Jason A. Mears

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   Jason A. Mears | Pathology | School of Medicine | Case Western Reserve University

   7 source claims · Reviewed Sep 9, 2026

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   Biographical context: Dr. Mears has a diverse scientific background that combines structural, biochemical and cellular methods to characterize functional relationships in macromolecular complexes.

   Dr. Mears has a diverse scientific background that combines structural, biochemical and cellular methods to characterize functional relationships in macromolecular complexes.

   Degree: PhD

   Jason A. Mears, PhD Email [contact withheld] Phone [contact withheld] Fax Number [contact withheld] Office Location: Wood Building W147 10900 Euclid Ave Cleveland, OH 44106-4965 Graduate Program Director, Department of Pharmacology, School of Medicine Professor, Department of Pharmacology, School of Medicine Associate Director, Training and Education, Case Comprehensive Cancer Center Member, Molecular Oncology Program, Case Comprehensive Cancer Center The central goal of research in the Mears Lab is to investigate proteins that regulate mitochondrial dynamics. Mitochondrial dynamics has recently come to the forefront as a therapeutic target in several diseases, including neurodegeneration, cancer, and aging. But the lack of insight into the regulation of the mitochondrial fission complex is a major limitation. To address this shortcoming, my lab has been at the leading edge of research that has characterized the functional roles of proteins in the mitochondrial fission complex. We have also provided novel mechanistic insight for this process by showing that this protein machinery actively constricts membranes to drive ensuing fission. From these studies, we have developed novel in vitro assays that we will use to identify the functional consequences of specific cellular perturbations that modify the fission machinery in human disease. Dr. Mears has a diverse scientific background that combines structural, biochemical and cellular methods to characterize functional relationships in macromolecular complexes. His studies as a post-doctoral fellow in the lab of Dr. Jenny Hinshaw at the NIH advanced our understanding of the basic mechanistic properties of dynamin mediated membrane remodeling. In his own lab, he has focused on the main regulator of mammalian mitochondrial fission, dynamin-related protein 1 (Drp1). While key attributes of the dynamin family are preserved in Drp1, several unique features have been identified. These differences highlight functional relationships within the larger protein family. In particular, the Mears lab has identified novel protein interactions that regulate Drp1 self-assembly and functional interactions with distinct partner proteins. The current research environment is optimally suited to address these fundamental questions about the mitochondrial fission complex using a variety of techniques, and regular interactions with mitochondrial, structural and cancer biologists continue to support our research interests. The over-arching goal is to resolve long-standing questions about key factors that alter mitochondrial dynamics, leading to organelle dysfunction in human pathologies. My research focuses on structural and functional studies to reveal the impact of mitochondrial dynamics on cell health and proliferation in human diseases, including cancer, neurodegeneration and cardiomyopathy. My areas include cryo-electron microscopy, biochemistry, computational biology, and cancer stem cell models. Jason A. Mears's Biography

   Identity: Jason A. Mears, PhD

   Jason A. Mears, PhD Email [contact withheld] Phone [contact withheld] Fax Number [contact withheld] Office Location: Wood Building W147 10900 Euclid Ave Cleveland, OH 44106-4965 Graduate Program Director, Department of Pharmacology, School of Medicine Professor, Department of Pharmacology, School of Medicine Associate Director, Training and Education, Case Comprehensive Cancer Center Member, Molecular Oncology Program, Case Comprehensive Cancer Center The central goal of research in the Mears Lab is to investigate proteins that regulate mitochondrial dynamics. Mitochondrial dynamics has recently come to the forefront as a therapeutic target in several diseases, including neurodegeneration, cancer, and aging. But the lack of insight into the regulation of the mitochondrial fission complex is a major limitation. To address this shortcoming, my lab has been at the leading edge of research that has characterized the functional roles of proteins in the mitochondrial fission complex. We have also provided novel mechanistic insight for this process by showing that this protein machinery actively constricts membranes to drive ensuing fission. From these studies, we have developed novel in vitro assays that we will use to identify the functional consequences of specific cellular perturbations that modify the fission machinery in human disease. Dr. Mears has a diverse scientific background that combines structural, biochemical and cellular methods to characterize functional relationships in macromolecular complexes. His studies as a post-doctoral fellow in the lab of Dr. Jenny Hinshaw at the NIH advanced our understanding of the basic mechanistic properties of dynamin mediated membrane remodeling. In his own lab, he has focused on the main regulator of mammalian mitochondrial fission, dynamin-related protein 1 (Drp1). While key attributes of the dynamin family are preserved in Drp1, several unique features have been identified. These differences highlight functional relationships within the larger protein family. In particular, the Mears lab has identified novel protein interactions that regulate Drp1 self-assembly and functional interactions with distinct partner proteins. The current research environment is optimally suited to address these fundamental questions about the mitochondrial fission complex using a variety of techniques, and regular interactions with mitochondrial, structural and cancer biologists continue to support our research interests. The over-arching goal is to resolve long-standing questions about key factors that alter mitochondrial dynamics, leading to organelle dysfunction in human pathologies. My research focuses on structural and functional studies to reveal the impact of mitochondrial dynamics on cell health and proliferation in human diseases, including cancer, neurodegeneration and cardiomyopathy. My areas include cryo-electron microscopy, biochemistry, computational biology, and cancer stem cell models. Jason A. Mears's Biography

