David C. Rubinsztein

Last updated

David Rubinsztein
Born
David Chaim Rubinsztein

1963 (age 60–61)
Alma mater University of Cape Town (MBChB, PhD)
Known for autophagy and polyglutamine expansions
Awards
Scientific career
Fields Autophagy
Neurodegenerative diseases [4]
Institutions University of Cambridge
Cambridge Institute for Medical Research
Cambridge Drug Discovery Institute
Thesis Monogenic hypercholesterolemia in South Africans: familial hypercholesterolemia in Indians and familial defective apolipoprotein B-100  (1993)
Doctoral advisor Prof. D.R. van der Westhuyzen
Website

David Chaim Rubinsztein (born 1963) FRS [3] FMedSci [5] is the Deputy Director of the Cambridge Institute of Medical Research (CIMR), [6] Professor of Molecular Neurogenetics at the University of Cambridge [7] and a UK Dementia Research Institute Professor.

Contents

Education

Rubinsztein completed his Bachelor of Medicine, Bachelor of Surgery (MB ChB) in 1986 and PhD in 1993 in the Medical Research Council/University of Cape Town Unit for the Cell Biology of Atherosclerosis. In 1993 he went to Cambridge as a senior registrar in Genetic Pathology. [8]

Career

In 1997, Rubinsztein acquired his Certificate of Completion of Specialist Training at the University of Cambridge. He was appointed to a Personal Readership at the University of Cambridge in 2003. In 2005, he was promoted to Professor of Molecular Neurogenetics at the University of Cambridge (personal chair). He has been an author on more than 400 scientific papers, [4] [9] and was ranked as the 4th most cited European author from 2007 to 2013 in cell biology. [10] Rubinsztein has been invited to give talks at major international conferences, including Gordon Research Conferences and Keystone Symposia. [11] [12] [13]

Research

Rubinsztein has made major contributions to the field of neurodegeneration [4] with his laboratory's discovery that autophagy regulates the levels of intracytoplasmic aggregate-prone proteins that cause many neurodegenerative diseases, including Huntington's, Parkinson's and Alzheimer's disease. [14] [15] [16] [17] [18] His lab has found that autophagy may be inhibited in various neurodegenerative diseases [19] and has elucidated the pathological consequences of autophagy compromise. [20] In addition his research has advanced the basic understanding of autophagy, identifying the plasma membrane as a source of autophagosome membrane [21] and characterising early events in autophagosome biogenesis,. [22] [23] [24] Furthermore, he studied how lysosomal positioning regulates autophagy. [25] His goal is to understand the links between these diseases and autophagy. He is currently focused on understanding how to induce autophagy in vivo to remove toxic proteins and avoid the development of neurodegenerative disease [6] [26]

Honours and awards

Rubinsztein has won numerous awards including:

Related Research Articles

Cell biology is a branch of biology that studies the structure, function, and behavior of cells. All living organisms are made of cells. A cell is the basic unit of life that is responsible for the living and functioning of organisms. Cell biology is the study of the structural and functional units of cells. Cell biology encompasses both prokaryotic and eukaryotic cells and has many subtopics which may include the study of cell metabolism, cell communication, cell cycle, biochemistry, and cell composition. The study of cells is performed using several microscopy techniques, cell culture, and cell fractionation. These have allowed for and are currently being used for discoveries and research pertaining to how cells function, ultimately giving insight into understanding larger organisms. Knowing the components of cells and how cells work is fundamental to all biological sciences while also being essential for research in biomedical fields such as cancer, and other diseases. Research in cell biology is interconnected to other fields such as genetics, molecular genetics, molecular biology, medical microbiology, immunology, and cytochemistry.

<span class="mw-page-title-main">Autophagy</span> Cellular catabolic process in which cells digest parts of their own cytoplasm

Autophagy is the natural, conserved degradation of the cell that removes unnecessary or dysfunctional components through a lysosome-dependent regulated mechanism. It allows the orderly degradation and recycling of cellular components. Although initially characterized as a primordial degradation pathway induced to protect against starvation, it has become increasingly clear that autophagy also plays a major role in the homeostasis of non-starved cells. Defects in autophagy have been linked to various human diseases, including neurodegeneration and cancer, and interest in modulating autophagy as a potential treatment for these diseases has grown rapidly.

