Gideon Dreyfuss

Last updated
Gideon Dreyfuss
Born
New York City, New York, United States
Education Hebrew University of Jerusalem (undergraduate),
Harvard University (PhD),
Massachusetts Institute of Technology (Post-doctoral)
Known forDiscovering and naming several hnRNP's and the proteins associated with SMN, for which loss of function is the primary cause of SMA,
Scientific career
Fields Biochemistry, Molecular Biology
Institutions University of Pennsylvania,
Howard Hughes Medical Institute,
National Academy of Sciences,
Northwestern University (formerly)
Thesis On cyclic AMP-dependent protein kinases  (1978)
Doctoral advisor Elkan Blout
Other academic advisors David Baltimore

Gideon Dreyfuss is an American biochemist, the Isaac Norris Professor of Biochemistry and Biophysics at the University of Pennsylvania School of Medicine, and an investigator of the Howard Hughes Medical Institute. He was elected to the National Academy of Sciences in 2012. [1]

Contents

Dreyfuss received his Ph.D. in biological chemistry in 1978 from Harvard University and is a fellow of the American Academy of Arts and Sciences.

Research

The Dreyfuss Lab is interested in various projects studying the function and biogenesis of non-coding RNA and the proteins that interact with RNA. A primary research goal of the lab is to elucidate the function of Survival of Motor Neuron protein, SMN, which assembles a heptameric ring of Sm proteins on U snRNAs to form snRNPs that are essential components of the splicesome. Moreover, loss of functional SMN is directly linked to spinal muscular atrophy, a debilitating neurodegenerative disease that is characterize by the eventual death of motor neurons and muscular wasting. The Dreyfuss Lab is conducting research to understand the role of SMN in SMA pathology and using high throughput screening to discover potential therapeutics. The lab also studies the dynamic mechanism of RNA splicing, the RNA-binding proteins that determine exonic specificity, and snRNAs, that are important regulators of splicing and mRNA maturation.

Genes or Gene Functions Discovered

See also

Related Research Articles

<span class="mw-page-title-main">Survival of motor neuron</span> Protein in animal cells

Survival of motor neuron or survival motor neuron (SMN) is a protein that in humans is encoded by the SMN1 and SMN2 genes.

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

rRNA 2'-O-methyltransferase fibrillarin is an enzyme that in humans is encoded by the FBL gene.

<span class="mw-page-title-main">Small nuclear ribonucleoprotein D1</span> Protein-coding gene in the species Homo sapiens

Small nuclear ribonucleoprotein Sm D1 is a protein that in humans is encoded by the SNRPD1 gene.

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

Small nuclear ribonucleoprotein-associated proteins B and B' is a protein that in humans is encoded by the SNRPB gene.

<span class="mw-page-title-main">Small nuclear ribonucleoprotein D2</span> Protein-coding gene in the species Homo sapiens

Small nuclear ribonucleoprotein Sm D2 is a protein that in humans is encoded by the SNRPD2 gene. It belongs to the small nuclear ribonucleoprotein core protein family, and is required for pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis. Alternative splicing occurs at this locus and two transcript variants encoding the same protein have been identified.

<span class="mw-page-title-main">Small nuclear ribonucleoprotein polypeptide E</span> Protein-coding gene in the species Homo sapiens

Small nuclear ribonucleoprotein E is a protein that in humans is encoded by the SNRPE gene.

<span class="mw-page-title-main">SNRPD3</span> Protein-coding gene in the species Homo sapiens

Small nuclear ribonucleoprotein Sm D3 is a protein that in humans is encoded by the SNRPD3 gene.

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

Synaptotagmin-binding, cytoplasmic RNA-interacting protein (SYNCRIP), also known as heterogeneous nuclear ribonucleoprotein (hnRNP) Q or NS1-associated protein-1 (NSAP-1), is a protein that in humans is encoded by the SYNCRIP gene. As the name implies, SYNCRIP is localized predominantly in the cytoplasm. It is evolutionarily conserved across eukaryotes and participates in several cellular and disease pathways, especially in neuronal and muscular development. In humans, there are three isoforms, all of which are associated in vitro with pre-mRNAs, mRNA splicing intermediates, and mature mRNA-protein complexes, including mRNA turnover.

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

Heterogeneous nuclear ribonucleoprotein G is a protein that in humans is encoded by the RBMX gene.

<span class="mw-page-title-main">Gem-associated protein 2</span> Protein-coding gene in the species Homo sapiens

Gem-associated protein 2 (GEMIN2), also called survival of motor neuron protein-interacting protein 1 (SIP1), is a protein that in humans is encoded by the GEMIN2 gene.

