Andrew P. Carter

Last updated

Andrew P Carter
AndrewCarter wikki 2018.jpg
NationalityBritish
Alma mater
Awards EMBO Member (2016)
Scientific career
Fields
Institutions
Doctoral advisor Venki Ramakrishnan
Other academic advisors Ron Vale
Website www2.mrc-lmb.cam.ac.uk/groups/cartera/

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. [1] [2] [3] [4]

Contents

Education

Carter studied Biochemistry at the University of Oxford, graduating in 1999. [5] He obtained a PhD in 2003 from the MRC Laboratory of Molecular Biology where he worked with Venki Ramakrishnan on the ribosome. He was a member of the team in Ramakrishnan's lab that solved the first X-ray crystal structure of the small (30S) ribosomal subunit. [6] Carter also determined structures of 30S bound to antibiotics [7] and bound to the initiation factor IF1. [8] Ramakrishnan shared the Nobel prize in Chemistry for the team's work on the 30S. [9]

Career and research

Carter was a post-doc in Ron Vale's lab [10] at University of California, San Francisco from 2003 to 2010. During his post-doc, he studied the molecular motor protein, dynein using X-ray crystallography and single molecule fluorescence microscopy. [11] [12]

He became a group leader at MRC Laboratory of Molecular Biology in Cambridge in 2010 where he uses X-ray crystallography, electron microscopy, and single molecule microscopy assays to understand how dynein transports cargo. His group solved X-ray crystal structures of the dynein motor domain showing how it generates force to pull cargos along microtubules [1] and reconstituted a recombinant dynein, showing how its processive movement is activated by cofactors/cargo adaptors. [13] His group used cryoEM to solve the structure of dynein's cofactor dynactin [2] and the full length dynein complex. [3] They showed how dynein and dynactin come together in the presence of cargos and how this activates transport.

Grants, awards and honours

Related Research Articles

<span class="mw-page-title-main">Ribosome</span> Intracellular organelle consisting of RNA and protein functioning to synthesize proteins

Ribosomes are macromolecular machines, found within all cells, that perform biological protein synthesis. Ribosomes link amino acids together in the order specified by the codons of messenger RNA (mRNA) molecules to form polypeptide chains. Ribosomes consist of two major components: the small and large ribosomal subunits. Each subunit consists of one or more ribosomal RNA (rRNA) molecules and many ribosomal proteins. The ribosomes and associated molecules are also known as the translational apparatus.

<span class="mw-page-title-main">Dynein</span> Class of enzymes

Dyneins are a family of cytoskeletal motor proteins that move along microtubules in cells. They convert the chemical energy stored in ATP to mechanical work. Dynein transports various cellular cargos, provides forces and displacements important in mitosis, and drives the beat of eukaryotic cilia and flagella. All of these functions rely on dynein's ability to move towards the minus-end of the microtubules, known as retrograde transport; thus, they are called "minus-end directed motors". In contrast, most kinesin motor proteins move toward the microtubules' plus-end, in what is called anterograde transport.

<span class="mw-page-title-main">Venki Ramakrishnan</span> Indian-born British-American structural biologist (born 1952)

Venkatraman "Venki" Ramakrishnan is an Indian-born British and American structural biologist. He shared the 2009 Nobel Prize in Chemistry with Thomas A. Steitz and Ada Yonath for research on the structure and function of ribosomes.

<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">Prokaryotic small ribosomal subunit</span> Smaller subunit of the 70S ribosome found in prokaryote cells

The prokaryotic small ribosomal subunit, or 30S subunit, is the smaller subunit of the 70S ribosome found in prokaryotes. It is a complex of the 16S ribosomal RNA (rRNA) and 19 proteins. This complex is implicated in the binding of transfer RNA to messenger RNA (mRNA). The small subunit is responsible for the binding and the reading of the mRNA during translation. The small subunit, both the rRNA and its proteins, complexes with the large 50S subunit to form the 70S prokaryotic ribosome in prokaryotic cells. This 70S ribosome is then used to translate mRNA into proteins.

<span class="mw-page-title-main">DCTN1</span> Protein-coding gene in the species Homo sapiens

Dynactin subunit 1 is a protein that in humans is encoded by the DCTN1 gene.

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

Dynactin is a 23 subunit protein complex that acts as a co-factor for the microtubule motor cytoplasmic dynein-1. It is built around a short filament of actin related protein-1 (Arp1).

<span class="mw-page-title-main">DCTN2</span> Gene of the species Homo sapiens

Dynactin subunit 2 is a protein that in humans is encoded by the DCTN2 gene

The eukaryotic small ribosomal subunit (40S) is the smaller subunit of the eukaryotic 80S ribosomes, with the other major component being the large ribosomal subunit (60S). The "40S" and "60S" names originate from the convention that ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. It is structurally and functionally related to the 30S subunit of 70S prokaryotic ribosomes. However, the 40S subunit is much larger than the prokaryotic 30S subunit and contains many additional protein segments, as well as rRNA expansion segments.