<span class="mw-page-title-main">Bafilomycin</span> Chemical compound

The bafilomycins are a family of macrolide antibiotics produced from a variety of Streptomycetes. Their chemical structure is defined by a 16-membered lactone ring scaffold. Bafilomycins exhibit a wide range of biological activity, including anti-tumor, anti-parasitic, immunosuppressant and anti-fungal activity. The most used bafilomycin is bafilomycin A1, a potent inhibitor of cellular autophagy. Bafilomycins have also been found to act as ionophores, transporting potassium K+ across biological membranes and leading to mitochondrial damage and cell death.

<span class="mw-page-title-main">Neurodegenerative disease</span> Central nervous system disease

A neurodegenerative disease is caused by the progressive loss of structure or function of neurons, in the process known as neurodegeneration. Such neuronal damage may ultimately involve cell death. Neurodegenerative diseases include amyotrophic lateral sclerosis, multiple sclerosis, Parkinson's disease, Alzheimer's disease, Huntington's disease, multiple system atrophy, tauopathies, and prion diseases. Neurodegeneration can be found in the brain at many different levels of neuronal circuitry, ranging from molecular to systemic. Because there is no known way to reverse the progressive degeneration of neurons, these diseases are considered to be incurable; however research has shown that the two major contributing factors to neurodegeneration are oxidative stress and inflammation. Biomedical research has revealed many similarities between these diseases at the subcellular level, including atypical protein assemblies and induced cell death. These similarities suggest that therapeutic advances against one neurodegenerative disease might ameliorate other diseases as well.

<span class="mw-page-title-main">Vojo Deretic</span> American geneticist

Vojo Deretic, is distinguished professor and chair of the Department of Molecular Genetics and Microbiology at the University of New Mexico School of Medicine. Deretic was the founding director of the Autophagy, Inflammation and Metabolism (AIM) Center of Biomedical Research Excellence. The AIM center promotes autophagy research nationally and internationally.

<span class="mw-page-title-main">TANK-binding kinase 1</span> Protein-coding gene in the species Homo sapiens

TBK1 is an enzyme with kinase activity. Specifically, it is a serine / threonine protein kinase. It is encoded by the TBK1 gene in humans. This kinase is mainly known for its role in innate immunity antiviral response. However, TBK1 also regulates cell proliferation, apoptosis, autophagy, and anti-tumor immunity. Insufficient regulation of TBK1 activity leads to autoimmune, neurodegenerative diseases or tumorigenesis.

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

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<span class="mw-page-title-main">MAP1LC3B</span> Protein-coding gene in the species Homo sapiens

Microtubule-associated proteins 1A/1B light chain 3B is a protein that in humans is encoded by the MAP1LC3B gene. LC3 is a central protein in the autophagy pathway where it functions in autophagy substrate selection and autophagosome biogenesis. LC3 is the most widely used marker of autophagosomes.

<span class="mw-page-title-main">ATG16L1</span> Protein-coding gene in the species Homo sapiens

Autophagy related 16 like 1 is a protein that in humans is encoded by the ATG16L1 gene. This protein is characterized as a subunit of the autophagy-related ATG12-ATG5/ATG16 complex and is essentially important for the LC3 (ATG8) lipidation and autophagosome formation. This complex localizes to the membrane and is released just before or after autophagosome completion.

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

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

<span class="mw-page-title-main">ATG9A</span> Protein-coding gene in the species Homo sapiens

Autophagy-related protein 9A is a protein that in humans is encoded by the ATG9A gene.

<span class="mw-page-title-main">ULK1</span> Enzyme found in humans

ULK1 is an enzyme that in humans is encoded by the ULK1 gene.

<span class="mw-page-title-main">ATG8</span> Protein in budding yeast

Autophagy-related protein 8 (Atg8) is a ubiquitin-like protein required for the formation of autophagosomal membranes. The transient conjugation of Atg8 to the autophagosomal membrane through a ubiquitin-like conjugation system is essential for autophagy in eukaryotes. Even though there are homologues in animals, this article mainly focuses on its role in lower eukaryotes such as Saccharomyces cerevisiae.

