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Novel isoform of the Xenopus tropicalis PKA catalytic alpha subunit: An example of alternative splicing
Authors:Mohammad Tabish  Vladimir I. Rodionov
Affiliation:1. Biology Department, Università di Firenze, Italy;2. Department of Public Health & Infectious Diseases, Laboratory Affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, University of Rome “Sapienza”, Rome, Italy;3. CISM, Mass Spectrometry Centre, Università di Firenze, Italy;4. Departments of Biological Sciences and Pharmacology, Vanderbilt University, Nashville, USA;1. Department of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, USA;2. Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, USA;1. Linus Pauling Institute, Oregon State University, Corvallis, OR 97331, USA;2. Molecular and Cellular Biology Program, Oregon State University, Corvallis, OR 97331, USA;3. Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, OR 97331, USA;4. Environmental Health Sciences Center, Oregon State University, Corvallis, OR 97331, USA;5. School of Biological and Population Health Sciences, Oregon State University, Corvallis, OR 97331, USA;1. Department of Physiological Sciences and Center for Environmental and Human Toxicology, University of Florida, Gainesville, FL 32611, USA;2. Department of Civil and Environmental Engineering and Nicholas School of the Environment, Duke University, Durham, NC 27708, USA;3. Department of Environmental and Global Health and Center for Environmental and Human Toxicology, University of Florida, Gainesville, FL 32611, USA
Abstract:The cAMP-dependent protein kinase (PKA) plays key roles in the control of various aspects of eukaryotic cellular activities by phosphorylating several proteins and is multifunctional in nature. In the case of frog, Xenopus tropicalis, a gene encoding the PKA catalytic alpha subunit has been identified which encodes a single protein. Here we report the occurrence of N-terminal alternative splicing events in X. tropicalis tadpole that, in addition to generating a myristoylatable isoforms, also generate the non-myristoylated variant of the catalytic alpha subunit as has been reported in various other organisms. In addition to the already characterized exon 1, the 5′ untranslated region and first intron actually contains one more other exon, that is alternatively spliced on to exon 2 at the 5′ end of the pre-mRNA. This N-terminal alternative splicing occurs in combination with already characterized all internal exons. Thus, X. tropicalis tadpole expresses at least two different isoforms of the catalytic alpha subunit of PKA. The significance of this structural diversity in the family of PKA catalytic subunits is discussed.
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