Ph.D. University of Minnesota, Twin Cities, U.S.A.
B.Sc. Universidad de Los Andes, Bogota, Colombia.
Our lab is interested in the study of a novel family of channel-forming proteins, called Pannexins (Panx1, Panx2 and Panx3) that were discovered in the last decade based on their similarity to the invertebrate innexins. Although they were originally thought to be another family of gap junction proteins, we have established that their primary function is to form single membrane channels for release and uptake of ions and large molecules, such as ATP, involved in paracrine signaling. Pannexins are very important for cellular communication and are involved in early developmental events in many systems, including skin, cartilage, bone, vasculature and central nervous system, where they regulate proliferation and differentiation of different cell types. However, when expressed in adult tissues, pannexins can also have detrimental effects, for instance, facilitating cell death under ischemic conditions and malignant transformation in melanomas.
S. Penuela, Simek J, Thompson R. (2014). Regulation of pannexin channels by post-translational modifications. FEBS Letters. 588(8):1411-5.
S. Penuela S, L. Harland, J. Simek, D.W. Laird. (2014). Pannexin channels and their links to human disease. Biochemical Journal. 461(3):371-81.
S. Langlois, X. Xiang, K. Young, B.J. Cowan, S. Penuela, K.N. Cowan. (2014). Pannexin 1 and pannexin 3 channels regulate skeletal muscle myoblast proliferation and differentiation. Journal of Biological Chemistry 289(44):30717-31.
A. Boyd-Tressler, S. Penuela, D.W. Laird, G.R. Dubyak. (2014). Chemotherapeutic drugs induce ATP release via caspase-gated pannexin-1 channels and a caspase/pannexin-1-independent mechanism. Journal of Biological Chemistry 289(39):27246-63.
S. Penuela, J.J. Kelly, J.M. Churko, K. Barr, A.C. Berger and D.W. Laird (2014). Panx1 regulates cellular properties of keratinocytes and dermal fibroblasts in skin development and wound healing. Journal of Investigative Dermatology 134: 2026-2035.
S. Penuela, A. Lohman, W. Lai, L. Gyenis, D.W. Litchfield, B. Isakson and D.W. Laird (2014) Diverse post-translational modifications of the pannexin family of channel-forming proteins. Channels 8:124-130.
S. Penuela, R. Gehi and D.W. Laird (2013) The biochemistry and function of pannexin channels. BBA-Biomembranes 1828:15-22.
S. Penuela, L. Gyenis, A. Ablack, J. Churko, A. Berger, D.W. Litchfield, J.D. Lewis and D.W. Laird (2012) . Loss of pannexin1 attenuates melanoma progression by reversion to a melanocytic phenotype. Journal of Biological Chemistry 287: 29184-29193. Highlighted in press releases by CTV News, Western Research and the London Free Press.
S. Penuela and D.W. Laird (2012) .The cellular life of Pannexins. WIREs Membrane Transport and Signaling 1:621-632, doi:10.1002/wmts.63
M. Billaud, A.W. Lohman, A.C. Straub, R. Looft-Wilson, C.A. Araj, A.K. Best, F. Chekeni, K. Ravichandran, S. Penuela, D.W. Laird and B.E. Isakson (2011). Pannexin1 regulates a1-adrenoreceptor-mediated vasoconstriction. Circulation Research 109: 80-85.
R. Bhalla-Gehi, S. Penuela, J.M. Churko, Q. Shao and D.W. Laird (2010). Pannexin1 and Pannexin3 delivery, cell surface dynamics and cytoskeletal interactions. Journal of Biological Chemistry 285: 9147-9160.
S.J. Celetti, K.N. Cowan, S. Penuela, Q. Shao and D.W. Laird (2010). Implications of pannexin 1 and Pannexin 3 for keratinocyte differentiation. Journal of Cell Science 123: 1363-1372.
F.B. Chekeni, M.R. Elliot, J.K. Sandilo, S.F. Walk, J.M. Kinchen, E.R. Lararowski, A.J. Armstrong, S. Penuela, D.W. Laird, G.S. Salvesen, B.E. Isakson, D.A. Bayliss and K.S. Ravichandran (2010). Pannexin 1 channels regulate “find-me” signal release and membrane permeability during apoptosis. Nature 467:863-867.
S. Penuela, R. Bhalla, K. Nag and D.W. Laird (2009). Glycosylation regulates pannexin intermixing and cellular localization. Molecular Biology of the Cell 20:4313-4323.
S. Penuela, R. Bhalla, Q. Shao and D.W. Laird (2007). Pannexin1 and pannexin3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins. Journal of Cell Science 120: 3772-3783.