ma, J, Dibartolo, S, Hägele, S, Peev, V, Hayek, SS, Cimbaluk, DJ, Tracy, M, Klein, J, Sever, S, Shattil, SJ, Arnaout, MA, Reiser, J

  8. Actin dynamics at focal adhesions: a common endpoint and putative therapeutic target for proteinuric kidney diseases. (Kidney Int 2018)
    Sever, S, Schiffer, M

  9. Rituximab and Therapeutic Plasma Exchange in Recurrent Focal Segmental Glomerulosclerosis Postkidney Transplantation. (Transplantation 2018)
    Alasfar, S, Matar, D, Montgomery, RA, Desai, N, Lonze, B, Vujjini, V, Estrella, MM, Manllo Dieck, J, Khneizer, G, Sever, S, Reiser, J, Alachkar, N

  10. Cardiovascular Disease Biomarkers and suPAR in Predicting Decline in Renal Function: A Prospective Cohort Study. (Kidney Int Rep 2017)
    Hayek, SS, Ko, YA, Awad, M, Ahmed, H, Gray, B, Hosny, KM, Aida, H, Tracy, MJ, Wei, C, Sever, S, Reiser, J, Quyyumi, AA

  11. Association of Serum Soluble Urokinase Receptor Levels With Progression of Kidney Disease in Children. (JAMA Pediatr 2017)
    Schaefer, F, Trachtman, H, Wühl, E, Kirchner, M, Hayek, SS, Anarat, A, Duzova, A, Mir, S, Paripovic, D, Yilmaz, A, Lugani, F, Arbeiter, K, Litwin, M, Oh, J, Matteucci, MC, Gellermann, J, Wygoda, S, Jankauskiene, A, Klaus, G, Dusek, J, Testa, S, Zurowska, A, Caldas Afonso, A, Tracy, M, Wei, C, Sever, S, Smoyer, W, Reiser, J, ESCAPE Trial Consortium and the 4C Study Group

  12. A tripartite complex of suPAR, APOL1 risk variants and αvβ3 integrin on podocytes mediates chronic kidney disease. (Nat Med 2017)
    Hayek, SS, Koh, KH, Grams, ME, Wei, C, Ko, YA, Li, J, Samelko, B, Lee, H, Dande, RR, Lee, HW, Hahm, E, Peev, V, Tracy, M, Tardi, NJ, Gupta, V, Altintas, MM, Garborcauskas, G, Stojanovic, N, Winkler, CA, Lipkowitz, MS, Tin, A, Inker, LA, Levey, AS, Zeier, M, Freedman, BI, Kopp, JB, Skorecki, K, Coresh, J, Quyyumi, AA, Sever, S, Reiser, J

  13. Soluble Urokinase Plasminogen Activator Receptor and Outcomes in Patients with Diabetes on Hemodialysis. (Clin J Am Soc Nephrol 2017)
    Drechsler, C, Hayek, SS, Wei, C, Sever, S, Genser, B, Krane, V, Meinitzer, A, März, W, Wanner, C, Reiser, J

  14. Drugs targeting dynamin can restore cytoskeleton and focal contact alterations of urinary podocytes derived from patients with nephrotic syndrome. (Ann Transl Med 2016)
    Müller-Deile, J, Teng, B, Schenk, H, Haller, H, Reiser, J, Sever, S, Schiffer, M

  15. Bone marrow-derived immature myeloid cells are a main source of circulating suPAR contributing to proteinuric kidney disease. (Nat Med 2017)
    Hahm, E, Wei, C, Fernandez, I, Li, J, Tardi, NJ, Tracy, M, Wadhwani, S, Cao, Y, Peev, V, Zloza, A, Lusciks, J, Hayek, SS, O'Connor, C, Bitzer, M, Gupta, V, Sever, S, Sykes, DB, Scadden, DT, Reiser, J

  16. Anks1a regulates COPII-mediated anterograde transport of receptor tyrosine kinases critical for tumorigenesis. (Nat Commun 2016)
    Lee, H, Noh, H, Mun, J, Gu, C, Sever, S, Park, S

  17. Dynamin Autonomously Regulates Podocyte Focal Adhesion Maturation. (J Am Soc Nephrol 2017)
    Gu, C, Lee, HW, Garborcauskas, G, Reiser, J, Gupta, V, Sever, S

