Samara Reck-Peterson

Last updated
Samara Reck-Peterson
Born1971 (age 53–54)
Seattle, Washington
Known forStudies of the motor protein dynein
Scientific career
Institutions Harvard Medical School
University of California, San Diego
Howard Hughes Medical Institute
Thesis Functional, Biochemical and Biophysical Characterization of Myo2p, a Class V Myosin of the Yeast Saccharomyces cerevisiae
Doctoral advisor Mark Mooseker and Peter Novick
Other academic advisors Ronald Vale

Samara Reck-Peterson is an American cell biologist and biophysicist. She is a Professor of Cellular and Molecular Medicine and Cell and Developmental Biology at the University of California, San Diego and an Investigator of the Howard Hughes Medical Institute. She is known for her contributions to our understanding of how dynein, an exceptionally large motor protein that moves many intracellular cargos, [1] works and is regulated. She developed one of the first systems to produce recombinant dynein [2] and discovered that, unlike other cytoskeletal motors, dynein can take a wide variety of step sizes, forward and back and even sideways. [2] [3] She lives in San Diego, California.

Contents

Early life and education

Reck-Peterson was educated at Litchfield High School in Litchfield, Minnesota, where she served as senior class president and graduated as salutatorian in 1989. She was an all-state track and cross-country runner and team captain. [4] She was inducted into the Litchfield High School Hall of Fame in 2017. [4]

Career

Reck-Peterson became interested in molecular motors when she took the Physiology Course at the Marine Biological Laboratory at Woods Hole, Massachusetts. She chose the motor protein myosin as the topic of her Ph.D. work in the laboratories of Mark Mooseker and Peter Novick at Yale University. Her work focused on the class V myosins, which have multiple functions in the cell ranging from mRNA transport to cell polarity and membrane trafficking. [5] She developed a modified in vitro motility assay to show that both Myo2p and Myo4p class V myosins in yeast appear to be non-processive motors in the absence of additional regulation, unlike their vertebrate counterparts. [6]

In 2001, Reck-Peterson moved to UCSF to pursue post-doctoral studies with Ronald Vale. She began to work on dynein, a molecular motor that transports cargoes such as proteins, organelles and messenger RNAs to locations where they are needed in the cell. Dynein uses the energy stored in ATP to move towards the "minus end" of microtubules. Defects in dyneins and their regulatory proteins lead to neurodevelopmental and neurodegenerative diseases, showing the importance of microtubule-based transport in long cells such as neurons. [7] Reck-Peterson used single-molecule techniques to examine the stepping behavior of dynein, finding that isolated dynein can step forwards, backwards and even sideways. [2]

In 2007, Reck-Peterson joined the Department of Cell Biology at Harvard Medical School as an assistant professor. She continued to study the mechanism of dynein-mediated transport. [8] Using DNA origami, she created artificial cargos that could be programmed to load onto multiple types of motors, and used these to create competition, or a "tug of war", between motors. [9] She used an assay for long-distance microtubule-based transport in the long, highly polarized hyphae of Aspergillus nidulans [10] to show that Lis-1 is an initiation factor for dynein-mediated transport, [11] and to show that some cargos of microtubule-based motors hitchhike on others. [12] Mutants in the gene encoding Lis-1 are one cause of lissencephaly, a severe brain disorder. In collaboration with Andres Leschziner, she showed that Lis-1 regulates the interaction between dynein and the microtubule in two different ways, [13] [14] and determined the structural basis for the switch between microtubule binding and microtubule release. [15]

In 2015 Reck-Peterson moved to the University of California, San Diego, [16] and in 2018 she became an Investigator of the Howard Hughes Medical Institute. [17]

Awards

Related Research Articles

<span class="mw-page-title-main">Microtubule</span> Polymer of tubulin that forms part of the cytoskeleton

Microtubules are polymers of tubulin that form part of the cytoskeleton and provide structure and shape to eukaryotic cells. Microtubules can be as long as 50 micrometres, as wide as 23 to 27 nm and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin into protofilaments that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement.

<span class="mw-page-title-main">Cilium</span> Organelle found on eukaryotic cells

The cilium is a short hair-like membrane protrusion from many types of eukaryotic cell. The cilium has the shape of a slender threadlike projection that extends from the surface of the much larger cell body. Eukaryotic flagella found on sperm cells and many protozoans have a similar structure to motile cilia that enables swimming through liquids; they are longer than cilia and have a different undulating motion.

