Lori Passmore

Last updated
Lori Passmore

FRS
LoriPassmore.jpg
Born
Lori Anne Passmore
NationalityCanadian/British
Alma mater
Awards
Scientific career
Fields
Institutions
Thesis Structural and functional studies of the anaphase promoting complex (APC)  (2003)
Doctoral advisor David Barford
Other academic advisors Venki Ramakrishnan
Richard Henderson
Website www2.mrc-lmb.cam.ac.uk/groups/passmore OOjs UI icon edit-ltr-progressive.svg

Lori Anne Passmore FRS is a Canadian/British cryo electron microscopist and structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) at the University of Cambridge. [3] [4] She is known for her work on multiprotein complexes involved in gene expression [5] [6] [7] and development of new supports for cryo-EM. [8]

Contents

Education

Lori Passmore graduated from the University of British Columbia, Canada in 1999. [9] She obtained a PhD in 2003 from University of London for research supervised by David Barford at the Institute of Cancer Research. She performed in vitro biochemical characterisation of the activity of the anaphase-promoting complex (APC) [10] and used cryo-EM to study the APC structure. [1] [11]

Career and research

Passmore worked as a postdoctoral researcher at the MRC-LMB. She worked with Venki Ramakrishnan and Richard Henderson, using cryo-EM to determine the structure of the eukaryotic ribosome bound to initiation factors. [12] Passmore became a group leader at the MRC-LMB in 2009. Her group uses in vitro reconstitution, biochemical assays and cryo-EM to understand the function of multiprotein complexes that regulate gene expression at the level of mRNA. [5] [6] [7] Her group has developed new sample grids for cryo-EM that reduce specimen movement during imaging. [8] In collaboration with Ketan J. Patel, Passmore is also actively studying the molecular mechanisms underlying Fanconi anemia. [13] [14]

Grants, awards and honours

Related Research Articles

<span class="mw-page-title-main">Anaphase-promoting complex</span> Cell-cycle regulatory complex

Anaphase-promoting complex is an E3 ubiquitin ligase that marks target cell cycle proteins for degradation by the 26S proteasome. The APC/C is a large complex of 11–13 subunit proteins, including a cullin (Apc2) and RING (Apc11) subunit much like SCF. Other parts of the APC/C have unknown functions but are highly conserved.

<span class="mw-page-title-main">Transmission electron cryomicroscopy</span>

Transmission electron cryomicroscopy (CryoTEM), commonly known as cryo-EM, is a form of cryogenic electron microscopy, more specifically a type of transmission electron microscopy (TEM) where the sample is studied at cryogenic temperatures. Cryo-EM is gaining popularity in structural biology.

<span class="mw-page-title-main">MRC Laboratory of Molecular Biology</span> Research institute in Cambridge, England

The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) is a research institute in Cambridge, England, involved in the revolution in molecular biology which occurred in the 1950–60s. Since then it has remained a major medical research laboratory at the forefront of scientific discovery, dedicated to improving the understanding of key biological processes at atomic, molecular and cellular levels using multidisciplinary methods, with a focus on using this knowledge to address key issues in human health.

<span class="mw-page-title-main">CDC20</span> Protein-coding gene in the species Homo sapiens

The cell division cycle protein 20 homolog is an essential regulator of cell division that is encoded by the CDC20 gene in humans. To the best of current knowledge its most important function is to activate the anaphase promoting complex (APC/C), a large 11-13 subunit complex that initiates chromatid separation and entrance into anaphase. The APC/CCdc20 protein complex has two main downstream targets. Firstly, it targets securin for destruction, enabling the eventual destruction of cohesin and thus sister chromatid separation. It also targets S and M-phase (S/M) cyclins for destruction, which inactivates S/M cyclin-dependent kinases (Cdks) and allows the cell to exit from mitosis. A closely related protein, Cdc20homologue-1 (Cdh1) plays a complementary role in the cell cycle.

<span class="mw-page-title-main">FZR1</span> Protein-coding gene in the species Homo sapiens

Fizzy-related protein homolog, also known as hCDH1, is a protein that in humans is encoded by the FZR1 gene.

<span class="mw-page-title-main">CDC16</span> Protein-coding gene in the species Homo sapiens

Cell division cycle protein 16 homolog is a protein that in humans is encoded by the CDC16 gene.