<span class="mw-page-title-main">DDX20</span> Protein-coding gene in the species Homo sapiens

Probable ATP-dependent RNA helicase DDX20, also known as DEAD-box helicase 20 and gem-associated protein 3 (GEMIN3), is an enzyme that in humans is encoded by the DDX20 gene.

<span class="mw-page-title-main">Small nuclear ribonucleoprotein polypeptide F</span> Protein-coding gene in the species Homo sapiens

Small nuclear ribonucleoprotein F is a protein that in humans is encoded by the SNRPF gene.

<span class="mw-page-title-main">SNRPB2</span> Protein-coding gene in the species Homo sapiens

U2 small nuclear ribonucleoprotein B is a protein that in humans is encoded by the SNRPB2 gene.

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

Small nuclear ribonucleoprotein G is a protein that in humans is encoded by the SNRPG gene.

<span class="mw-page-title-main">Small nuclear ribonucleoprotein polypeptide C</span> Protein-coding gene in the species Homo sapiens

U1 small nuclear ribonucleoprotein C is a protein that in humans is encoded by the SNRPC gene.

<span class="mw-page-title-main">Gem-associated protein 6</span> Protein-coding gene in the species Homo sapiens

Gem-associated protein 6 is a protein that in humans is encoded by the GEMIN6 gene. The gem-associated proteins are those found in the gems of Cajal bodies.

<span class="mw-page-title-main">LSM2</span> Protein-coding gene in the species Homo sapiens

U6 snRNA-associated Sm-like protein LSm2 is a protein that in humans is encoded by the LSM2 gene.

<span class="mw-page-title-main">Gem-associated protein 4</span> Protein-coding gene in the species Homo sapiens

Gem-associated protein 4 is a protein that in humans is encoded by the GEMIN4 gene.

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

Heterogeneous nuclear ribonucleoprotein R is a protein that in humans is encoded by the HNRNPR gene.

<span class="mw-page-title-main">Gem-associated protein 5</span> Protein-coding gene in the species Homo sapiens

Gem-associated protein 5 is a protein that in humans is encoded by the GEMIN5 gene.

References

  1. ↑ Penn Medicine Announcement, , May 3, 2012
  2. ↑ Chan, C. C.; Dostie, J.; Diem, M. D.; Feng, W.; Mann, M.; Rappsilber, J.; Dreyfuss, G. (2004). "EIF4A3 is a novel component of the exon junction complex". RNA. 10 (2): 200–209. doi:10.1261/rna.5230104. PMC   1370532 . PMID   14730019.
  3. ↑ Siomi, M. C.; Siomi, H.; Sauer, W. H.; Srinivasan, S.; Nussbaum, R. L.; Dreyfuss, G. (1995). "FXR1, an autosomal homolog of the fragile X mental retardation gene". The EMBO Journal. 14 (11): 2401–2408. doi:10.1002/j.1460-2075.1995.tb07237.x. PMC   398353 . PMID   7781595.
  4. ↑ Zhang, Y.; O'Connor, J. P.; Siomi, M. C.; Srinivasan, S.; Dutra, A.; Nussbaum, R. L.; Dreyfuss, G. (1995). "The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2". The EMBO Journal. 14 (21): 5358–5366. doi:10.1002/j.1460-2075.1995.tb00220.x. PMC   394645 . PMID   7489725.
  5. ↑ Liu, Q.; Fischer, U.; Wang, F.; Dreyfuss, G. (1997). "The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins". Cell. 90 (6): 1013–1021. doi: 10.1016/S0092-8674(00)80367-0 . PMID   9323129. S2CID   10855404.
  6. ↑ Charroux, B.; Pellizzoni, L.; Perkinson, R. A.; Shevchenko, A.; Mann, M.; Dreyfuss, G. (1999). "Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems". The Journal of Cell Biology. 147 (6): 1181–1194. doi:10.1083/jcb.147.6.1181. PMC   2168095 . PMID   10601333.
  7. ↑ Charroux, B.; Pellizzoni, L.; Perkinson, R. A.; Yong, J.; Shevchenko, A.; Mann, M.; Dreyfuss, G. (2000). "Gemin4. A novel component of the SMN complex that is found in both gems and nucleoli". The Journal of Cell Biology. 148 (6): 1177–1186. doi:10.1083/jcb.148.6.1177. PMC   2174312 . PMID   10725331.
  8. ↑ Gubitz, A. K.; Mourelatos, Z.; Abel, L.; Rappsilber, J.; Mann, M.; Dreyfuss, G. (2001). "Gemin5, a Novel WD Repeat Protein Component of the SMN Complex That Binds Sm Proteins". Journal of Biological Chemistry. 277 (7): 5631–5636. doi: 10.1074/jbc.M109448200 . PMID   11714716.
  9. ↑ Pellizzoni, L.; Baccon, J.; Rappsilber, J.; Mann, M.; Dreyfuss, G. (2001). "Purification of Native Survival of Motor Neurons Complexes and Identification of Gemin6 as a Novel Component". Journal of Biological Chemistry. 277 (9): 7540–7545. doi: 10.1074/jbc.M110141200 . PMID   11748230.
  10. ↑ Baccon, J.; Pellizzoni, L.; Rappsilber, J.; Mann, M.; Dreyfuss, G. (2002). "Identification and Characterization of Gemin7, a Novel Component of the Survival of Motor Neuron Complex". Journal of Biological Chemistry. 277 (35): 31957–31962. doi: 10.1074/jbc.M203478200 . PMID   12065586.
  11. ↑ Dreyfuss, G.; Choi, Y. D.; Adam, S. A. (1984). "Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies". Molecular and Cellular Biology. 4 (6): 1104–1114. doi:10.1128/mcb.4.6.1104. PMC   368879 . PMID   6204191.
  12. ↑ Kamma, H.; Horiguchi, H.; Wan, L.; Matsui, M.; Fujiwara, M.; Fujimoto, M.; Yazawa, T.; Dreyfuss, G. (1999). "Molecular Characterization of the hnRNP A2/B1 Proteins: Tissue-Specific Expression and Novel Isoforms". Experimental Cell Research. 246 (2): 399–411. doi:10.1006/excr.1998.4323. PMID   9925756.
  13. ↑ Choi, Y. D.; Dreyfuss, G. (1984). "Monoclonal antibody characterization of the C proteins of heterogeneous nuclear ribonucleoprotein complexes in vertebrate cells". The Journal of Cell Biology. 99 (6): 1997–2004. doi:10.1083/jcb.99.6.1997. PMC   2113551 . PMID   6209285.
  14. ↑ Ghetti, A.; Piñol-Roma, S.; Michael, W. M.; Morandi, C.; Dreyfuss, G. (1992). "HnRNP I, the polypyrimidine tract-binding protein: Distinct nuclear localization and association with hnRNAs". Nucleic Acids Research. 20 (14): 3671–3678. doi:10.1093/nar/20.14.3671. PMC   334017 . PMID   1641332.
  15. ↑ Siomi, H.; Matunis, M. J.; Michael, W. M.; Dreyfuss, G. (1993). "The pre-mRNA binding K protein contains a novel evolutionarily conserved motif". Nucleic Acids Research. 21 (5): 1193–1198. doi:10.1093/nar/21.5.1193. PMC   309281 . PMID   8464704.
  16. ↑ Datar, K. V.; Dreyfuss, G.; Swanson, M. S. (1993). "The human hnRNP M proteins: Identification of a methionine/arginine-rich repeat motif in ribonucleoproteins". Nucleic Acids Research. 21 (3): 439–446. doi:10.1093/nar/21.3.439. PMC   309137 . PMID   8441656.
  17. 1 2 Mourelatos, Z.; Abel, L.; Yong, J.; Kataoka, N.; Dreyfuss, G. (2001). "SMN interacts with a novel family of hnRNP and spliceosomal proteins". The EMBO Journal. 20 (19): 5443–5452. doi:10.1093/emboj/20.19.5443. PMC   125643 . PMID   11574476.
  18. ↑ Kiledjian, M.; Dreyfuss, G. (1992). "Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box". The EMBO Journal. 11 (7): 2655–2664. doi:10.1002/j.1460-2075.1992.tb05331.x. PMC   556741 . PMID   1628625.
  19. ↑ Kataoka, N.; Yong, J.; Kim, V. N.; Velazquez, F.; Perkinson, R. A.; Wang, F.; Dreyfuss, G. (2000). "Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm". Molecular Cell. 6 (3): 673–682. doi: 10.1016/S1097-2765(00)00065-4 . PMID   11030346.
  20. ↑ Kataoka, N.; Diem, M. D.; Kim, V. N.; Yong, J.; Dreyfuss, G. (2001). "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex". The EMBO Journal. 20 (22): 6424–6433. doi:10.1093/emboj/20.22.6424. PMC   125744 . PMID   11707413.
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