Nancy Kedersha

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Nancy Kedersha
Born1951 (age 72–73)
Hackensack, New Jersey, U.S.
NationalityAmerican
Alma mater Bucknell University (Bachelors) Rutgers University (PhD)
Awards Lennart Nilsson Award Nikon Small World finalist
Scientific career
FieldsMicroscopy
Institutions UCLA ImmunoGen Inc.
Thesis  (1983)
Doctoral advisor Richard A Berg
Other academic advisors Leonard Rome

Nancy Kedersha (born 1951) is an American cell biologist and micrographer. She got her Ph.D. from Rutgers University where she worked in Richard Berg's lab studying the characteristics and assembly of prolyl hydroxylases. Afterwards she joined Leonard Rome's lab at UCLA as a post-doctoral fellow where she co-discovered the vault (organelle). Subsequently, she worked at ImmunoGen Inc. where she worked on staining and photographing different cancer cells. She then worked as an instructor of medicine at Brigham and Women's Hospital in Paul Anderson's lab, where her work focused on studying stress granule formation. In late-2020, she retired. In addition to her contributions as a scientist, Kedersha has been quite successful in different microscopy competitions. She is a four-time Nikon Small World finalist and in 2011 she won the Lennart Nilsson Award.

Contents

Education and early life

Kedersha is the daughter of Richard Kedersha, a professor of business administration and basketball coach at Rutgers University. [1] She graduated high school from Rutherford High School in the class of 1969. [2] [3] After completing her bachelor's in biology from Bucknell University in 1973, Kedersha pursued her graduate studies at Rutgers University in Richard Berg's lab where she characterized the purification, assembly, and biosynthesis of prolyl hydroxylase. [4] [5] [6] In 1983 she obtained her PhD in biochemistry. [7]

Career

From 1983 to 1988 Kedersha worked as a post doctoral fellow in Leonard Rome's lab at UCLA. [3] In collaboration with Rome, she co-discovered the vault (organelle). [8] The vault is this large cytoplasmic organelle found in eukaryotes, but whose function has not fully been elucidated. [9] Recent studies done in trypanosome suggest it plays a role in trans-spliced mRNA. [10]

After her post-doctoral fellowship, Kedersha worked briefly in industry for ImmunoGen Inc. using microscopy to study cancer cells. She returned to academia where she became an instructor of medicine within Paul Anderson's lab at Brigham and Women's Hospital and studied stress granules. [11] [12] [13] While there, she became the director of the confocal microscopy core. [7] She also co-wrote a chapter in Translation Mechanisms and Control. [14]

Awards and honors

Kedersha has placed ten times in the Nikon Small World competition in which four of those times she was a finalist. [15] She has also won the prestigious Lennart Nilsson Award in 2011 for her work in fluorescence microscopy. [7] [16] [17]

Nancy Kedersha's colour images open our eyes to the smallest components of life. Through her work she has pushed cell biology into new scientific, pedagogical and aesthetic realms. With the aid of a confocal microscope, she has turned biological data into an artistic experience.

— Lennart Nilsson award panel

Related Research Articles

In cellular biology, P-bodies, or processing bodies, are distinct foci formed by phase separation within the cytoplasm of a eukaryotic cell consisting of many enzymes involved in mRNA turnover. P-bodies are highly conserved structures and have been observed in somatic cells originating from vertebrates and invertebrates, plants and yeast. To date, P-bodies have been demonstrated to play fundamental roles in general mRNA decay, nonsense-mediated mRNA decay, adenylate-uridylate-rich element mediated mRNA decay, and microRNA (miRNA) induced mRNA silencing. Not all mRNAs which enter P-bodies are degraded, as it has been demonstrated that some mRNAs can exit P-bodies and re-initiate translation. Purification and sequencing of the mRNA from purified processing bodies showed that these mRNAs are largely translationally repressed upstream of translation initiation and are protected from 5' mRNA decay.