<span class="mw-page-title-main">CDC23</span> Protein-coding gene in the species Homo sapiens

Cell division cycle 23 homolog , also known as CDC23, is a protein that, in humans, is encoded by the CDC23 gene.

<span class="mw-page-title-main">ANAPC2</span> Protein-coding gene in the species Homo sapiens

Anaphase-promoting complex subunit 2 is an enzyme that in humans is encoded by the ANAPC2 gene.

<span class="mw-page-title-main">Tetratricopeptide repeat</span> Protein tandem repeat

The tetratricopeptide repeat (TPR) is a structural motif. It consists of a degenerate 34 amino acid tandem repeat identified in a wide variety of proteins. It is found in tandem arrays of 3–16 motifs, which form scaffolds to mediate protein–protein interactions and often the assembly of multiprotein complexes. These alpha-helix pair repeats usually fold together to produce a single, linear solenoid domain called a TPR domain. Proteins with such domains include the anaphase-promoting complex (APC) subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, the protein kinase R (PKR), the major receptor for peroxisomal matrix protein import PEX5, protein arginine methyltransferase 9 (PRMT9), and mitochondrial import proteins.

David Barford is a British medical researcher and structural biologist at the MRC Laboratory of Molecular Biology Cambridge, UK.

<span class="mw-page-title-main">Ketan J. Patel</span>

Ketan Jayakrishna Patel is a British-Kenyan scientist who is Director of the MRC Weatherall Institute of Molecular Medicine and the MRC Molecular Haematology Unit at the University of Oxford. Until 2020 he was a tenured principal investigator at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB).

<span class="mw-page-title-main">Jan Löwe</span> Director of the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB)

Jan Löwe is a German molecular and structural biologist and the Director of the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He became Director of the MRC-LMB in April 2018, succeeding Sir Hugh Pelham. Löwe is known for his contributions to the current understanding of bacterial cytoskeletons.

<span class="mw-page-title-main">Sjors Scheres</span>

Sjors Hendrik Willem ScheresFRS is a Dutch scientist at the MRC Laboratory of Molecular Biology Cambridge, UK.

<span class="mw-page-title-main">Andrew P. Carter</span> British structural biologist

Andrew P. Carter is a British structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He is known for his work on the microtubule motor dynein.

<span class="mw-page-title-main">Melina Schuh</span> German molecular biologist

Melina Schuh is a German biochemist and Director at the Max Planck Institute for Multidisciplinary Sciences. She is known for her work on meiosis in mammalian oocytes, for her studies on the mechanisms leading to the age-related decline in female fertility, and for the development of the Trim-Away protein depletion method.

<span class="mw-page-title-main">Kiyoshi Nagai</span> Japanese structural biologist (1949–2019)

Kiyoshi Nagai was a Japanese structural biologist at the MRC Laboratory of Molecular Biology Cambridge, UK. He was known for his work on the mechanism of RNA splicing and structures of the spliceosome.

Anne Bertolotti is a French biochemist and cell biologist who works as Programme Leader at the MRC Laboratory of Molecular Biology in Cambridge, UK. In 2022 she was appointed Head of the MRC LMB's Neurobiology Division. She is known for her research into the cellular defences against misfolded proteins and the mechanisms underlying their deposition, the molecular problem causative of neurodegenerative diseases.

<span class="mw-page-title-main">CCR4-Not</span> Multiprotein complex used in gene expression

Carbon Catabolite Repression—Negative On TATA-less, or CCR4-Not, is a multiprotein complex that functions in gene expression. The complex has multiple enzymatic activities as both a poly(A) 3′-5′ exonuclease and a ubiquitin ligase. The complex is present both in the nucleus where it regulates transcription and in the cytoplasm where it associates with translating ribosomes and RNA processing bodies.

<span class="mw-page-title-main">M. Madan Babu</span> Indian-American computational biologist

M. Madan Babu is an Indian-American computational biologist and bioinformatician. He is the endowed chair in biological data science and director of the center of excellence for data-driven discovery at St. Jude Children’s Research Hospital. Previously, he served as a programme leader at the MRC Laboratory of Molecular Biology (LMB).

