期刊文献+

Quantification of Membrane Protein Dynamics and Interactions in Plant Cells by Fluorescence Correlation Spectroscopy 被引量:2

Quantification of Membrane Protein Dynamics and Interactions in Plant Cells by Fluorescence Correlation Spectroscopy
原文传递
导出
摘要 Deciphering the dynamics of protein and lipid molecules on appropriate spatial and temporal scales may shed light on protein function and membrane organization. However, traditional bulk approaches cannot unambiguously quantify the extremely diverse mobility and interactions of proteins in living cells. Fluores- cence correlation spectroscopy (FCS) is a powerful technique to describe events that occur at the singlemolecule level and on the nanosecond to second timescales; therefore, FCS can provide data on the heterogeneous organization of membrane systems. FCS can also be combined with other microscopy techniques, such as super-resolution techniques. More importantly, FCS is minimally invasive, which makes it an ideal approach to detect the heterogeneous distribution and dynamics of key proteins during development. In this review, we give a brief introduction about the development of FCS and summarize the significant contributions of FCS in understanding the organization of plant cell membranes and the dy- namics and interactions of membrane proteins .We also discuss the potential applications of this technique in plant biology. Deciphering the dynamics of protein and lipid molecules on appropriate spatial and temporal scales may shed light on protein function and membrane organization. However, traditional bulk approaches cannot unambiguously quantify the extremely diverse mobility and interactions of proteins in living cells. Fluores- cence correlation spectroscopy (FCS) is a powerful technique to describe events that occur at the singlemolecule level and on the nanosecond to second timescales; therefore, FCS can provide data on the heterogeneous organization of membrane systems. FCS can also be combined with other microscopy techniques, such as super-resolution techniques. More importantly, FCS is minimally invasive, which makes it an ideal approach to detect the heterogeneous distribution and dynamics of key proteins during development. In this review, we give a brief introduction about the development of FCS and summarize the significant contributions of FCS in understanding the organization of plant cell membranes and the dy- namics and interactions of membrane proteins .We also discuss the potential applications of this technique in plant biology.
出处 《Molecular Plant》 SCIE CAS CSCD 2016年第9期1229-1239,共11页 分子植物(英文版)
关键词 fluorescence correlation spectroscopy MICRODOMAIN membrane protein DYNAMICS INTERACTION fluorescence correlation spectroscopy, microdomain, membrane protein, dynamics, interaction
  • 相关文献

参考文献1

二级参考文献78

  • 1Arkhipov, A., Shan, Y., Das, R., Endres, N.F., Eastwood, M.P., Wemmer, D.E., Kuriyan, J., and Shaw, D.E. (2013). Architecture and membrane interactions of the EGF receptor. Cell 152:557-569.
  • 2Bacia, K., Kim, S.A., and Schwille, P. (2006). Fluorescence cross- correlation spectroscopy in living cells. Nat. Methods 3:83-89.
  • 3Baisa, G., Mayers, J.R., and Bednarek, S.Y. (2013). Budding and braking news about clathrin-mediated endocytosis. Curr. Opin. Plant Biol. 16:718-725.
  • 4Banbury, D.N., Oakley, J.D., Sessions, R.B., and Banting, G. (2003). Tyrphostin A23 inhibits internalization of the transferrin receptor by perturbing the interaction between tyrosine motifs and the medium chain subunit of the AP-2 adaptor complex. J. Biol. Chem. 278: 12022-12028.
  • 5Bolte, S., and Cordelieres, F.P. (2006). A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224:213-232.
  • 6Borner, G.H., Sherrier, D.J., Weimar, T., Michselson, L.V., Hawkins, N.D., Macaskill, A., Napier, J.A., Beale, M.H., Lilley, K.S., and Dupree, P. (2005). Analysis of detergent-resistant membranes inArabidopsis. Evidence for plasma membrane lipid rafts. Plant Physiol. 137:104-116.
  • 7B(icherl, C.A., van Esse, G.W., Kruis, A., Luchtenberg, J., Westphal, A.H., Aker, J., van Hoek, A., Albrecht, C., Borst, J.W., and de Vries, S.C. (2013). Visualization of BRI1 and BAKI(SERK3) membrane receptor hetero-oligomers during brassinosteroid signaling. Plant Physiol. 162:1911-1925.
  • 8Chen, J., and Irudayaraj, J. (2010). Fluorescence lifetime cross correlation spectroscopy resolves EGFR and antagonist interaction in live cells. Anal. Chem. 82:6415-6421.
  • 9Cho, M.R., Knowles, D.W., Smith, B.L., Moulds, J.J., Agre, P., Mohandas, N., and Golan, D.E. (1999). Membrane dynamics of the water transport protein aquaporin-1 in intact human red cells. Biophye. J. 76:1136-1144.
  • 10Chung, I., Akita, R., Vandlen, R., Toomre, D., Schlessinger, J., and Mellman, I. (2010). Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 464:783-787.

共引文献11

同被引文献7

引证文献2

二级引证文献4

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部