<span class="mw-page-title-main">Stress granule</span> Cytoplasmic biomolecular condensates of proteins and RNA occurring in cells under stress

In the cellular biology, stress granules are biomolecular condensates in the cytosol composed of proteins and RNA that assemble into 0.1–2 μm membraneless organelles when the cell is under stress. The mRNA molecules found in stress granules are stalled translation pre-initiation complexes associated with 40S ribosomal subunits, translation initiation factors, poly(A)+ mRNA and RNA-binding proteins (RBPs). While they are membraneless organelles, stress granules have been proposed to be associated with the endoplasmatic reticulum. There are also nuclear stress granules. This article is about the cytosolic variety.

<span class="mw-page-title-main">Vault RNA</span>

Many eukaryotic cells contain large ribonucleoprotein particles in the cytoplasm known as vaults. The vault complex comprises the major vault protein (MVP), two minor vault proteins, and a variety of small untranslated RNA molecules known as vault RNAs only found in higher eukaryotes. These molecules are transcribed by RNA polymerase III.

<span class="mw-page-title-main">XPO1</span> Protein-coding gene in the species Homo sapiens

Exportin 1 (XPO1), also known as chromosomal region maintenance 1 (CRM1), is a eukaryotic protein that mediates the nuclear export of various proteins and RNAs.

<span class="mw-page-title-main">PARP4</span> Enzyme

Poly [ADP-ribose] polymerase 4 is an enzyme that in humans is encoded by the PARP4 gene.

<span class="mw-page-title-main">Vault (organelle)</span> Eukaryotic organelle

The vault or vault cytoplasmic ribonucleoprotein is a eukaryotic organelle whose function is not yet fully understood. Discovered and isolated by Nancy Kedersha and Leonard Rome in 1986, vaults are cytoplasmic organelles which, when negative-stained and viewed under an electron microscope, resemble the arches of a cathedral's vaulted ceiling, with 39-fold symmetry. They are present in many types of eukaryotic cells, and appear to be highly conserved among eukaryotes.

<span class="mw-page-title-main">Jennifer Lippincott-Schwartz</span> American biologist

Jennifer Lippincott-Schwartz is a Senior Group Leader at Howard Hughes Medical Institute's Janelia Research Campus and a founding member of the Neuronal Cell Biology Program at Janelia. Previously, she was the Chief of the Section on Organelle Biology in the Cell Biology and Metabolism Program, in the Division of Intramural Research in the Eunice Kennedy Shriver National Institute of Child Health and Human Development at the National Institutes of Health from 1993 to 2016. Lippincott-Schwartz received her PhD from Johns Hopkins University, and performed post-doctoral training with Richard Klausner at the NICHD, NIH in Bethesda, Maryland.

Leonard H. Rome is a cell biologist and biochemist who has been a faculty member of the David Geffen School of Medicine at UCLA, since he joined the Department of Biological Chemistry there, in 1979. He became a full professor in 1988 and has also served as the Senior Associate Dean for Research in the Geffen School of Medicine from 1997 to 2012. He is the Associate Director of the California NanoSystems Institute (CNSI) since 2004, and was Interim Director from 2007-2009. In addition, he served from 2001 to 2005 as University of California, Los Angeles (UCLA) Associate Vice Chancellor for Research for the Life and Health Sciences.