<span class="mw-page-title-main">Nicolas H. Thomä</span> German structural and chemical biologist

Nicolas H. Thomä is a German researcher, senior group leader at the Friedrich Miescher Institute for Biomedical Research in Basel, Switzerland. He is a biochemist and structural biologist and a leading researcher in the fields of ubiquitin ligase biology and DNA repair.

References

  1. 1 2 Passmore, Lori Anne (2003). Structural and functional studies of the anaphase promoting complex (APC). london.ac.uk (PhD thesis). University Of London. OCLC   500247667. EThOS   uk.bl.ethos.406167.
  2. 1 2 "Celebrating women in science on Ada Lovelace Day 2016". suffragescience.org. Retrieved 2018-06-08.
  3. Lori Passmore publications indexed by Google Scholar OOjs UI icon edit-ltr-progressive.svg
  4. Lori Passmore publications from Europe PubMed Central
  5. 1 2 Wolf J, Valkov E, Allen MD, Meineke B, Gordiyenko Y, McLaughlin SH, Olsen TM, Robinson CV, Bycroft M, Stewart M, Passmore LA (2014). "Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation". The EMBO Journal. 33 (14): 1514–26. doi:10.15252/embj.201488373. PMC   4158885 . PMID   24872509.
  6. 1 2 Casañal A, Kumar A, Hill CH, Easter AD, Emsley P, Degliesposti G, Gordiyenko Y, Santhanam B, Wolf J, Wiederhold K, Dornan GL, Skehel M, Robinson CV, Passmore LA (2017). "Architecture of eukaryotic mRNA 3'-end processing machinery". Science. 358 (6366): 1056–1059. doi:10.1126/science.aao6535. PMC   5788269 . PMID   29074584.
  7. 1 2 Stowell JA, Webster MW, Kögel A, Wolf J, Shelley KL, Passmore LA (2016). "Reconstitution of Targeted Deadenylation by the Ccr4-Not Complex and the YTH Domain Protein Mmi1". Cell Reports. 17 (8): 1978–1989. doi:10.1016/j.celrep.2016.10.066. PMC   5120349 . PMID   27851962.
  8. 1 2 Russo CJ, Passmore LA (2014). "Electron microscopy: Ultrastable gold substrates for electron cryomicroscopy". Science. 346 (6215): 1377–80. doi:10.1126/science.1259530. PMC   4296556 . PMID   25504723.
  9. 1 2 3 4 "Dr. Lori Anne Passmore - AcademiaNet". www.academia-net.org. Retrieved 2018-06-08.
  10. Passmore LA, McCormack EA, Au SW, Paul A, Willison KR, Harper JW, Barford D (2003). "Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition". The EMBO Journal. 22 (4): 786–96. doi:10.1093/emboj/cdg084. PMC   145444 . PMID   12574115.
  11. Passmore LA, Booth CR, Vénien-Bryan C, Ludtke SJ, Fioretto C, Johnson LN, Chiu W, Barford D (2005). "Structural analysis of the anaphase-promoting complex reveals multiple active sites and insights into polyubiquitylation". Molecular Cell. 20 (6): 855–66. doi: 10.1016/j.molcel.2005.11.003 . PMID   16364911.
  12. Passmore LA, Schmeing TM, Maag D, Applefield DJ, Acker MG, Algire MA, Lorsch JR, Ramakrishnan V (2007). "The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome". Molecular Cell. 26 (1): 41–50. doi: 10.1016/j.molcel.2007.03.018 . PMID   17434125.
  13. Rajendra E, Garaycoechea JI, Patel KJ, Passmore LA (2014). "Abundance of the Fanconi anaemia core complex is regulated by the RuvBL1 and RuvBL2 AAA+ ATPases". Nucleic Acids Research. 42 (22): 13736–13748. doi:10.1093/nar/gku1230. PMC   4267650 . PMID   25428364.
  14. Rajendra E, Oestergaard VH, Langevin F, Wang M, Dornan GL, Patel KJ, Passmore LA (2014). "The Genetic and Biochemical Basis of FANCD2 Monoubiquitination". Molecular Cell. 54 (5): 858–869. doi:10.1016/j.molcel.2014.05.001. PMC   4051986 . PMID   24905007.
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