CELLULAR LOGISTICS 2016, VOL. 16, NO. 1, e1178036 (1 pages) http://dx.doi.org/10.1080/21592799.2016.1178036
GTPASES IN TRAFFICKING SERIES-EDITORIAL
Small GTPases in trafficking – a family approach Introducing a rolling series focused on groups or families of small GTPases in trafficking Jennifer L. Stow Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia ARTICLE HISTORY Received 8 April 2016; Accepted 9 April 2016 KEYWORDS GTPase families; molecular tools; trafficking
The Ras superfamily of small GTPases is made up of families of Ras, Rho, Rab, Ran, and Arf GTPases, which together comprise well over one hundred proteins distinguished by their monomeric nature and their ability to bind and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). Functionally, the GTPase families are further expanded by their attendant accessory proteins, their GTPase activating proteins (GAPs), guanine nucleotide exchange factors (GEFs) and other proteins that guide the small GTPases through their “on-off” cycles of nucleotide exchange and membrane translocation. These G protein networks and the effectors they control impinge on a large and diverse array of cell functions in eukaryotes, and in some instances even in prokaryotes. In many eukaryotic cells, the intracellular trafficking of membrane and cargo relies on large contingencies of Rab and ARF family members, as well as members of other GTPase families. Many members of these families are deployed on membranes throughout cells to coordinate multi-step transport and functions on different compartments. Through the experimental approaches available in past decades of cell biology, the current knowledge of GTPases has been built by studying one Rab or ARF or GAP at a time. However it is increasingly clear that small GTPases often function in series or cascades, interlinked with each other and with their accessory proteins, to coordinate complex cell functions. Moreover most cell functions themselves are intricately harmonized through large dynamic protein complexes. So, modern cell biology increasingly demands consideration of GTPases on the larger scales of location-dependent groups or even whole families. This is made possible for many organisms and cell types through the advent of genomic data, gene expression profiles, pathway analysis, proteomics, gene editing and advanced imaging. With these approaches we can begin to “connect the dots” for GTPases functioning in spatiotemporal arrays within cellular landscapes and as part of the molecular machinery of cells, tissues or organisms. At this level we can explore evolution, species differences, and a very wide spread of homeostatic and disease-associated states, as well as growth, differentiation and responses to environmental, pathogenic or pharmacological agents.
CONTACT Jennifer L. Stow [email protected] y GTPases in Trafficking Series- Editorial © 2016 Taylor & Francis
In keeping with the ethos of the journal, to “serve the community of cell biologists in multiple ways” we are launching a rolling series of articles, reviews, toolboxes and commentaries dedicated to small GTPases in trafficking. The aim of this series is to inform, present data, and assist ongoing research by highlighting resources, reagents and approaches that facilitate family-wide or broad spectrum analysis of GTPase expression, location, function, protein interactions, cross species comparisons and roles in disease. For instance, in an accompanying article by Yeo et al.1 in this issue we present a sequence of multiple members of the Rab family recruited to phagosomal membranes in macrophages, as a basis for dissecting coordinated Rab control of phaogocytosis in different infectious or developmental contexts. Another particularly potent use of this series will be “Toolbox” articles used to present and discuss GTPase resources, for instance large plasmid collections that are simultaneously deposited with the not-for-profit distributor Addgene (www.addgene.org). Kicking off this initiative is a family wide repository of ARF family plasmids and a Toolbox by Richard Kahn.2 We hope that this series, together with the CellLogBlog, will foster collaborations and ensure maximal use of the experimental reagents we all create. The series will also be a ready source of information on families of GTPases as a reference for those working in the field and also for those new to studies on GTPase families or family members. We invite expressions of interest from those who may have resources or articles to contribute.
References [1] Yeo JC, Wall AA, Luo L, Stow J. Sequential recruitment of Rab GTPases during early stages of phagocytosis. Cell Logist 2016; 6(1): e1140615 [12 p]. [2] Kerr SC, Kahn R. Tool box: Plasmids for the expression or knockdown of human ARF Family GTPases (ARF/ARL/SAR) and their co-expression in bacteria with N-myristoyltransferases. Cell Logist 2015; 5(3): e1090523 [6 p].
