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Mariusz Karbowski, PhD

Academic Title:

Associate Professor

Primary Appointment:

Biochemistry and Molecular Biology


Biomedical Engineering & Tech, School of Pharmacy, Room S542

Phone (Primary):



Dr. Karbowski received his M.S. degree in 1994 from the Department of Biochemistry of Adam Mickiewicz University (Poznan, Poland). For his graduate studies he moved to Nagoya, Japan.  He received Ph.D. degree from the Department of Molecular Pathology, Nagoya University School of Medicine (Nagoya, Japan) in 2001, where, under mentorship of Dr. Takashi Wakabayashi, he studied mitochondrial function in alcohol- and drug-induced liver pathologies. He trained as a postdoctoral fellow at the National Institute of Neurological Disease and Stroke, National Institutes of Health (Bethesda, MD, USA) under guidance of Dr. Richard J Youle.

During his postdoctoral training, he studied regulation of mitochondrial-steps in apoptosis and the role of mitochondrial membrane dynamics in cell life and death. He joined the University of Maryland faculty in 2007 as a tenure-track assistant professor and was promoted to the rank of associate professor in 2014.

Dr. Karbowski is an author of ~70 publications, in peer-reviewed scientific journals, currently with ~6000 citations by others. 

Research/Clinical Keywords

mitochondrial membrane dynamics, impact of ubiquitin and proteasome-dependent control of mitochondria

Highlighted Publications

Cherok E, Xu S, Li S, Das S, Meltzer WA, Zalzman M, Wang C, Karbowski M. Novel regulatory roles of Mff and Drp1 in E3 ubiquitin ligase MARCH5-dependent degradation of MiD49 and Mcl1 and control of mitochondrial dynamics; Mol. Biol. Cell. 2017; 28(3):396-410

Xu S, Cherok E, Das S, Li S, Roelofs BA, Ge SX, Polster BM, Boyman L, Lederer WJ, Wang C, Karbowski M. Mitochondrial E3 ubiquitin ligase MARCH5 controls mitochondrial fission and cell sensitivity to stress-induced apoptosis through regulation of MiD49 protein; Mol. Biol. Cell. 2016; 27(2):349-59

Li S, Xu S, Roelofs BA, Boyman L, Lederer WJ, Sesaki H, Karbowski M. Transient assembly of F-actin on the outer mitochondrial membrane contributes to mitochondrial fission; J. Cell Biol. 2015; 208:109-123. (“Actin is good at long division”, an editorial on the article was published in J. Cell Biol.2015 208:2)

Roelofs B, Cleland MM, Karbowski M. Visualization and quantification of mitochondrial fusion. Methods Enzymol. 2014; 547:57-73.

Karbowski M and Youle RJ Regulating Mitochondrial Outer Membrane Proteins by Ubiquitination and Proteasomal Degradation. (Review) Current Opinions in Cell Biology. 2011 23(4): 476-82.

Xu S, Peng G, Wang Y, Fang S, Karbowski M. The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover. Mol. Biol. Cell 2011, 22(3): 291-300.

Tanaka A, Cleland MC, Xu S, Narendra DP, Suen D-F, Karbowski M*, Youle R. Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J. Cell Biol. 2010, 191(7): 1367-80. *M. Karbowski is a co-corresponding author

Benard G, Neutzner A, Peng G, Wang C, Livak F, Youle RJ, Karbowski M. IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation. EMBO J. 2010, 29: 1458-71.

Karbowski M*, Norris K, Cleland M, Jeong SY, Youle RJ. Role of Bax and Bak in mitochondrial morphogenesis. Nature 2006, 443: 658-662 (“Cell biology: mitochondria shape up”, an editorial on the article was published in Nature 2006, 443:646-7). *M. Karbowski is a co-corresponding author.

Research Interests

Dr. Karbowski’s major scientific expertise and research achievements are as follows:

  1. revealing role of mitochondria in cellular homeostasis
  2. control of mitochondrial fusion and fission
  3. impact of ubiquitin and proteasome-dependent control of mitochondria
  4. development of novel tools to study mitochondrial function in living cells

His current research centers on:

  1. role of ubiquitin-dependent signaling in control of mitochondrial function
  2. reciprocal regulation of mitochondrial fusion and fission
  3. crosstalk between mitochondria and actin cytoskeleton