<span class="mw-page-title-main">Cytoskeleton</span> Network of filamentous proteins that forms the internal framework of cells

The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. In eukaryotes, it extends from the cell nucleus to the cell membrane and is composed of similar proteins in the various organisms. It is composed of three main components: microfilaments, intermediate filaments, and microtubules, and these are all capable of rapid growth and or disassembly depending on the cell's requirements.

<span class="mw-page-title-main">Kinesin</span> Eukaryotic motor protein

A kinesin is a protein complex belonging to a class of motor proteins found in eukaryotic cells. Kinesins move along microtubule (MT) filaments and are powered by the hydrolysis of adenosine triphosphate (ATP). The active movement of kinesins supports several cellular functions including mitosis, meiosis and transport of cellular cargo, such as in axonal transport, and intraflagellar transport. Most kinesins walk towards the plus end of a microtubule, which, in most cells, entails transporting cargo such as protein and membrane components from the center of the cell towards the periphery. This form of transport is known as anterograde transport. In contrast, dyneins are motor proteins that move toward the minus end of a microtubule in retrograde transport.

<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">Molecular motor</span> Biological molecular machines

Molecular motors are natural (biological) or artificial molecular machines that are the essential agents of movement in living organisms. In general terms, a motor is a device that consumes energy in one form and converts it into motion or mechanical work; for example, many protein-based molecular motors harness the chemical free energy released by the hydrolysis of ATP in order to perform mechanical work. In terms of energetic efficiency, this type of motor can be superior to currently available man-made motors. One important difference between molecular motors and macroscopic motors is that molecular motors operate in the thermal bath, an environment in which the fluctuations due to thermal noise are significant.

<span class="mw-page-title-main">Motor protein</span> Class of molecular proteins

Motor proteins are a class of molecular motors that can move along the cytoskeleton of cells. They convert chemical energy into mechanical work by the hydrolysis of ATP. Flagellar rotation, however, is powered by a proton pump.

<span class="mw-page-title-main">PAFAH1B1</span> Protein-coding gene in the species Homo sapiens

Platelet-activating factor acetylhydrolase IB subunit alpha or Lisencephaly protein-1 (LIS-1) is an enzyme that in humans is encoded by the PAFAH1B1 gene. The protein plays an important role in regulating the motor protein dynein.

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

Unconventional myosin-Va is a motor protein in charge of the intracellular transport of vesicles, organelles and protein complexes along the actin filaments. In humans it is coded for by the MYO5A gene.

<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">DYNLL1</span> Protein-coding gene in humans

Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the DYNLL1 gene.

<span class="mw-page-title-main">NDEL1</span> Protein-coding gene in the species Homo sapiens

Nuclear distribution protein nudE-like 1 is a protein that in humans is encoded by the NDEL1 gene.

<span class="mw-page-title-main">DYNC1H1</span> Protein-coding gene in the species Homo sapiens

Cytoplasmic dynein 1 heavy chain 1 is a protein that in humans is encoded by the DYNC1H1 gene. Dynein is a molecular motor protein that is responsible for the transport of numerous cellular cargoes to minus ends of microtubules, which are typically found in the center of a cell, or the cell body of neurons. It is located on the 14th chromosome at position 14q32.31. Cytoplasmic dynein transports cargoes along the axon in the retrograde direction, bringing materials from the axon to the cell body. Dynein heavy chain binds microtubules and hydrolyzes ATP at its C-terminal head. It binds cargo via interaction with other dynein subunits at its N-terminal tail.

<span class="mw-page-title-main">Ronald Vale</span> American biochemist

Ronald David Vale ForMemRS is an American biochemist and cell biologist. He is a professor at the Department of Cellular and Molecular Pharmacology, University of California, San Francisco. His research is focused on motor proteins, particularly kinesin and dynein. He was awarded the Canada Gairdner International Award for Biomedical Research in 2019, the Shaw Prize in Life Science and Medicine in 2017 together with Ian Gibbons, and the Albert Lasker Award for Basic Medical Research in 2012 alongside Michael Sheetz and James Spudich. He is a fellow of the American Academy of Arts and Sciences and a member of the National Academy of Sciences. He was the president of the American Society for Cell Biology in 2012. He has also been an investigator at the Howard Hughes Medical Institute since 1995. In 2019, Vale was named executive director of the Janelia Research Campus and a vice president of HHMI; his appointment began in early 2020.