  18. Soluble Urokinase Receptor and Chronic Kidney Disease. (N Engl J Med 2015)
    Hayek, SS, Sever, S, Ko, YA, Trachtman, H, Awad, M, Wadhwani, S, Altintas, MM, Wei, C, Hotton, AL, French, AL, Sperling, LS, Lerakis, S, Quyyumi, AA, Reiser, J

  19. CD2AP, dendrin, and cathepsin L in the kidney. (Am J Pathol 2015)
    Sever, S, Reiser, J

  20. Pharmacological targeting of actin-dependent dynamin oligomerization ameliorates chronic kidney disease in diverse animal models. (Nat Med 2015)
    Schiffer, M, Teng, B, Gu, C, Shchedrina, VA, Kasaikina, M, Pham, VA, Hanke, N, Rong, S, Gueler, F, Schroder, P, Tossidou, I, Park, JK, Staggs, L, Haller, H, Erschow, S, Hilfiker-Kleiner, D, Wei, C, Chen, C, Tardi, N, Hakroush, S, Selig, MK, Vasilyev, A, Merscher, S, Reiser, J, Sever, S

  21. A Podocyte-Based Automated Screening Assay Identifies Protective Small Molecules. (J Am Soc Nephrol 2015)
    Lee, HW, Khan, SQ, Faridi, MH, Wei, C, Tardi, NJ, Altintas, MM, Elshabrawy, HA, Mangos, S, Quick, KL, Sever, S, Reiser, J, Gupta, V

  22. The grand challenge of nephrology. (Front Med (Lausanne) 2014)
    Trachtman, H, Benzing, T, Sever, S, Harris, RC, Reiser, J

  23. Regulation of dynamin oligomerization in cells: the role of dynamin-actin interactions and its GTPase activity. (Traffic 2014)
    Gu, C, Chang, J, Shchedrina, VA, Pham, VA, Hartwig, JH, Suphamungmee, W, Lehman, W, Hyman, BT, Bacskai, BJ, Sever, S

  24. Reduction of proteinuria through podocyte alkalinization. (J Biol Chem 2014)
    Altintas, MM, Moriwaki, K, Wei, C, Möller, CC, Flesche, J, Li, J, Yaddanapudi, S, Faridi, MH, Gödel, M, Huber, TB, Preston, RA, Jiang, JX, Kerjaschki, D, Sever, S, Reiser, J

  25. Signal transduction in podocytes--spotlight on receptor tyrosine kinases. (Nat Rev Nephrol 2014)
    Reiser, J, Sever, S, Faul, C

  26. Transient receptor potential channel 6 (TRPC6) protects podocytes during complement-mediated glomerular disease. (J Biol Chem 2013)
    Kistler, AD, Singh, G, Altintas, MM, Yu, H, Fernandez, IC, Gu, C, Wilson, C, Srivastava, SK, Dietrich, A, Walz, K, Kerjaschki, D, Ruiz, P, Dryer, S, Sever, S, Dinda, AK, Faul, C, Reiser, J

  27. Dynamin rings: not just for fission. (Traffic 2013)
    Sever, S, Chang, J, Gu, C

  28. Is there clinical value in measuring suPAR levels in FSGS? (Clin J Am Soc Nephrol 2013)
    Sever, S, Trachtman, H, Wei, C, Reiser, J

  29. Podocyte biology and pathogenesis of kidney disease. (Annu Rev Med 2013)
    Reiser, J, Sever, S

  30. CD2AP in mouse and human podocytes controls a proteolytic program that regulates cytoskeletal structure and cellular survival. (J Clin Invest 2011)
    Yaddanapudi, S, Altintas, MM, Kistler, AD, Fernandez, I, Möller, CC, Wei, C, Peev, V, Flesche, JB, Forst, AL, Li, J, Patrakka, J, Xiao, Z, Grahammer, F, Schiffer, M, Lohmüller, T, Reinheckel, T, Gu, C, Huber, TB, Ju, W, Bitzer, M, Rastaldi, MP, Ruiz, P, Tryggvason, K, Shaw, AS, Faul, C, Sever, S, Reiser, J

  31. Direct dynamin-actin interactions regulate the actin cytoskeleton. (EMBO J 2010)
    Gu, C, Yaddanapudi, S, Weins, A, Osborn, T, Reiser, J, Pollak, M, Hartwig, J, Sever, S

