Structural diversity of eukaryotic protein tyrosine phosphatases: functional and evolutionary implications |
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| Affiliation: | 1. Department of Geology, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran;2. Department of Earth and Environmental Sciences, The University of Manchester, Manchester, UK;3. Earth Sciences Department, Faculty of Science, Vrije Universiteit Amsterdam, Amsterdam, the Netherlands;4. National Iranian South Oil Company, Ahvaz, Iran;1. Key Laboratory of Marine Sedimentology and Environmental Geology, First Institute of Oceanography, Ministry of Natural Resources, Qingdao 266061, China;2. Laboratory for Marine Geology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266061, China;3. Key Laboratory of Marine Hydrocarbon Resources and Environmental Geology, Ministry of Land and Resources, Qingdao Institute of Marine Geology, Qingdao 266071, China |
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| Abstract: | In the past few years, very rapid advances have been made in determining the primary structure of protein tyrosine phosphatases (PTPases). PTPase genes have now been isolated from bacteria, viruses, yeasts and insects as well as vertebrates. The cytosolic PTPases have a catalytic domain associated with various accessory domains that are believed to be involved in protein-protein interaction or subcellular localization. The transmembrane PTPases have either one or two cytoplasmic PTPase domains and an extracellular receptor-like structure. The existence of a large number of structurally diverse PTPases suggests that they play specific and crucial roles in signal transduction. In this article, the structural features of the PTPases from higher eukaryotes are reviewed. |
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