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References

  1. ↑ "Richard Kedersha Obituary (2008) FloridaToday". Legacy.com. Retrieved 2021-09-28.
  2. ↑ "Rutherford is looking for distinguished graduates to add to list", South Bergenite, January 29, 2003. Accessed September 29, 2021, via Newspapers.com. "cell biologist Nancy Kedersha, '69, whose examination of the components of a cell led to the identification of a new organelle named 'vault,' 1997."
  3. 1 2 "Welcome to the Vault Website: Maintained by the Rome Laboratory at UCLA: OPEN_CMS". vaults.arc.ucla.edu. Retrieved 2021-09-29.
  4. ↑ Berg, R. A.; Kedersha, N. L.; Guzman, N. A. (1979-04-25). "Purification and partial characterization of the two nonidentical subunits of prolyl hydroxylase". The Journal of Biological Chemistry. 254 (8): 3111–3118. doi: 10.1016/S0021-9258(17)30189-8 . ISSN   0021-9258. PMID   218963.
  5. ↑ Kedersha, N. L.; Berg, R. A. (July 1981). "An improved method for the purification of vertebrate prolyl hydroxylase by affinity chromatography". Collagen and Related Research. 1 (4): 345–353. doi:10.1016/s0174-173x(81)80011-8. ISSN   0174-173X. PMID   6286234.
  6. ↑ Kedersha, N. L.; Tkacz, J. S.; Berg, R. A. (1985-10-08). "Biosynthesis of prolyl hydroxylase: evidence for two separate dolichol-media pathways of glycosylation". Biochemistry. 24 (21): 5960–5967. doi:10.1021/bi00342a041. ISSN   0006-2960. PMID   3002430.
  7. 1 2 3 "Lennart Nilsson Award 2011: The Secret Life of Cells – in Colour". Wiley Analytical Science. doi:10.1002/imaging.2768 (inactive 1 November 2024). Retrieved 2021-09-29.{{cite web}}: CS1 maint: DOI inactive as of November 2024 (link)
  8. ↑ Kedersha, N. L.; Rome, L. H. (1986-09-01). "Isolation and characterization of a novel ribonucleoprotein particle: large structures contain a single species of small RNA". The Journal of Cell Biology. 103 (3): 699–709. doi:10.1083/jcb.103.3.699. ISSN   0021-9525. PMC   2114306 . PMID   2943744.
  9. ↑ Kedersha, N. L.; Miquel, M. C.; Bittner, D.; Rome, L. H. (1990-04-01). "Vaults. II. Ribonucleoprotein structures are highly conserved among higher and lower eukaryotes". The Journal of Cell Biology. 110 (4): 895–901. doi:10.1083/jcb.110.4.895. ISSN   0021-9525. PMC   2116106 . PMID   1691193.
  10. ↑ Kolev, Nikolay G.; Rajan, K. Shanmugha; Tycowski, Kazimierz T.; Toh, Justin Y.; Shi, Huafang; Lei, Yuling; Michaeli, Shulamit; Tschudi, Christian (2019-10-25). "The vault RNA of Trypanosoma brucei plays a role in the production of trans-spliced mRNA". The Journal of Biological Chemistry. 294 (43): 15559–15574. doi: 10.1074/jbc.RA119.008580 . ISSN   0021-9258. PMC   6816085 . PMID   31439669.
  11. ↑ Kedersha, N. L.; Gupta, M.; Li, W.; Miller, I.; Anderson, P. (1999-12-27). "RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules". The Journal of Cell Biology. 147 (7): 1431–1442. doi:10.1083/jcb.147.7.1431. ISSN   0021-9525. PMC   2174242 . PMID   10613902.
  12. ↑ Kedersha, Nancy; Stoecklin, Georg; Ayodele, Maranatha; Yacono, Patrick; Lykke-Andersen, Jens; Fritzler, Marvin J.; Scheuner, Donalyn; Kaufman, Randal J.; Golan, David E.; Anderson, Paul (2005-06-20). "Stress granules and processing bodies are dynamically linked sites of mRNP remodeling". The Journal of Cell Biology. 169 (6): 871–884. doi:10.1083/jcb.200502088. ISSN   0021-9525. PMC   2171635 . PMID   15967811.
  13. ↑ Kedersha, Nancy; Panas, Marc D.; Achorn, Christopher A.; Lyons, Shawn; Tisdale, Sarah; Hickman, Tyler; Thomas, Marshall; Lieberman, Judy; McInerney, Gerald M.; Ivanov, Pavel; Anderson, Paul (2016-03-28). "G3BP-Caprin1-USP10 complexes mediate stress granule condensation and associate with 40S subunits". The Journal of Cell Biology. 212 (7): 845–860. doi:10.1083/jcb.201508028. ISSN   1540-8140. PMC   4810302 . PMID   27022092.
  14. ↑ "Translation Mechanisms and Control". cshperspectives.cshlp.org. Retrieved 2021-09-28.
  15. ↑ "Nancy Kedersha". Nikon’s Small World. Retrieved 2021-09-28.
  16. ↑ "The secret life of cells – in colour". www.bionity.com. Retrieved 2021-09-28.
  17. ↑ "Fotografen Lennart Nilsson och Lennart Nilsson Award". Lennartnilssonaward.se (in Swedish). Retrieved 2021-09-29.
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