Linked Life Data

11758564

Source:http://linkedlifedata.com/resource/pubmed/id/11758564

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pubmed-article:11758564pubmed:abstractTextRecent investigations of the biochemistry, physiology and molecular genetics of polar auxin transport have greatly advanced our understanding of the process and of the part it plays in the regulation of development and in the responses of cells, tissues and organs to internal and external stimuli. The molecular and physiological characterization of mutants which exhibit lesions in polar auxin transport has led to the isolation and sequencing of genes which encode putative components of auxin carrier systems, or proteins which directly or indirectly regulate these systems. This work has revealed that specific auxin uptake and efflux carriers are coded not by single genes, but by whole families of genes, the expression of which is tissue or stimulus specific. Furthermore, evidence is accumulating rapidly that at least the auxin efflux carrier is a multi-component system consisting of both catalytic and regulatory subunits, including a separate phytotropin-binding protein. Other genes have been tentatively identified which code proteins that regulate the expression of genes coding auxin carrier components, or which regulate the intracellular traffic or activity of auxin carriers. Investigations of the turn-over and Golgi-mediated trafficking of auxin carrier proteins have revealed that essential components of at least the efflux carrier have a very short half-life in the plasma membrane and are replaced without the need for concurrent protein synthesis, leading to speculation that they might cycle between internal stores and the plasma membrane. The way is now clear for the development of specific molecular probes with which to investigate the intracellular transport and targeting of auxin carrier proteins.lld:pubmed
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pubmed-article:11758564pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:11758564pubmed:articleTitleTransmembrane auxin carrier systems--dynamic regulators of polar auxin transport.lld:pubmed
pubmed-article:11758564pubmed:affiliationCell Sciences Division, School of Biological Sciences, University of Southampton, Southampton, UK. dam3@soton.ac.uklld:pubmed
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