<span class="mw-page-title-main">Yoshinori Ohsumi</span> Japanese cell biologist

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<span class="mw-page-title-main">Felix Armin Randow</span>

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<span class="mw-page-title-main">Rubicon (protein)</span> Human protein involved in autophagy regulation

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<span class="mw-page-title-main">AMBRA1</span> Protein-coding gene

AMBRA1 is a protein that is able to regulate cancer cells through autophagy. AMBRA1 is described as a mechanism cells use to divide and there is new evidence demonstrating the role and impact of AMBRA1 as a candidate for the treatment of several disorders and diseases, including anticancer therapy. It is known to suppress tumors and plays a role in mitophagy and apoptosis. AMBRA1 can be found in the cytoskeleton and mitochondria and during the process of autophagy, it is localized at the endoplasmic reticulum. In normal conditions, AMBRA1 is dormant and will bind to BCL2 in the outer membrane. This relocation enables autophagosome nucleation. AMBRA1 protein is involved in several cellular processes and is involved in the regulation of the immune system and nervous system.

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References

  1. ↑ "14 Academy Fellows elected to the Royal Society in 2017 | the Academy of Medical Sciences".
  2. 1 2 "EMBO people: David C. Rubinsztein". people.embo.org.
  3. 1 2 3 Anon (2017). "Professor David Rubinsztein FRS". London: royalsociety.org.
  4. 1 2 3 David C. Rubinsztein publications indexed by Google Scholar OOjs UI icon edit-ltr-progressive.svg
  5. 1 2 Anon (2004). "Professor David Rubinsztein FMedSci". acmedsci.ac.uk. London: Academy of Medical Sciences. Archived from the original on 4 March 2016. Retrieved 26 November 2015.
  6. 1 2 "Professor David C. Rubinsztein". University of Cambridge.[ permanent dead link ]
  7. ↑ "Professor David Rubinsztein :: Cambridge Neuroscience". www.neuroscience.cam.ac.uk. Retrieved 8 January 2018.
  8. ↑ F1000 Prime Faculty Member
  9. ↑ Research Gate
  10. ↑ "Publication analysis 2007–2013, Cell Biology" (PDF). Archived from the original (PDF) on 4 March 2016. Retrieved 26 November 2015.
  11. ↑ "Centre for Science and Policy". University of Cambridge.
  12. ↑ Renna, M.; Jimenez-Sanchez, M.; Sarkar, S.; Rubinsztein, D. C. (2010). "Chemical Inducers of Autophagy That Enhance the Clearance of Mutant Proteins in Neurodegenerative Diseases". Journal of Biological Chemistry . 285 (15): 11061–11067. doi: 10.1074/jbc.R109.072181 . ISSN   0021-9258. PMC   2856980 . PMID   20147746. Open Access logo PLoS transparent.svg
  13. ↑ Renna, M.; Jimenez-Sanchez, M.; Sarkar, S.; Rubinsztein, D. C. (2010). "Chemical Inducers of Autophagy That Enhance the Clearance of Mutant Proteins in Neurodegenerative Diseases". The Journal of Biological Chemistry. 285 (15): 11061–11067. doi: 10.1074/jbc.R109.072181 . PMC   2856980 . PMID   20147746.
  14. ↑ Rubinsztein, D. C. (2012). "Autophagy modulation as a potential therapeutic target for diverse diseases". Nature Reviews Drug Discovery . 11 (9): 709–730. doi:10.1038/nrd3802. PMC   3518431 . PMID   22935804.
  15. ↑ Ravikumar, B.; Rubinsztein, D. C. (2004). "Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease". Nature Genetics . 36 (6): 585–595. doi: 10.1038/ng1362 . PMID   15146184.
