Brian David Dynlacht | |
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Born | |
Nationality | American |
Alma mater | Yale University University of California, Berkeley |
Known for | Discovery of CP110 Identification of USP33 |
Awards |
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Scientific career | |
Fields | Biochemistry |
Institutions | New York University Grossman School of Medicine |
Doctoral advisor | Robert Tjian |
Doctoral students | Nathan H. Lents |
Brian David Dynlacht (born September 3, 1965), is an American biochemist and professor in the department of pathology of New York University Grossman School of Medicine at NYU Langone Health. [1] Before moving his lab to New York University, he was an associate professor in the department of molecular and cellular biology at Harvard University. In 2002, while researching at the Harvard University, Dynlacht reported the discovery of CP110, [2] which is now thought to be at the center of a molecular switch governing the centriole to ciliary transition in mammalian cells. [3] His lab identified the first centriolar deubiquitinating enzyme, USP33, whose expression regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110, and thus regulates the centrosome duplication. [4] [ jargon ]
Brian David Dynlacht is the middle child of three children born to Sigmund (Zdzislaw) Dynlacht of Warsaw, Poland and Janice Deutsch of Brooklyn, New York. Dynlacht's father was orphaned during WWII and was a child survivor of the Holocaust. [5] [6] Dynlacht earned a Bachelor of Science in 1987 from Yale University, where he first conducted research under the mentorship of Paul Howard-Flanders. He was awarded a PhD in biochemistry in 1992 from the University of California at Berkeley. In 1991, as a graduate student with Robert Tjian, Dynlacht and Timothy Hoey reported for the first time the major protein components of TFIID. [7] [ when? ] Dynlacht carried out postdoctoral studies with Ed Harlow at the Massachusetts General Hospital, where he definitively proved for the first time, in vitro using purified proteins, the biochemical mechanism through which transcription can be directly repressed by the Rb tumor suppressor protein. This study also provided the first example of an in vitro transcription system that responds to regulatory events acting upstream of the binding of a transactivator. [8]
Dynlacht was appointed to the position of assistant professor in the department of molecular and cellular biology at Harvard University in 1995 and then associate professor in 1999. He is currently a professor in pathology in the Laura and Isaac Perlmutter Cancer Center of the New York University School of Medicine. [5] [6] At Harvard University, Dynlacht’s research was recognized by a Presidential Early Career Award for Scientists and Engineers in 1998. He has also received numerous career awards including Kenneth G. and Elaine A. Langone Damon Runyon Scholar Award (1996), Pew Scholar in the Biomedical Sciences (1998) and the Irma T. Hirchl Trust Career Award (2005).
Nathan H. Lents, postdoctoral fellow, scientist and author.
In cell biology, the centrosome is an organelle that serves as the main microtubule organizing center (MTOC) of the animal cell, as well as a regulator of cell-cycle progression. The centrosome provides structure for the cell. The centrosome is thought to have evolved only in the metazoan lineage of eukaryotic cells. Fungi and plants lack centrosomes and therefore use other structures to organize their microtubules. Although the centrosome has a key role in efficient mitosis in animal cells, it is not essential in certain fly and flatworm species.
A basal body is a protein structure found at the base of a eukaryotic undulipodium. The basal body was named by Theodor Wilhelm Engelmann in 1880. It is formed from a centriole and several additional protein structures, and is, essentially, a modified centriole. The basal body serves as a nucleation site for the growth of the axoneme microtubules. Centrioles, from which basal bodies are derived, act as anchoring sites for proteins that in turn anchor microtubules, and are known as the microtubule organizing center (MTOC). These microtubules provide structure and facilitate movement of vesicles and organelles within many eukaryotic cells.
Robert G. Roeder is an American biochemist. He is known as a pioneer scientist in eukaryotic transcription. He discovered three distinct nuclear RNA polymerases in 1969 and characterized many proteins involved in the regulation of transcription, including basic transcription factors and the first mammalian gene-specific activator over five decades of research. He is the recipient of the Gairdner Foundation International Award in 2000, the Albert Lasker Award for Basic Medical Research in 2003, and the Kyoto Prize in 2021. He currently serves as Arnold and Mabel Beckman Professor and Head of the Laboratory of Biochemical and Molecular Biology at The Rockefeller University.
