Faculty mentor/PI email address
strichra@rowan.edu
Keywords
Cyclin C (CCNC), Programmed cell death (PCD), Mitochondrial fragmentation, Oxidative stress, Yeast model system
Date of Presentation
5-6-2026 12:00 AM
Poster Abstract
Background: Programmed cell death (PCD) is a tightly regulated process that maintains tissue homeostasis and eliminates damaged, infected, or malignant cells. A key regulator of this process is Cyclin C (CCNC), which functions as a component of the mediator complex to regulate gene transcription. During cellular stress, CCNC translocates from the nucleus to the mitochondria, where it associates with Dnm1 to promote mitochondrial fragmentation and apoptosis.
Objective: This study aimed to unravel conservation of CCNC’s function between yeast and humans by investigating whether human CCNC can induce apoptosis in yeast and whether it does so through interaction with the same molecular machinery.
Methods: Yeast lacking the endogenous Cyclin C gene (cnc1Δ) were transformed with a plasmid encoding human CCNC fused to EGFP reporter. To evaluate the role of CCNC–Dnm1 interaction in PCD, a double substitution mutation (ND→AA) was introduced within a predicted DRP1-binding domain. CCNC localization was assessed by fluorescence microscopy, and cell viability was evaluated under basal conditions and following exposure to cumene hydroperoxide (CHP).
Results: CCNC-GFP transformed yeast exhibited nuclear localization of human CCNC under basal conditions and translocation to the mitochondria following oxidative stress. This was accompanied by loss of cell viability in exposure to stress, indicating that human CCNC can induce PCD in yeast. Furthermore, disruption of the CCNC-Dnm1 interaction rendered cells resistant to death, suggesting that CCNC-mediated PCD is dependent on its interaction with Dnm1 and proceeds through a conserved molecular pathway.
Discussion: These findings provide evidence for the functional conservation of Cyclin C between yeast and humans, highlighting its evolutionary importance in regulating PCD and its role as a key determinant of cellular fate in response to environmental stress.
Disciplines
Bacteria | Cell Biology | Medicine and Health Sciences
Included in
A Conserved Role for Cyclin C in Regulated Cell Death Across Yeast and Humans
Background: Programmed cell death (PCD) is a tightly regulated process that maintains tissue homeostasis and eliminates damaged, infected, or malignant cells. A key regulator of this process is Cyclin C (CCNC), which functions as a component of the mediator complex to regulate gene transcription. During cellular stress, CCNC translocates from the nucleus to the mitochondria, where it associates with Dnm1 to promote mitochondrial fragmentation and apoptosis.
Objective: This study aimed to unravel conservation of CCNC’s function between yeast and humans by investigating whether human CCNC can induce apoptosis in yeast and whether it does so through interaction with the same molecular machinery.
Methods: Yeast lacking the endogenous Cyclin C gene (cnc1Δ) were transformed with a plasmid encoding human CCNC fused to EGFP reporter. To evaluate the role of CCNC–Dnm1 interaction in PCD, a double substitution mutation (ND→AA) was introduced within a predicted DRP1-binding domain. CCNC localization was assessed by fluorescence microscopy, and cell viability was evaluated under basal conditions and following exposure to cumene hydroperoxide (CHP).
Results: CCNC-GFP transformed yeast exhibited nuclear localization of human CCNC under basal conditions and translocation to the mitochondria following oxidative stress. This was accompanied by loss of cell viability in exposure to stress, indicating that human CCNC can induce PCD in yeast. Furthermore, disruption of the CCNC-Dnm1 interaction rendered cells resistant to death, suggesting that CCNC-mediated PCD is dependent on its interaction with Dnm1 and proceeds through a conserved molecular pathway.
Discussion: These findings provide evidence for the functional conservation of Cyclin C between yeast and humans, highlighting its evolutionary importance in regulating PCD and its role as a key determinant of cellular fate in response to environmental stress.