The changing climate of Plant membrane technology
The changing climate of Plant membrane technology
Journal of Experimental Botany Special Issue
Corratg.-Faillie C, Lacombe B. 2017. Substrate (un)specificity of Arabidopsis NRT1/PTR FAMILY (NPF) proteins. Journal of Experimental Botany 68, 3107–3113.
Kriechbaumer V, Botchway SW, Hawes C. 2017. Localization and interactions between Arabidopsis auxin biosynthetic enzymes in the TAA/ YUC-dependent pathway. Journal of Experimental Botany 67, 4195–4207.
Damineli DSC, Portes MT, Feij JA. 2017. Oscillatory signatures underlie growth regimes in Arabidopsis pollen tubes: computational methods to estimate tip location, periodicity, and synchronization in growing cells. Journal of Experimental Botany 68, 3267–3281.
https://academic.oup.com/jxb/issue/68/12
The International Workshop on Plant Membrane Biology (IWPMB) 2016, was held in Annapolis (USA), and from this the special issue entitled “The Changing Climate of Plant Membrane Biology” was produced. In this special issue one focus was on the emergent understanding that members of a single gene family often exhibit differential biochemical, or transport, activities despite a high degree of sequence similarity. Such diversity of function is exemplified by the NTR1/ PTR FAMILY (NPF) proteins, which have been shown to exhibit isoform-specific transport of substrates other than nitrate and oligopeptides reviewed by Corratgé-Faillie and Lacombe (pp, 3107–3113). Another hot topic was the need to identify the membrane-bound compartments in which biosynthetic enzymes and transporters function. A paper from Kriechbaumer et al. (pp, 4195–4207) describes the localization of auxin biosynthetic enzymes to the plant endoplasmic reticulum. Advances in how to interpret and utilize complex data are exemplified by a new system, dubbed CHUKNORRIS, to interpret oscillatory signatures and transform them to quantitative data (Damineli et al. , 68, 3267–3281.). An accompanying Insight article assesses the value of such a system and its potential uses (Gilroy, 2017). The 18th IWPMB will be hosted by Mike Blatt and the University of Glasgow in 2019.
By Angus Murphy, University of Maryland, Handling Editor
The International Workshop on Plant Membrane Biology (IWPMB) 2016, was held in Annapolis (USA), and from this the special issue entitled “The Changing Climate of Plant Membrane Biology” was produced. In this special issue one focus was on the emergent understanding that members of a single gene family often exhibit differential biochemical, or transport, activities despite a high degree of sequence similarity. Such diversity of function is exemplified by the NTR1/ PTR FAMILY (NPF) proteins, which have been shown to exhibit isoform-specific transport of substrates other than nitrate and oligopeptides reviewed by Corratgé-Faillie and Lacombe (pp, 3107–3113). Another hot topic was the need to identify the membrane-bound compartments in which biosynthetic enzymes and transporters function. A paper from Kriechbaumer et al. (pp, 4195–4207) describes the localization of auxin biosynthetic enzymes to the plant endoplasmic reticulum. Advances in how to interpret and utilize complex data are exemplified by a new system, dubbed CHUKNORRIS, to interpret oscillatory signatures and transform them to quantitative data (Damineli et al. , 68, 3267–3281.). An accompanying Insight article assesses the value of such a system and its potential uses (Gilroy, 2017). The 18th IWPMB will be hosted by Mike Blatt and the University of Glasgow in 2019.
By Angus Murphy, University of Maryland, Handling Editor