<span class="mw-page-title-main">KIF15</span> Protein-coding gene in the species Homo sapiens

Kinesin family member 15 is a protein that in humans is encoded by the KIF15 gene.

<span class="mw-page-title-main">Intracellular transport</span> Directed movement of vesicles and substances within a cell

Intracellular transport is the movement of vesicles and substances within a cell. Intracellular transport is required for maintaining homeostasis within the cell by responding to physiological signals. Proteins synthesized in the cytosol are distributed to their respective organelles, according to their specific amino acid’s sorting sequence. Eukaryotic cells transport packets of components to particular intracellular locations by attaching them to molecular motors that haul them along microtubules and actin filaments. Since intracellular transport heavily relies on microtubules for movement, the components of the cytoskeleton play a vital role in trafficking vesicles between organelles and the plasma membrane by providing mechanical support. Through this pathway, it is possible to facilitate the movement of essential molecules such as membrane‐bounded vesicles and organelles, mRNA, and chromosomes.

<span class="mw-page-title-main">Ian R. Gibbons</span> English biophysicist and cell biologist

Ian Read Gibbons, was a biophysicist and cell biologist. He discovered and named dynein, and demonstrated energy source as ATP is sufficient for dynein to walk on microtubules. In 2017, he and Ronald Vale received the Shaw Prize for their research on microtubule motor proteins.

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

Neurotubules are microtubules found in neurons in nervous tissues. Along with neurofilaments and microfilaments, they form the cytoskeleton of neurons. Neurotubules are undivided hollow cylinders that are made up of tubulin protein polymers and arrays parallel to the plasma membrane in neurons. Neurotubules have an outer diameter of about 23 nm and an inner diameter, also known as the central core, of about 12 nm. The wall of a neurotubule is about 5 nm in width. There is a non-opaque clear zone surrounding the neurotubule and it is about 40 nm in diameter. Like microtubules, neurotubules are greatly dynamic and their length can be adjusted by polymerization and depolymerization of tubulin.