<span class="mw-page-title-main">Translation initiation factor IF-3</span>

In molecular biology, translation initiation factor IF-3 is one of the three factors required for the initiation of protein biosynthesis in bacteria. IF-3 is thought to function as a fidelity factor during the assembly of the ternary initiation complex which consists of the 30S ribosomal subunit, the initiator tRNA and the messenger RNA. IF-3 is a basic protein that binds to the 30S ribosomal subunit. The chloroplast homolog enhances the poly(A,U,G)-dependent binding of the initiator tRNA to its ribosomal 30s subunits. IF1–IF3 may also perform ribosome recycling.

<span class="mw-page-title-main">Nenad Ban</span> Croatian biochemist

Nenad Ban is a biochemist born in Zagreb, Croatia who currently works at the ETH Zurich, Swiss Federal Institute of Technology, as a professor of Structural Molecular Biology. He is a pioneer in studying gene expression mechanisms and the participating protein synthesis machinery.

In molecular biology, DCTN6 is that subunit of the dynactin protein complex that is encoded by the p27 gene. Dynactin is the essential component for microtubule-based cytoplasmic dynein motor activity in intracellular transport of a variety of cargoes and organelles.

David Chaim Rubinsztein FRS FMedSci is the Deputy Director of the Cambridge Institute of Medical Research (CIMR), Professor of Molecular Neurogenetics at the University of Cambridge and a UK Dementia Research Institute Professor.

<span class="mw-page-title-main">Lalita Ramakrishnan</span> Indian-American microbiologist

Lalita Ramakrishnan is an Indian-born American microbiologist who is known for her contributions to the understanding of the biological mechanism of tuberculosis. As of 2019 she serves as a professor of Immunology and Infectious Diseases at the University of Cambridge, where she is also a Wellcome Trust Principal Research Fellow and a practicing physician. Her research is conducted at the MRC Laboratory of Molecular Biology, where she serves as the Head of the Molecular Immunity Unit of the Department of Medicine embedded at the MRC LMB. Working with Stanley Falkow at Stanford, she developed the strategy of using Mycobacterium marinum infection as a model for tuberculosis. Her work has appeared in a number of journals, including Science, Nature, and Cell. In 2018 and 2019 Ramakrishnan coauthored two influential papers in the British Medical Journal (BMJ) arguing that the widely accepted estimates of the prevalence of latent tuberculosis—estimates used as a basis for allocation of research funds—are far too high. She is married to Mark Troll, a physical chemist.

<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">Lori Passmore</span> Canadian/British scientist

Lori Anne Passmore 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. She is known for her work on multiprotein complexes involved in gene expression and development of new supports for cryo-EM.

<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">Helen Walden</span> English structural biologist

Helen Walden is an English structural biologist who received the Colworth medal from the Biochemical Society in 2015. She was awarded European Molecular Biology Organization (EMBO) membership in 2022. She is a Professor of Structural Biology at the University of Glasgow and has made significant contributions to the Ubiquitination field.

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">Erika Holzbaur</span> American biologist

Erika L F. Holzbaur is an American biologist who is the William Maul Measey Professor of Physiology at University of Pennsylvania Perelman School of Medicine. Her research considers the dynamics of organelle motility along cytoskeleton of cells. She is particularly interested in the molecular mechanisms that underpin neurodegenerative diseases.