GTPASES IN TRAFFICKING SERIES-EDITORIAL
Small GTPases in trafficking – a family approach Introducing a rolling series focused on groups or families of small GTPases in trafficking Jennifer L. Stow Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia ARTICLE HISTORY Received 8 April 2016; Accepted 9 April 2016 KEYWORDS GTPase families; molecular tools; trafficking
The Ras superfamily of small GTPases is made up of families of Ras, Rho, Rab, Ran, and Arf GTPases, which together comprise well over one hundred proteins distinguished by their monomeric nature and their ability to bind and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). Functionally, the GTPase families are further expanded by their attendant accessory proteins, their GTPase activating proteins (GAPs), guanine nucleotide exchange factors (GEFs) and other proteins that guide the small GTPases through their “on-off” cycles of nucleotide exchange and membrane translocation. These G protein networks and the effectors they control impinge on a large and diverse array of cell functions in eukaryotes, and in some instances even in prokaryotes. In many eukaryotic cells, the intracellular trafficking of membrane and cargo relies on large contingencies of Rab and ARF family members, as well as members of other GTPase families. Many members of these families are deployed on membranes throughout cells to coordinate multi-step transport and functions on different compartments. Through the experimental approaches available in past decades of cell biology, the current knowledge of GTPases has been built by studying one Rab or ARF or GAP at a time. However it is increasingly clear that small GTPases often function in series or cascades, interlinked with each other and with their accessory proteins, to coordinate complex cell functions. Moreover most cell functions themselves are intricately harmonized through large dynamic protein complexes. So, modern cell biology increasingly demands consideration of GTPases on the larger scales of location-dependent groups or even whole families. This is made possible for many organisms and cell types through the advent of genomic data, gene expression profiles, pathway analysis, proteomics, gene editing and advanced imaging. With these approaches we can begin to “connect the dots” for GTPases functioning in spatiotemporal arrays within cellular landscapes and as part of the molecular machinery of cells, tissues or organisms. At this level we can explore evolution, species differences, and a very wide spread of homeostatic and disease-associated states, as well as growth, differentiation and responses to environmental, pathogenic or pharmacological agents.
CONTACT Jennifer L. Stow [email protected] y GTPases in Trafficking Series- Editorial © 2016 Taylor & Francis
In keeping with the ethos of the journal, to “serve the community of cell biologists in multiple ways” we are launching a rolling series of articles, reviews, toolboxes and commentaries dedicated to small GTPases in trafficking. The aim of this series is to inform, present data, and assist ongoing research by highlighting resources, reagents and approaches that facilitate family-wide or broad spectrum analysis of GTPase expression, location, function, protein interactions, cross species comparisons and roles in disease. For instance, in an accompanying article by Yeo et al.1 in this issue we present a sequence of multiple members of the Rab family recruited to phagosomal membranes in macrophages, as a basis for dissecting coordinated Rab control of phaogocytosis in different infectious or developmental contexts. Another particularly potent use of this series will be “Toolbox” articles used to present and discuss GTPase resources, for instance large plasmid collections that are simultaneously deposited with the not-for-profit distributor Addgene (www.addgene.org). Kicking off this initiative is a family wide repository of ARF family plasmids and a Toolbox by Richard Kahn.2 We hope that this series, together with the CellLogBlog, will foster collaborations and ensure maximal use of the experimental reagents we all create. The series will also be a ready source of information on families of GTPases as a reference for those working in the field and also for those new to studies on GTPase families or family members. We invite expressions of interest from those who may have resources or articles to contribute.
References [1] Yeo JC, Wall AA, Luo L, Stow J. Sequential recruitment of Rab GTPases during early stages of phagocytosis. Cell Logist 2016; 6(1): e1140615 [12 p]. [2] Kerr SC, Kahn R. Tool box: Plasmids for the expression or knockdown of human ARF Family GTPases (ARF/ARL/SAR) and their co-expression in bacteria with N-myristoyltransferases. