Raul Padron

University of Massachusetts Medical School

Election Year: 2018
Primary Section: 42, Medical Physiology and Metabolism
Secondary Section: 29, Biophysics and Computational Biology
Membership Type: International Member
Photo Credit: Marie Craig


Raúl Padrón is a structural biologist recognized for his work on the structure and function of myosin thick filaments of skeletal, cardiac and smooth muscle. He is known particularly for his studies on the myosin interacting-head motif (IHM) structure and function and their  implications on how muscle thick filaments relax, super-relax and become activated, and its consequences on the molecular pathogenesis of human muscle diseases like hypertrophic and dilated cardiomyopathy. Padrón was born and grew up in Caracas, Venezuela. He graduated from the Universidad Central de Venezuela with a degree in Electrical Engineering and from the Venezuelan Institute for Scientific Research with a M. Sc. in Biology and a summa cum laude Ph.D. in Biophysics and Physiology in 1979. He was a postdoctoral fellow in muscle structure and function at the  MRC Laboratory of Molecular Biology (Cambridge, U.K.) in 1980 and joined the Venezuelan Institute for Scientific Research in 1983, where he founded the Center of Structural Biology, been an International Research Scholar of the Howard Hughes Medical Institute (HHMI) from 1997 until 2011. He is an elected member of the Latin American Academy of Sciences (ACAL), the World Academy of Sciences (TWAS) and an elected foreign associate of the National Academy of Sciences.

Research Interests

Raúl Padrón´s laboratory is interested in the muscle thick filament structure, function and evolution and their implications on human disease. With his collaborators they found by cryo-electron microscopy that in thick filaments of tarantula muscle the two heads of myosin form an asymmetric arrangement they called the myosin interacting-heads motif (IHM), where both heads ATPases were inhibited explaining relaxation. They have demonstrated that the IHM is conserved since before animals emerged, independently of the muscle type (striated, cardiac or smooth) or in nonmuscle cells. This conservation demonstrated the fundamental importance of the IHM as the structural basis underlying relaxation through both heads ATPase inhibition, implying ATP energy-saving via a super-relaxation mechanism. They have proposed a cooperative phosphorylation activation mechanism that explains potentiation and post-tetanic potentiation on tarantula contracting muscles. They found that mutations of hypertrophic cardiomyopathy cluster on human cardiac IHM intramolecular interactions accounting for hypercontractility, reduced diastolic relaxation, and increased energy consumption. To further these studies they are focusing on elucidating by single particle cryo-electron microscopy the near atomic structure of the IHM from skeletal, smooth and cardiac muscle, and nonmuscle cells.

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