References

  1. 1 2 Schmidt, Helgo; Zalyte, Ruta; Urnavicius, Linas; Carter, Andrew P. (19 February 2015). "Structure of human cytoplasmic dynein-2 primed for its power stroke". Nature. 518 (7539): 435–438. Bibcode:2015Natur.518..435S. doi:10.1038/nature14023. ISSN   1476-4687. PMC   4336856 . PMID   25470043.
  2. 1 2 Urnavicius, Linas; Zhang, Kai; Diamant, Aristides G.; Motz, Carina; Schlager, Max A.; Yu, Minmin; Patel, Nisha A.; Robinson, Carol V.; Carter, Andrew P. (27 March 2015). "The structure of the dynactin complex and its interaction with dynein". Science. 347 (6229): 1441–1446. Bibcode:2015Sci...347.1441U. doi:10.1126/science.aaa4080. ISSN   1095-9203. PMC   4413427 . PMID   25814576.
  3. 1 2 Zhang, Kai; Foster, Helen E.; Rondelet, Arnaud; Lacey, Samuel E.; Bahi-Buisson, Nadia; Bird, Alexander W.; Carter, Andrew P. (15 June 2017). "Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated". Cell. 169 (7): 1303–1314.e18. doi:10.1016/j.cell.2017.05.025. ISSN   1097-4172. PMC   5473941 . PMID   28602352.
  4. Urnavicius, Linas; Lau, Clinton K.; Elshenawy, Mohamed M.; Morales-Rios, Edgar; Motz, Carina; Yildiz, Ahmet; Carter, Andrew P. (7 February 2018). "Cryo-EM shows how dynactin recruits two dyneins for faster movement". Nature. 554 (7691): 202–206. Bibcode:2018Natur.554..202U. doi:10.1038/nature25462. ISSN   1476-4687. PMC   5988349 . PMID   29420470.
  5. "2012 Alumni Lecture celebrating Oxford Biochemistry graduate success Page - Department of Biochemistry, University of Oxford". www.bioch.ox.ac.uk. Archived from the original on 13 August 2018. Retrieved 26 August 2018.
  6. Wimberly, B. T.; Brodersen, D. E.; Clemons, W. M.; Morgan-Warren, R. J.; Carter, A. P.; Vonrhein, C.; Hartsch, T.; Ramakrishnan, V. (21 September 2000). "Structure of the 30S ribosomal subunit". Nature. 407 (6802): 327–339. Bibcode:2000Natur.407..327W. doi:10.1038/35030006. ISSN   0028-0836. PMID   11014182. S2CID   4419944.
  7. Carter, A. P.; Clemons, W. M.; Brodersen, D. E.; Morgan-Warren, R. J.; Wimberly, B. T.; Ramakrishnan, V. (21 September 2000). "Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics". Nature. 407 (6802): 340–348. Bibcode:2000Natur.407..340C. doi:10.1038/35030019. ISSN   0028-0836. PMID   11014183. S2CID   4408938.
  8. Carter, A. P.; Clemons, W. M.; Brodersen, D. E.; Morgan-Warren, R. J.; Hartsch, T.; Wimberly, B. T.; Ramakrishnan, V. (19 January 2001). "Crystal structure of an initiation factor bound to the 30S ribosomal subunit". Science. 291 (5503): 498–501. Bibcode:2001Sci...291..498C. doi:10.1126/science.1057766. ISSN   0036-8075. PMID   11228145.
  9. "Venkatraman Ramakrishnan - Nobel Lecture: Unraveling the Structure of the Ribosome". NobelPrize.org. Retrieved 26 August 2018.
  10. "Carter". valelab.ucsf.edu. Retrieved 25 August 2018.
  11. Carter, Andrew P.; Garbarino, Joan E.; Wilson-Kubalek, Elizabeth M.; Shipley, Wesley E.; Cho, Carol; Milligan, Ronald A.; Vale, Ronald D.; Gibbons, I. R. (12 December 2008). "Structure and functional role of dynein's microtubule-binding domain". Science. 322 (5908): 1691–1695. Bibcode:2008Sci...322.1691C. doi:10.1126/science.1164424. ISSN   1095-9203. PMC   2663340 . PMID   19074350.
  12. Carter, Andrew P.; Cho, Carol; Jin, Lan; Vale, Ronald D. (4 March 2011). "Crystal structure of the dynein motor domain". Science. 331 (6021): 1159–1165. Bibcode:2011Sci...331.1159C. doi:10.1126/science.1202393. ISSN   1095-9203. PMC   3169322 . PMID   21330489.
  13. Schlager, Max A.; Hoang, Ha Thi; Urnavicius, Linas; Bullock, Simon L.; Carter, Andrew P. (1 September 2014). "In vitro reconstitution of a highly processive recombinant human dynein complex". The EMBO Journal. 33 (17): 1855–1868. doi:10.15252/embj.201488792. ISSN   1460-2075. PMC   4158905 . PMID   24986880.
  14. "LMB Student Prize - MRC Laboratory of Molecular Biology". MRC Laboratory of Molecular Biology. Retrieved 26 August 2018.
  15. "Agouron Institute | Fellowships". agi.org. Retrieved 26 August 2018.
  16. Cambridge, Clare College. "Dr Andrew Carter - Clare College Cambridge". www.clare.cam.ac.uk. Retrieved 25 August 2018.
  17. adit. "22 young group leaders recognized as EMBO Young Investigators". EMBO. Retrieved 26 August 2018.
  18. 1 2 "Investigator Awards in Science: people we've funded | Wellcome". wellcome.ac.uk. Retrieved 26 August 2018.
  19. "Find people in the EMBO Communities". people.embo.org. Retrieved 26 August 2018.
  20. "58 life science researchers elected as new EMBO Members". EMBO. Archived from the original on 15 August 2016. Retrieved 26 August 2018.