Phillip B. Carpenter, PhD
Professor
Department of Biochemistry and Molecular Biology
McGovern Medical School
UTHealth Houston
Email: [email protected]
Phone: 713-500-6032
Educational Philosophy
I love teaching and truly believe that it is a performing and creative art. This means that just “knowing the material” is only a starting point. Delivering the material is what makes the difference and what makes the learners remember the topic. We have developed some innovative strategies to engage learners through active learning. For this we created a pedagogy by merging the flipped classroom model with think-pair-share. In this model, students watch pre-class videos and then come to class to engage in individual and peer to peer learning using the Poll Everywhere system. Our project was recently published in Medical Education: Improved Performance in and Preference for Using Think-Pair-Share in a Flipped Classroom Med Educ. 2020 May;54(5):449-450.
As I have taught MCAT instruction for over 10 years, I have a strong understanding what concepts require mastery at the undergraduate level versus the medical school level. Such experience enables me to be a positive contributor to the thoughts and development of the 2015 New Curriculum currently in creation.
Area of Expertise
Medical education
Faculty development
Development of active learning pedagogy
Education
PhD
University of Illinois
Postdoctoral Fellow
California Technical Institute
Research
DNA repair, chromatin regulation
Epigenetics and the NSD family in development and disease
Our lab has been traditionally interested in the cellular response to DNA damage and more recently interested in the understanding the role of the nuclear receptor SET domain containing family, or “NSD” family in biological pathways that are relevant for health and disease. NSD proteins are very clinically relevant and have been found to be perturbed in various diseases including neuroblastoma, glioma, breast and prostate cancer. In fact, a recent, epigenetic gene expression profiling study identified a candidate gene signature that includes NSD1 (DNMT3A, MBD4,MLL2, MLL3, NSD1, and SRCAP), that can significantly discriminated nonmalignant from prostate tumor tissue (P = 0.0063) in an independent cohort. Translocations in NSD1 are well established to be causal for the generation of acute myeloid leukemia and overexpression of NSD2 has been implicated in multiple myeloma. Moreover, haploinsufficiency in NSD1 is the major, if not only, cause of Sotos syndrome, a developmental abnormality marked by bone overgrowth, craniofacial defects, learning disabilities, and a spectrum of other disorders. Translocations at chromosome 4 can lead to defects in NSD2 and the developmental disorder known as Wolf Hirschhorn syndrome. Additional pathologies caused by perturbations in the NSD family have also been noted.
Although highly relevant to human health and disease, surprisingly only a few details have been published regarding the mechanism of NSD family action. NSD family members are large proteins that possess numerous domains, many of which have been implicated in chromatin biology. Notably, NSD family members possess a catalytic SET domain that has been shown to methylate histone side chains, particularly lysine 36 of histone H3 (H3-K36). Additional studies have revealed that in response to tumor necrosis factor α or interleukin-1, NSD1 is essential in mammals and methylates two lysine residues in the p65 subunit of NF-κB, a critical factor in numerous cell systems. Thus, NSD1, and by, extension additional family members, target non-histone proteins. The nature of these substrates and the pathways that they lie upon promise to be important in any of the numerous pathologies linked to the NSD family.
Our lab has created various research tools to understand the role of the NSD family in development and disease. Using a recently described “FLAG knock-in” strategy, we determined the global targets of NSD1. We found that NSD1 dependent methylation of H3-K36 recruits RNA Polymerase II to various promoter elements including that of bone morphogenic protein 4 (BMP4). We are currently examining the relationship between H3-K36 methylation and RNA Pol II activity.