   Professional role: Associate Director, Training and Education, Case Comprehensive Cancer Center

   Jason A. Mears, PhD Email [contact withheld] Phone [contact withheld] Fax Number [contact withheld] Office Location: Wood Building W147 10900 Euclid Ave Cleveland, OH 44106-4965 Graduate Program Director, Department of Pharmacology, School of Medicine Professor, Department of Pharmacology, School of Medicine Associate Director, Training and Education, Case Comprehensive Cancer Center Member, Molecular Oncology Program, Case Comprehensive Cancer Center The central goal of research in the Mears Lab is to investigate proteins that regulate mitochondrial dynamics. Mitochondrial dynamics has recently come to the forefront as a therapeutic target in several diseases, including neurodegeneration, cancer, and aging. But the lack of insight into the regulation of the mitochondrial fission complex is a major limitation. To address this shortcoming, my lab has been at the leading edge of research that has characterized the functional roles of proteins in the mitochondrial fission complex. We have also provided novel mechanistic insight for this process by showing that this protein machinery actively constricts membranes to drive ensuing fission. From these studies, we have developed novel in vitro assays that we will use to identify the functional consequences of specific cellular perturbations that modify the fission machinery in human disease. Dr. Mears has a diverse scientific background that combines structural, biochemical and cellular methods to characterize functional relationships in macromolecular complexes. His studies as a post-doctoral fellow in the lab of Dr. Jenny Hinshaw at the NIH advanced our understanding of the basic mechanistic properties of dynamin mediated membrane remodeling. In his own lab, he has focused on the main regulator of mammalian mitochondrial fission, dynamin-related protein 1 (Drp1). While key attributes of the dynamin family are preserved in Drp1, several unique features have been identified. These differences highlight functional relationships within the larger protein family. In particular, the Mears lab has identified novel protein interactions that regulate Drp1 self-assembly and functional interactions with distinct partner proteins. The current research environment is optimally suited to address these fundamental questions about the mitochondrial fission complex using a variety of techniques, and regular interactions with mitochondrial, structural and cancer biologists continue to support our research interests. The over-arching goal is to resolve long-standing questions about key factors that alter mitochondrial dynamics, leading to organelle dysfunction in human pathologies. My research focuses on structural and functional studies to reveal the impact of mitochondrial dynamics on cell health and proliferation in human diseases, including cancer, neurodegeneration and cardiomyopathy. My areas include cryo-electron microscopy, biochemistry, computational biology, and cancer stem cell models. Jason A. Mears's Biography

   Professional role: Graduate Program Director, Department of Pharmacology, School of Medicine

