Lipid anchoring of Arabidopsis phototropin 1 to assess the functional significance of receptor internalization : should I stay or should I go?

© 2015 The Authors. New Phytologist © 2015 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 206(2015), 3 vom: 23. Mai, Seite 1038-1050
1. Verfasser: Preuten, Tobias (VerfasserIn)
Weitere Verfasser: Blackwood, Lisa, Christie, John M, Fankhauser, Christian
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana farnesylation internalization myristoylation phototropin 1 (phot1) phototropism receptor turnover subcellular localization mehr... Arabidopsis Proteins Lipid-Linked Proteins Phosphoproteins Phototropins NPH1 protein, Arabidopsis EC 2.7.11.1 Protein Serine-Threonine Kinases
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520 |a The phototropin 1 (phot1) blue light receptor mediates a number of adaptive responses, including phototropism, that generally serve to optimize photosynthetic capacity. Phot1 is a plasma membrane-associated protein, but upon irradiation, a fraction is internalized into the cytoplasm. Although this phenomenon has been reported for more than a decade, its biological significance remains elusive. Here, we use a genetic approach to revisit the prevalent hypotheses regarding the functional importance of receptor internalization. Transgenic plants expressing lipidated versions of phot1 that are permanently anchored to the plasma membrane were used to analyse the effect of internalization on receptor turnover, phototropism and other phot1-mediated responses. Myristoylation and farnesylation effectively prevented phot1 internalization. Both modified photoreceptors were found to be fully functional in Arabidopsis, rescuing phototropism and all other phot1-mediated responses tested. Light-mediated phot1 turnover occurred as in the native receptor. Furthermore, our work does not provide any evidence of a role of phot1 internalization in the attenuation of receptor signalling during phototropism. Our results demonstrate that phot1 signalling is initiated at the plasma membrane. They furthermore indicate that release of phot1 into the cytosol is not linked to receptor turnover or desensitization 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Arabidopsis thaliana 
650 4 |a farnesylation 
650 4 |a internalization 
650 4 |a myristoylation 
650 4 |a phototropin 1 (phot1) 
650 4 |a phototropism 
650 4 |a receptor turnover 
650 4 |a subcellular localization 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Lipid-Linked Proteins  |2 NLM 
650 7 |a Phosphoproteins  |2 NLM 
650 7 |a Phototropins  |2 NLM 
650 7 |a NPH1 protein, Arabidopsis  |2 NLM 
650 7 |a EC 2.7.11.1  |2 NLM 
650 7 |a Protein Serine-Threonine Kinases  |2 NLM 
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700 1 |a Blackwood, Lisa  |e verfasserin  |4 aut 
700 1 |a Christie, John M  |e verfasserin  |4 aut 
700 1 |a Fankhauser, Christian  |e verfasserin  |4 aut 
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