  32. Nucleoside diphosphate kinase Nm23-H1 regulates chromosomal stability by activating the GTPase dynamin during cytokinesis. (Proc Natl Acad Sci U S A 2010)
    Conery, AR, Sever, S, Harlow, E

  33. Establishment of protein delivery systems targeting podocytes. (PLoS One 2010)
    Chiang, WC, Geel, TM, Altintas, MM, Sever, S, Ruiters, MH, Reiser, J

  34. Synaptotagmin-mediated vesicle fusion regulates cell migration. (Nat Immunol 2010)
    Colvin, RA, Means, TK, Diefenbach, TJ, Moita, LF, Friday, RP, Sever, S, Campanella, GS, Abrazinski, T, Manice, LA, Moita, C, Andrews, NW, Wu, D, Hacohen, N, Luster, AD

  35. Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease. (J Clin Invest 2007)
    Sever, S, Altintas, MM, Nankoe, SR, Möller, CC, Ko, D, Wei, C, Henderson, J, del Re, EC, Hsing, L, Erickson, A, Cohen, CD, Kretzler, M, Kerjaschki, D, Rudensky, A, Nikolic, B, Reiser, J

  36. Dynasore puts a new spin on dynamin: a surprising dual role during vesicle formation. (Trends Cell Biol 2006)
    Nankoe, SR, Sever, S

  37. Physical and functional connection between auxilin and dynamin during endocytosis. (EMBO J 2006)
    Sever, S, Skoch, J, Newmyer, S, Ramachandran, R, Ko, D, McKee, M, Bouley, R, Ausiello, D, Hyman, BT, Bacskai, BJ

  38. Assays and functional properties of auxilin-dynamin interactions. (Methods Enzymol 2005)
    Sever, S, Skoch, J, Bacskai, BJ, Newmyer, SL

  39. The low density lipoprotein receptor-related protein (LRP) is a novel beta-secretase (BACE1) substrate. (J Biol Chem 2005)
    von Arnim, CA, Kinoshita, A, Peltan, ID, Tangredi, MM, Herl, L, Lee, BM, Spoelgen, R, Hshieh, TT, Ranganathan, S, Battey, FD, Liu, CX, Bacskai, BJ, Sever, S, Irizarry, MC, Strickland, DK, Hyman, BT

  40. AP-2 makes room for rivals. (Dev Cell 2003)
    Sever, S

  41. Auxilin-dynamin interactions link the uncoating ATPase chaperone machinery with vesicle formation. (Dev Cell 2003)
    Newmyer, SL, Christensen, A, Sever, S

  42. Dynamin and endocytosis. (Curr Opin Cell Biol 2002)
    Sever, S

  43. Expression, purification, and functional assays for self-association of dynamin-1. (Methods Enzymol 2001)
    Damke, H, Muhlberg, AB, Sever, S, Sholly, S, Warnock, DE, Schmid, SL

  44. Garrotes, springs, ratchets, and whips: putting dynamin models to the test. (Traffic 2000)
    Sever, S, Damke, H, Schmid, SL

  45. Dynamin:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis. (J Cell Biol 2000)
    Sever, S, Damke, H, Schmid, SL

  46. Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis. (Nucleic Acids Res 1999)
    Ibba, M, Sever, S, Praetorius-Ibba, M, Söll, D

  47. Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. (Nature 1999)
    Sever, S, Muhlberg, AB, Schmid, SL

  48. Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme. (Proc Natl Acad Sci U S A 1996)
    Ibba, M, Hong, KW, Sherman, JM, Sever, S, Söll, D

  49. Escherichia coli tryptophanyl-tRNA synthetase mutants selected for tryptophan auxotrophy implicate the dimer interface in optimizing amino acid binding. (Biochemistry 1996)
    Sever, S, Rogers, K, Rogers, MJ, Carter, C Jr, Söll, D

  50. Substrate selection by aminoacyl-tRNA synthetases. (Nucleic Acids Symp Ser 1995)
    Ibba, M, Thomann, HU, Hong, KW, Sherman, JM, Weygand-Durasevic, I, Sever, S, Stange-Thomann, N, Praetorius, M, Söll, D

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Principal Investigator, Associate Professor of Medicine

Postdoctoral Research Fellow, The Scripps Research Institute

Ph.D. in Biochemistry, Zagreb University & Visiting graduate student, Yale University

M.S. in Molecular Biology, Zagreb University

B.S. in Molecular Biology, Zagreb University


Postdoctoral Research Fellow, Harvard Medical School and the Massachusetts General Hospital