   Jason A. Mears, PhD Email [contact withheld] Phone [contact withheld] Fax Number [contact withheld] Office Location: Wood Building W147 10900 Euclid Ave Cleveland, OH 44106-4965 Graduate Program Director, Department of Pharmacology, School of Medicine Professor, Department of Pharmacology, School of Medicine Associate Director, Training and Education, Case Comprehensive Cancer Center Member, Molecular Oncology Program, Case Comprehensive Cancer Center The central goal of research in the Mears Lab is to investigate proteins that regulate mitochondrial dynamics. Mitochondrial dynamics has recently come to the forefront as a therapeutic target in several diseases, including neurodegeneration, cancer, and aging. But the lack of insight into the regulation of the mitochondrial fission complex is a major limitation. To address this shortcoming, my lab has been at the leading edge of research that has characterized the functional roles of proteins in the mitochondrial fission complex. We have also provided novel mechanistic insight for this process by showing that this protein machinery actively constricts membranes to drive ensuing fission. From these studies, we have developed novel in vitro assays that we will use to identify the functional consequences of specific cellular perturbations that modify the fission machinery in human disease. Dr. Mears has a diverse scientific background that combines structural, biochemical and cellular methods to characterize functional relationships in macromolecular complexes. His studies as a post-doctoral fellow in the lab of Dr. Jenny Hinshaw at the NIH advanced our understanding of the basic mechanistic properties of dynamin mediated membrane remodeling. In his own lab, he has focused on the main regulator of mammalian mitochondrial fission, dynamin-related protein 1 (Drp1). While key attributes of the dynamin family are preserved in Drp1, several unique features have been identified. These differences highlight functional relationships within the larger protein family. In particular, the Mears lab has identified novel protein interactions that regulate Drp1 self-assembly and functional interactions with distinct partner proteins. The current research environment is optimally suited to address these fundamental questions about the mitochondrial fission complex using a variety of techniques, and regular interactions with mitochondrial, structural and cancer biologists continue to support our research interests. The over-arching goal is to resolve long-standing questions about key factors that alter mitochondrial dynamics, leading to organelle dysfunction in human pathologies. My research focuses on structural and functional studies to reveal the impact of mitochondrial dynamics on cell health and proliferation in human diseases, including cancer, neurodegeneration and cardiomyopathy. My areas include cryo-electron microscopy, biochemistry, computational biology, and cancer stem cell models. Jason A. Mears's Biography

   Professional role: Professor, Department of Pharmacology, School of Medicine

   Jason A. Mears, PhD Email [contact withheld] Phone [contact withheld] Fax Number [contact withheld] Office Location: Wood Building W147 10900 Euclid Ave Cleveland, OH 44106-4965 Graduate Program Director, Department of Pharmacology, School of Medicine Professor, Department of Pharmacology, School of Medicine Associate Director, Training and Education, Case Comprehensive Cancer Center Member, Molecular Oncology Program, Case Comprehensive Cancer Center The central goal of research in the Mears Lab is to investigate proteins that regulate mitochondrial dynamics. Mitochondrial dynamics has recently come to the forefront as a therapeutic target in several diseases, including neurodegeneration, cancer, and aging. But the lack of insight into the regulation of the mitochondrial fission complex is a major limitation. To address this shortcoming, my lab has been at the leading edge of research that has characterized the functional roles of proteins in the mitochondrial fission complex. We have also provided novel mechanistic insight for this process by showing that this protein machinery actively constricts membranes to drive ensuing fission. From these studies, we have developed novel in vitro assays that we will use to identify the functional consequences of specific cellular perturbations that modify the fission machinery in human disease. Dr. Mears has a diverse scientific background that combines structural, biochemical and cellular methods to characterize functional relationships in macromolecular complexes. His studies as a post-doctoral fellow in the lab of Dr. Jenny Hinshaw at the NIH advanced our understanding of the basic mechanistic properties of dynamin mediated membrane remodeling. In his own lab, he has focused on the main regulator of mammalian mitochondrial fission, dynamin-related protein 1 (Drp1). While key attributes of the dynamin family are preserved in Drp1, several unique features have been identified. These differences highlight functional relationships within the larger protein family. In particular, the Mears lab has identified novel protein interactions that regulate Drp1 self-assembly and functional interactions with distinct partner proteins. The current research environment is optimally suited to address these fundamental questions about the mitochondrial fission complex using a variety of techniques, and regular interactions with mitochondrial, structural and cancer biologists continue to support our research interests. The over-arching goal is to resolve long-standing questions about key factors that alter mitochondrial dynamics, leading to organelle dysfunction in human pathologies. My research focuses on structural and functional studies to reveal the impact of mitochondrial dynamics on cell health and proliferation in human diseases, including cancer, neurodegeneration and cardiomyopathy. My areas include cryo-electron microscopy, biochemistry, computational biology, and cancer stem cell models. Jason A. Mears's Biography

   Professor, Department of Pharmacology, School of Medicine

   Research interests: My research focuses on structural and functional studies to reveal the impact of mitochondrial dynamics on cell health and proliferation in human diseases, including cancer, neurodegeneration and cardiomyopathy.

   My research focuses on structural and functional studies to reveal the impact of mitochondrial dynamics on cell health and proliferation in human diseases, including cancer, neurodegeneration and cardiomyopathy.