Raul Padron

University of Massachusetts Medical School


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

Biosketch

Raúl Padrón, a Professor at the University of Massachusetts Medical School 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 research focus is on the structure, function and evolution of the myosin interacting-heads motif (IHM) and their implications on human disease. The IHM is established by the interactions of the two heads of the myosin molecule and its myosin tail subfragment-2, forming an asymmetric arrangement that inhibits the ATPases of both heads in the relaxed state. The IHM is conserved since before animals emerged, independently of the muscle type (striated, cardiac or smooth) or in non-muscle cells; showing its fundamental importance as the structural basis underlying relaxation through both heads ATPase inhibition, implying ATP energy-saving via a super-relaxation mechanism. Current focus is on: (1) the study by single-particle cryo-EM of the near atomic structure and function of the IHM from skeletal, smooth and cardiac muscle, and non-muscle cells, and of the IHM on thick filaments of invertebrate skeletal and vertebrate skeletal and cardiac muscle, aiming to understand the implications of the clustering of mutations on human diseases involving the IHM; (2) to study by time-resolved X-ray diffraction the structure and function of the blocked and free heads of the IHM in live relaxed and contracting muscle.

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