Transcription factor II D (TFIID) is one of several general transcription factors that make up the RNA polymerase II preinitiation complex. RNA polymerase II holoenzyme is a form of eukaryotic RNA polymerase II that is recruited to the promoters of protein-coding genes in living cells. It consists of RNA polymerase II, a subset of general transcription factors, and regulatory proteins known as SRB proteins. Before the start of transcription, the transcription Factor II D (TFIID) complex binds to the core promoter DNA of the gene through specific recognition of promoter sequence motifs, including the TATA box, Initiator, Downstream Promoter, Motif Ten, or Downstream Regulatory elements.
Cyclin E is a member of the cyclin family.
Nucleophosmin (NPM), also known as nucleolar phosphoprotein B23 or numatrin, is a protein that in humans is encoded by the NPM1 gene.
Serine/threonine-protein kinase PLK1, also known as polo-like kinase 1 (PLK-1) or serine/threonine-protein kinase 13 (STPK13), is an enzyme that in humans is encoded by the PLK1 gene.
Transcription factor E2F3 is a protein that in humans is encoded by the E2F3 gene.
Mitochondrial transcription factor A, abbreviated as TFAM or mtTFA, is a protein that in humans is encoded by the TFAM gene.
Activating transcription factor 5, also known as ATF5, is a protein that, in humans, is encoded by the ATF5 gene.
Afadin- and alpha-actinin-binding protein is a protein that in humans is encoded by the SSX2IP gene. It has been shown that it functions together with WDR8 in centrosome maturation, ensuring proper spindle length and orientation. The SSX2IP-WDR8 complex additionally promotes ciliary vesicle docking during ciliogenesis.
Centrosome-associated protein CEP250 is a protein that in humans is encoded by the CEP250 gene. This gene encodes a core centrosomal protein required for centriole-centriole cohesion during interphase of the cell cycle. The encoded protein dissociates from the centrosomes when parental centrioles separate at the beginning of mitosis. The protein associates with and is phosphorylated by NIMA-related kinase 2, which is also associated with the centrosome. Furthermore, CEP135 is also required for the centriolar localization of CEP250.
G2/mitotic-specific cyclin-F is a protein that in humans is encoded by the CCNF gene.
Centriolar coiled-coil protein of 110 kDa also known as centrosomal protein of 110 kDa or CP110 is a protein that in humans is encoded by the CCP110 gene. It is a cell cycle-dependent CDK substrate and regulates centrosome duplication. CP110 suppresses a cilia assembly program.
Robert Tjian is a Hong Kong-born American biochemist best known for his work on eukaryotic transcription. He is currently professor of biochemistry and molecular biology at the University of California, Berkeley and an Investigator of the Howard Hughes Medical Institute (HHMI). On April 1, 2009, Tjian became the President of HHMI. On August 4, 2015, he announced that he would step down as President at the end of 2016.
Mitochondrial biogenesis is the process by which cells increase mitochondrial numbers. It was first described by John Holloszy in the 1960s, when it was discovered that physical endurance training induced higher mitochondrial content levels, leading to greater glucose uptake by muscles. Mitochondrial biogenesis is activated by numerous different signals during times of cellular stress or in response to environmental stimuli, such as aerobic exercise.
Lewis C. Cantley is an American cell biologist and biochemist who has made significant advances to the understanding of cancer metabolism. Among his most notable contributions are the discovery and study of the enzyme PI-3-kinase, now known to be important to understanding cancer and diabetes mellitus. He is currently Meyer Director and Professor of Cancer Biology at the Sandra and Edward Meyer Cancer Center at Weill Cornell Medicine in New York City. He was formerly a professor in the Departments of Systems Biology and Medicine at Harvard Medical School, and the Director of Cancer Research at the Beth Israel Deaconess Medical Center, in Boston, Massachusetts. In 2016, he was elected Chairman of the Board for the Hope Funds for Cancer Research.
Centrosomal protein of 192 kDa, also known as Cep192, is a protein that in humans is encoded by the CEP192 gene. It is the homolog of the C. elegans and D. melanogaster gene SPD-2.
Spindle assembly abnormal protein 6 homolog (SAS-6) is a protein that in humans is encoded by the SASS6 gene.
Sharon Tooze, FMedSci is an American cell biologist who has made significant contributions to the field of autophagy. She is a senior scientist at the Francis Crick Institute and was awarded European Molecular Biology Organization (EMBO) membership in 2010.