<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. ↑ Reck-Peterson, Samara L.; Redwine, William B.; Vale, Ronald D.; Carter, Andrew P. (2018). "The cytoplasmic dynein transport machinery and its many cargoes" (PDF). Nature Reviews Molecular Cell Biology. 19 (6): 382–398. doi:10.1038/s41580-018-0004-3. ISSN   1471-0080. PMC   6457270 . PMID   29662141.
  2. 1 2 3 Reck-Peterson, Samara L.; Yildiz, Ahmet; Carter, Andrew P.; Gennerich, Arne; Zhang, Nan; Vale, Ronald D. (2006). "Single-Molecule Analysis of Dynein Processivity and Stepping Behavior". Cell. 126 (2): 335–348. doi:10.1016/j.cell.2006.05.046. PMC   2851639 . PMID   16873064.
  3. ↑ Qiu, Weihong; Derr, Nathan D.; Goodman, Brian S.; Villa, Elizabeth; Wu, David; Shih, William; Reck-Peterson, Samara L. (2012-01-08). "Dynein achieves processive motion using both stochastic and coordinated stepping". Nature Structural & Molecular Biology. 19 (2): 193–200. doi:10.1038/nsmb.2205. ISSN   1545-9985. PMC   3272163 . PMID   22231401.
  4. 1 2 O'Connor, Molly. "LHS Hall of Fame inducts three". Crow River Media. Retrieved 2019-03-08.
  5. ↑ Reck-Peterson, S. L.; Provance, D. W.; Mooseker, M. S.; Mercer, J. A. (2000-03-17). "Class V myosins". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1496 (1): 36–51. doi:10.1016/s0167-4889(00)00007-0. ISSN   0006-3002. PMID   10722875.
  6. ↑ Reck-Peterson, S. L.; Tyska, M. J.; Novick, P. J.; Mooseker, M. S. (2001-05-28). "The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin-based motors". The Journal of Cell Biology. 153 (5): 1121–1126. doi:10.1083/jcb.153.5.1121. ISSN   0021-9525. PMC   2174330 . PMID   11381095.
  7. ↑ Hirokawa, Nobutaka; Niwa, Shinsuke; Tanaka, Yosuke (2010). "Molecular Motors in Neurons: Transport Mechanisms and Roles in Brain Function, Development, and Disease". Neuron. 68 (4): 610–638. doi: 10.1016/j.neuron.2010.09.039 . PMID   21092854.
  8. ↑ Qiu, Weihong; Derr, Nathan D; Goodman, Brian S; Villa, Elizabeth; Wu, David; Shih, William; Reck-Peterson, Samara L (2012). "Dynein achieves processive motion using both stochastic and coordinated stepping". Nature Structural & Molecular Biology. 19 (2): 193–200. doi:10.1038/nsmb.2205. ISSN   1545-9993. PMC   3272163 . PMID   22231401.
  9. ↑ Derr, N. D.; Goodman, B. S.; Jungmann, R.; Leschziner, A. E.; Shih, W. M.; Reck-Peterson, S. L. (2012-11-02). "Tug-of-war in motor protein ensembles revealed with a programmable DNA origami scaffold". Science. 338 (6107): 662–665. Bibcode:2012Sci...338..662D. doi:10.1126/science.1226734. ISSN   1095-9203. PMC   3840815 . PMID   23065903.
  10. ↑ Egan, Martin J.; McClintock, Mark A.; Reck-Peterson, Samara L. (2012). "Microtubule-based transport in filamentous fungi". Current Opinion in Microbiology. 15 (6): 637–645. doi:10.1016/j.mib.2012.10.003. ISSN   1879-0364. PMC   3518651 . PMID   23127389.
  11. ↑ Egan, Martin J.; Tan, Kaeling; Reck-Peterson, Samara L. (2012-06-25). "Lis1 is an initiation factor for dynein-driven organelle transport". The Journal of Cell Biology. 197 (7): 971–982. doi:10.1083/jcb.201112101. ISSN   0021-9525. PMC   3384415 . PMID   22711696.
  12. ↑ Salogiannis, John; Egan, Martin J.; Reck-Peterson, Samara L. (2016-02-01). "Peroxisomes move by hitchhiking on early endosomes using the novel linker protein PxdA". The Journal of Cell Biology. 212 (3): 289–296. doi:10.1083/jcb.201512020. ISSN   1540-8140. PMC   4748578 . PMID   26811422.
  13. ↑ Huang, Julie; Roberts, Anthony J.; Leschziner, Andres E.; Reck-Peterson, Samara L. (2012-08-31). "Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor". Cell. 150 (5): 975–986. doi:10.1016/j.cell.2012.07.022. ISSN   1097-4172. PMC   3438448 . PMID   22939623.
  14. ↑ DeSantis, Morgan E.; Cianfrocco, Michael A.; Htet, Zaw Min; Tran, Phuoc Tien; Reck-Peterson, Samara L.; Leschziner, Andres E. (2017-09-07). "Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein". Cell. 170 (6): 1197–1208.e12. doi:10.1016/j.cell.2017.08.037. ISSN   1097-4172. PMC   5625841 . PMID   28886386.
  15. ↑ Redwine, W. B.; Hernandez-Lopez, R.; Zou, S.; Huang, J.; Reck-Peterson, S. L.; Leschziner, A. E. (2012-09-21). "Structural basis for microtubule binding and release by dynein". Science. 337 (6101): 1532–1536. Bibcode:2012Sci...337.1532R. doi:10.1126/science.1224151. ISSN   1095-9203. PMC   3919166 . PMID   22997337.
  16. ↑ "Samara Reck-Peterson". biology.ucsd.edu. Retrieved 2019-03-10.
  17. ↑ "HHMI Bets Big On 19 New Investigators". HHMI.org. Retrieved 2019-03-10.
  18. ↑ "2016 Faculty Scholars". 2016 Faculty Scholars. Retrieved 2019-03-10.
  19. ↑ "Molecular & Cellular Biology - Harvard University". mcbpublic.unix.fas.harvard.edu. Retrieved 2019-03-10.
  20. ↑ "Women in Cell Biology Awards". ASCB. Retrieved 2019-03-10.
  21. ↑ "Excellence in Mentoring Awards Past Recipients". The Office for Diversity Inclusion and Community Partnership at Harvard Medical School. Retrieved 2019-03-10.
  22. ↑ "Armenise Grants Advance Junior Faculty Studies | Harvard Medical School". hms.harvard.edu. 3 September 2010. Retrieved 2019-03-10.
  23. ↑ "Years 2009 - Rita Allen Foundation" . Retrieved 2019-03-10.
  24. ↑ "NIH Director's New Innovator Award Program - 2008 Award Recipients | NIH Common Fund". commonfund.nih.gov. 18 September 2018. Retrieved 2019-03-10.
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