Brian David Dynlacht

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Brian David Dynlacht (born September 3, 1965 in Brooklyn, New York), 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 ]

Contents

Early life and education

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]

Career

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).

Notable trainees

Nathan H. Lents, postdoctoral fellow, scientist and author.

Related Research Articles

<span class="mw-page-title-main">Basal body</span> Protein structure found at the base of cilium or flagellum).

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.

<span class="mw-page-title-main">Robert G. Roeder</span> American biochemist

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.

<span class="mw-page-title-main">Cyclin E</span> Member of the cyclin family

Cyclin E is a member of the cyclin family.

<span class="mw-page-title-main">NPM1</span> Protein-coding gene in humans

Nucleophosmin (NPM), also known as nucleolar phosphoprotein B23 or numatrin, is a protein that in humans is encoded by the NPM1 gene.

<span class="mw-page-title-main">PLK1</span> Mammalian protein found in Homo sapiens

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.

<span class="mw-page-title-main">E2F3</span> Protein-coding gene in the species Homo sapiens

Transcription factor E2F3 is a protein that in humans is encoded by the E2F3 gene.

<span class="mw-page-title-main">TFAM</span> Protein-coding gene in the species Homo sapiens

Mitochondrial transcription factor A, abbreviated as TFAM or mtTFA, is a protein that in humans is encoded by the TFAM gene.

<span class="mw-page-title-main">ATF5</span> Protein-coding gene in the species Homo sapiens

Activating transcription factor 5, also known as ATF5, is a protein that, in humans, is encoded by the ATF5 gene.

<span class="mw-page-title-main">SSX2IP</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">TFAP2A</span> Protein-coding gene in the species Homo sapiens

Transcription factor AP-2 alpha, also known as TFAP2A, is a protein that in humans is encoded by the TFAP2A gene.

<span class="mw-page-title-main">CEP250</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">USP20</span> Protein-coding gene in the species Homo sapiens

Ubiquitin carboxyl-terminal hydrolase 20 is an enzyme that in humans is encoded by the USP20 gene.

<span class="mw-page-title-main">CCP110</span> Protein-coding gene in the species Homo sapiens

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.

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<span class="mw-page-title-main">CEP192</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">SASS6</span> Protein-coding gene in the species Homo sapiens

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References

  1. "Brian D. Dynlacht".
  2. Chen Z, Indjeian VB, McManus M, Wang L, Dynlacht BD (September 2002). "CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells". Dev. Cell. 3 (3): 339–50. doi: 10.1016/S1534-5807(02)00258-7 . PMID   12361598.
  3. Spektor A, Tsang WY, Khoo D, Dynlacht BD (August 2007). "CP110 suppresses a cilia assembly program". Cell. 130 (4): 678–90. doi: 10.1016/j.cell.2007.06.027 . PMID   17719545. S2CID   17974875.
  4. Li, J.; d'Angiolella, V.; Seeley, E. S.; Kim, S.; Kobayashi, T.; Fu, W.; Campos, E. I.; Pagano, M.; Dynlacht, B. D. (2013). "USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110". Nature. 495 (7440): 255–259. Bibcode:2013Natur.495..255L. doi:10.1038/nature11941. PMC   3815529 . PMID   23486064.
  5. 1 2 Center for Oral History. "Brian D. Dynlacht". Science History Institute .
  6. 1 2 Van Benschoten, William (20 August 2004). Brian D. Dynlacht, Transcript of an Interview Conducted by William Van Benschoten at New York University New York City, New York on 19 and 20 August 2004 (PDF). Philadelphia, PA: Chemical Heritage Foundation.
  7. Dynlacht, Brian David; Hoey, Timothy; Tjian, Robert (Aug 1991). "Isolation of co-activators associated with the TATA-binding protein that mediate transcriptional activation". Cell. 66 (3): 563–576. doi:10.1016/0092-8674(81)90019-2. PMID   1907890. S2CID   5000858.
  8. Dynlacht BD, Flores O, Lees JA, Harlow E (August 1994). "Differential Regulation of E2F transactivation by cyclin/cdk2 complex". Genes & Development. 8 (15): 1172–86. doi: 10.1101/gad.8.15.1772 . PMID   7958856.

External list