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Profile

Profile of Raúl Padrón

Jennifer Viegas
PNAS December 29, 2020 117 (52) 32830-32832; first published December 17, 2020; https://doi.org/10.1073/pnas.2015960117
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  • The myosin interacting-heads motif present in live tarantula muscle explains tetanic and posttetanic phosphorylation mechanisms
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Over the past four decades, structural biologist Raúl Padrón has elucidated muscle contraction at the molecular and atomic level using a model system that he and his colleague Roger Craig developed: tarantula skeletal muscle. Padrón’s research on how skeletal muscle thick filaments relax and become activated is helping to inform the molecular pathogenesis of human muscle diseases. For such advances, Padrón was elected as an international member of the National Academy of Sciences (NAS) in 2018; later, he emigrated to the United States due to his native Venezuela’s ongoing political crisis. Now a professor at the University of Massachusetts Medical School, Padrón answers longstanding questions in his Inaugural Article (1) concerning striated muscle contraction that shed light on its underlying mechanisms in invertebrates and vertebrates.

Raúl Padrón. Image credit: Marie Craig (photographer).

Home Laboratory at Age 11

Padrón was born in Caracas to a concert pianist mother and pharmacologist and microbiologist father. Through his mother he gained a strong work ethic. He was also greatly influenced by his father, who maintained a home laboratory. “I still remember my surprise when he showed me paramecia swimming under a microscope,” Padrón says. “Soon, I started raising yeast on chicken soup to see them under magnification.”

When he was 11 years old, Padrón was permitted to have a separate laboratory, where he did chemistry and biology experiments and built electronic equipment. He attended San Ignacio High School in Caracas, where mathematician Angel Urmeneta and biologist Raphael Bredy reinforced his academic interests. In 1966, Bredy suggested that Padrón visit the Venezuelan Institute for Scientific Research (IVIC). During the visit, he met biochemist Karl Gaede, whose laboratory he joined at age 16. Padrón says, “Under Gaede’s advice, I decided to study electrical engineering at the Central University of Venezuela, as he thought this would provide a good background for a …

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References

  1. ↵
    1. R. Padrón et al
    ., The myosin interacting-heads motif present in live tarantula muscle explains tetanic and posttetanic phosphorylation mechanisms. Proc. Natl. Acad. Sci. U.S.A. 117, 11865–11874 (2020).
    OpenUrlAbstract/FREE Full Text
  2. ↵
    1. R. Padrón,
    2. L. Mateu
    , In vivo structure of frog sciatic nerve myelin membranes: An X-ray diffraction study at 13A resolution. J. Neurosci. Res. 6, 251–260 (1981).
    OpenUrlPubMed
  3. ↵
    1. R. Padrón,
    2. H. E. Huxley
    , The effect of the ATP analogue AMPPNP on the structure of crossbridges in vertebrate skeletal muscles: X-ray diffraction and mechanical studies. J. Muscle Res. Cell Motil. 5, 613–655 (1984).
    OpenUrlPubMed
  4. ↵
    1. R. A. Crowther,
    2. R. Padrón,
    3. R. Craig
    , Arrangement of the heads of myosin in relaxed thick filaments from tarantula muscle. J. Mol. Biol. 184, 429–439 (1985).
    OpenUrlCrossRefPubMed
  5. ↵
    1. R. Padrón
    “Two and a half years at the LMB that imprinted my scientific career (1980–83)” in Memoirs and Consequences: Visiting Scientists at the MRC Laboratory of Molecular Biology, H. E. Huxley, Ed. (MRC Laboratory of Molecular Biology, Cambridge, 2013) Chapter 38, pp. 315–322.
  6. ↵
    1. J. L. Woodhead et al
    ., Atomic model of a myosin filament in the relaxed state. Nature 436, 1195–1199 (2005).
    OpenUrlCrossRefPubMed
  7. ↵
    1. L. Alamo et al
    ., Conserved intramolecular interactions maintain myosin interacting-heads motifs explaining tarantula muscle super-relaxed state structural basis. J. Mol. Biol. 428, 1142–1164 (2016).
    OpenUrlCrossRefPubMed
  8. ↵
    1. L. Alamo et al
    ., Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity. J. Mol. Biol. 384, 780–797 (2008).
    OpenUrlCrossRefPubMed
  9. ↵
    1. R. Brito et al
    ., A molecular model of phosphorylation-based activation and potentiation of tarantula muscle thick filaments. J. Mol. Biol. 414, 44–61 (2011).
    OpenUrlCrossRefPubMed
  10. ↵
    1. G. Sulbarán et al
    ., An invertebrate smooth muscle with striated muscle myosin filaments. Proc. Natl. Acad. Sci. U.S.A. 112, E5660–E5668 (2015).
    OpenUrlAbstract/FREE Full Text
  11. ↵
    1. M. E. Zoghbi,
    2. J. L. Woodhead,
    3. R. L. Moss,
    4. R. Craig
    , Three-dimensional structure of vertebrate cardiac muscle myosin filaments. Proc. Natl. Acad. Sci. U.S.A. 105, 2386–2390 (2008).
    OpenUrlAbstract/FREE Full Text
  12. ↵
    1. K. H. Lee et al
    ., Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals. Proc. Natl. Acad. Sci. U.S.A. 115, E1991–E2000 (2018).
    OpenUrlAbstract/FREE Full Text
  13. ↵
    1. L. Alamo et al
    ., Effects of myosin variants on interacting-heads motif explain distinct hypertrophic and dilated cardiomyopathy phenotypes. eLife 6, e24634 (2017).
    OpenUrlCrossRefPubMed
  14. ↵
    1. L. Alamo et al
    ., Lessons from a tarantula: New insights into muscle thick filament and myosin interacting-heads motif structure and function. Biophys. Rev. 9, 461–480 (2017).
    OpenUrl
  15. ↵
    1. L. Alamo,
    2. A. Pinto,
    3. G. Sulbarán,
    4. J. Mavárez,
    5. R. Padrón
    , Lessons from a tarantula: New insights into myosin interacting-heads motif evolution and its implications on disease. Biophys. Rev. 10, 1465–1477 (2018).
    OpenUrl
  16. ↵
    1. S. Yang et al
    ., Cryo-EM structure of the inhibited (10S) form of myosin II. Nature, doi:10.1038/s41586-020-3007-0 (2020).
    OpenUrlCrossRef

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Profile of Raúl Padrón
Jennifer Viegas
Proceedings of the National Academy of Sciences Dec 2020, 117 (52) 32830-32832; DOI: 10.1073/pnas.2015960117

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Jennifer Viegas
Proceedings of the National Academy of Sciences Dec 2020, 117 (52) 32830-32832; DOI: 10.1073/pnas.2015960117
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    • Home Laboratory at Age 11
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