  16. ↑ Analytics, Clarivate. "David Rubinsztein Interview - Special Topic of Autophagy - ScienceWatch.com". archive.sciencewatch.com. Retrieved 8 January 2018.
  17. ↑ Davies, J. E.; Rubinsztein, D. C. (2005). "Doxycycline attenuates and delays toxicity of the oculopharyngeal muscular dystrophy mutation in transgenic mice". Nature Medicine . 11 (6): 672–677. doi:10.1038/nm1242. PMID   15864313. S2CID   13190118.
  18. ↑ Sarkar, S.; Rubinsztein, D. C. (2007). "Small molecules enhance autophagy and reduce toxicity in Huntington's disease models". Nature Chemical Biology. 3 (6): 331–338. doi:10.1038/nchembio883. PMC   2635561 . PMID   17486044.
  19. ↑ Winslow, A. R.; Rubinsztein, D. C. (2010). "α-Synuclein impairs macroautophagy: implications for Parkinson's disease". The Journal of Cell Biology. 190 (6): 1023–1037. doi:10.1083/jcb.201003122. PMC   3101586 . PMID   20855506.
  20. ↑ Ravikumar, B.; Rubinsztein, D. C. (2005). "Dynein mutations impair autophagic clearance of aggregate-prone proteins". Nature Genetics. 37 (7): 771–776. doi:10.1038/ng1591. PMID   15980862. S2CID   7628772.
  21. ↑ Ravikumar, B.; Rubinsztein, D. C. (2010). "Plasma membrane contributes to the formation of pre-autophagosomal structures". Nature Cell Biology . 12 (8): 747–757. doi:10.1038/ncb2078. PMC   2923063 . PMID   20639872.
  22. ↑ Moreau, K.; Rubinsztein, D. C. (2011). "Autophagosome precursor maturation requires homotypic fusion". Cell . 146 (2): 303–317. doi:10.1016/j.cell.2011.06.023. PMC   3171170 . PMID   21784250.
  23. ↑ Puri, C.; Rubinsztein, D. C. (2013). "Diverse autophagosome membrane sources coalesce in recycling endosomes". Cell. 154 (6): 1285–1299. doi:10.1016/j.cell.2013.08.044. PMC   3791395 . PMID   24034251.
  24. ↑ Vicinanza, M.; Rubinsztein, D. C. (2015). "PI(5)P regulates autophagosome biogenesis". Molecular Cell. 57 (2): 219–234. doi:10.1016/j.molcel.2014.12.007. PMC   4306530 . PMID   25578879.
  25. ↑ Korolchuk, V. I.; Rubinsztein, D. C. (2011). "Lysosomal positioning coordinates cellular nutrient responses". Nature Cell Biology. 13 (4): 453–460. doi:10.1038/ncb2204. PMC   3071334 . PMID   21394080.
  26. ↑ "Autophagy, a guardian against neurodegeneration - Part 2 - David Rubinsztein". SENS Research Foundation. 27 November 2013. Archived from the original on 8 December 2015. Retrieved 8 January 2018.
  27. ↑ "Wellcome Trust". Archived from the original on 2 October 2015. Retrieved 26 November 2015.
  28. ↑ "Editor biographies". Nature.
  29. ↑ "Funded People and Projects - Grant Funding | Wellcome".
  30. 1 2 Thomson Reuters
  31. ↑ "Labtimes: Publication Statistics: Cell Biology". Archived from the original on 29 July 2017. Retrieved 12 April 2016.
  32. ↑ "2017 Award Winners". biochemistry.org. Archived from the original on 4 June 2016. Retrieved 12 April 2016.
  33. ↑ "Highly Cited Researchers - the Most Influential Scientific Minds".
  34. ↑ "Highly Cited Researchers".
  35. ↑ "Main Programme 212th Scientific Meeting of the Pathological Society of Great Britain & Ireland".[ permanent dead link ]
  36. ↑ "Highly Cited Researchers".
  37. ↑ "Highly Cited Researchers". Archived from the original on 24 November 2021. Retrieved 24 November 2021.
  38. ↑ "Member > Rubinsztein David".
  39. ↑ "Highly Cited Researchers".
  40. ↑ "Highly Cited Researchers".
  41. ↑ "Scientific Research Award Recipients".
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