Postdoctoral Research Fellow, Department of Life Science, Sookmyung Women’s University

Ph.D. in Biomedical Gerontology, Hallym University

M.S. in Biomedical Gerontology, Hallym University

B.S. in Microbiology, Hankuk University of Foreign Studies

Postdoctoral Research Fellow 

Postdoctoral Research Associate in Chemical Biology, State University of New York at Binghamton

Ph.D. in Chemistry, State University of New York at Binghamton

M.S. in Applied Microbiology, Vellore Institute of Technology University

B.S. in Biochemistry, Microbiology, and Botany, Bangalore University

Research Scientist

Research Scientist, Brandeis University, Rosenstiel Basic Medical Sciences Research Center

Research Associate, University of Pennsylvania

Postdoctoral Researcher, Boston University School of Medicine                                                                                 

Ph.D. in Biochemistry, Nencki Institute of Experimental Biology, Polish Academy of Sciences

M.S. in Organic Chemistry, Warsaw University of Technology

B. Eng. in Organic Chemistry, Warsaw University of Technology

Research Technician

B.S. in Molecular Biology and Biochemistry, and the College of Integrative Sciences, Wesleyan University

Research Technician

B.S. in Biology, College of Natural Sciences, University of Massachusetts Amherst


  • Post-Doctoral Fellows
  • Research Technicians
  • Visiting Scholars and Summer Students
Post-Doctoral Fellows


Postdoctoral Fellow at Dana Farber Cancer Institute

Postdoctoral Research Fellow, Tufts University

Ph.D. in Biochemistry, University of Nebraska-Lincoln

B.S./M.S. in Bioorganic Chemistry, Moscow State University


Scientist at BioVision

Postdoctoral Research Fellow, Brigham & Women’s Hospital

Postdoctoral Research Fellow, University of Nebraska-Lincoln

Ph.D. in Biochemistry, Moscow State University

M.S. in Chemistry, Moscow State University

B.S. in Chemistry, Moscow State University

MIROSLAV SEKULIC, M.D./PH.D. (2012-2013)

Assistant Professor, Department of Pathology, Case Western Reserve University School of Medicine, University Hospitals Cleveland Medical Center

Fellowship in Renal Pathology, Brigham And Women's Hospital

Research Fellowship in Fabry Disease, University Of Bergen

Residency in Anatomic and Clinical Pathology, University Of Minnesota Affiliated Hospitals

M.D. University of Belgrade School of Medicine'

M.A. in Medical Sciences, Boston University School of Medicine

B.S. in Physiology & Neurobiology, University of Connecticut


Senior Manager- Medical Affairs Training and Field Alignment at TESARO, inc.

Principal Scientist at Pfizer

Ph.D. in Pharmaceutical Sciences, University of Connecticut

B.S. in Pharmacy, Osmania University


UGC Assistant Professor at Pondicherry Central University

Senior Scientist at Vision Research Foundation

ELISABETTA DEL RE, PH.D. (2003-2005)

Assistant Professor of Psychiatry at Harvard Medical School

Research Technicians


Transitioning to Industry

M.S. in pharmaceutics, MCPHS University

B.S. in pharmaceutics, Wuhan Institute of Technology


Applying for Medical School

B.S. in Biology, Saint Michael's College


Research Associate II at The Broad Institute of MIT and Harvard

Research Technician at Dana Farber Cancer Institute

B.S. Smith College

VINCENT A. PHAM (2013-2015)

Research Associate at Massachusetts Institute of Technology

B.S. in Neuroscience, Brown University

EILEEN KAPPLES (2013-2015)

Went on to Medical School

B.S. in Biology, Georgetown University

JOANN CHANG (2011-2013)

Brown University Residence Program

Case Western Reserve School of Medicine

University of Michigan School of Law, J.D.

Cornell University, B.A.

AMANDA C. TAUS (2011-2013)

Tufts University School of Medicine

Smith College, B.A

DAVID KO (2005-2007)

UC Riverside Medical School

LAVAN KHANDAN (2005-2006)

Scientist, In Vivo Discovery at Editas Medicine

Ph.D. in Molecular, Cellular, and Developmental Biology, University of Colorado Boulder

SHARIF NANKOE (2004-2006)

Residency in Family Medicine and Community health at UMass Medical School

M.D. University of Vermont College of Medicine

THOMAS GILMORE (2003-2005)

Went on to Medical School


Associate Professor at Anna Maria College

Assistant Professor at CUNY York College

Postdoctoral Researcher at the US Geological Survey

Ph.D. in Molecular and Cellular Biology, University of Massachusetts, Amherst

Visiting Scholars and Summer Students


Summer Student (Tufts University)


Summer Student (Harvard University)


Summer Student (University of Virginia)


Visiting Scholar (Rush University)


Visiting Scholar (University of São Paulo)


2009 Summer Student (University of Connecticut)


Summer Student (Williams College)


Summer Student (Brown University)


We are hiring! See below for available positions.


If you are a recent Ph.D. or M.D. Ph.D., are highly motivated, have a background in modern biology, biophysics (for single molecule work) or physiology, and a strong publication record, you are encouraged to apply for a post-doctoral position in the Sever lab.


The Sever lab accepts recent B.S. interested in pursuing carrier in science or medicine. The successful applicant is required to have a Bachelor's degree in Molecular Biology, Biochemistry, Cell Biology, Neurobiology, Chemistry, or a related field.  Some previous lab experience with molecular biology or chemistry is preferred, although all necessary techniques will be taught.

To Apply

Interested candidates should send a cover letter, resume, and a list of three references to Prof. Sanja Sever, Ph.D. (


Celebrating Ben's successful completion of the Harvard Summer Research Program in Kidney Medicine July 2019

Left to Right: Kamalika, Olivia, Sanja, Changkyu, Bradley, Agnieszka, Ben

The Sever Lab celebrating MGH being voted #1 best hospital in U.S. News and World Reports

Left to right: Changkyu, Garrett, Vincent, Eileen

By the water near our lab in Charlestown

Left to right: Changkyu, Eileen, Vincent, Marina, Garrett, Sanja

Lunch at Pier 6

Left to right: Marina, Changkyu, Vincent, Eileen, Garrett

Left to right: Miro, Changkyu, Amanda, Joann, Marina, Valentina, Sanja


Left to Right: Monica, Garret, Kamalika, Sanja, Sophia, Agnieszka, and Changkyu

Lab members and their significant others on the Brookline roof top 



Room 8205

149 13th Street, 

Charlestown, MA



+1 (617) 724 8922



By Public Transportation

From the MBTA Green Line, go to North Station. Here, you may board the free MGH/Partners shuttle bus (located at the intersection of Causeway Street and Haverhill Street) to the Charlestown Navy Yard, MGH East Research Building 149. The Sever Lab is on the 8th floor. The shuttle goes every 15 minutes during working hours (less often on weekends and holidays). 

From the MBTA Red Line, go to Charles/MGH. Here you may board the free MGH/Partners shuttle bus to the Charlestown Navy Yard, MGH East Research Building 149. The bus stops behind the MGH Jackson building and on Staniford St. behind the Whole Foods. The Sever Lab is on the 8th floor. The shuttle goes every 15 minutes during working hours (less often on weekends and holidays).

By Car from Storrow Drive

At the end of Storrow Drive, just beyond the MGH Main Campus, take a left onto the McGrath-O'Brien Highway. The Museum of Science will be on your left. At the first set of lights, proceed right onto the Gilmore Bridge, then at the next lights take a right onto Rutherford Avenue. Turn left at the second lights onto Chelsea Street. The Navy Yard and the U.S.S. Constitution will be on your right. Continue on Chelsea Street through three sets of traffic lights (about 1 mile). At the fourth set of lights take a right and the MGH East Navy Yard Research Building (Bldg. 149) will be one block away on the right. Take the first left to the MGH Parking Garage, which is connected to the Research Building by overhead walkways.

By Car from the Mass. Turnpike (90) and Route 93 North

Take I-90 to Route 93 North through downtown Boston and over the Zakim/Bunker Hill Bridge. Take the Sullivan Square exit. Go right at the bottom of the ramp and take the second exit off the Sullivan Square rotary towards Charlestown (keep Schrafft building on your left). At the first intersection, take a left onto Medford Street. At the end of Medford Street, take a left and an immediate right into the Navy Yard. The MGH East Navy Yard Research Building (Bldg. 149) will be one block away on your right. Take the first left to the Parking Garage, which is connected to the Research Building by overhead walkways.

Once you have arrived please call us at (617) 724-8922. You will have to check in with Security before we can escort you to the lab, so please bring your driver’s license or other government-issued identification.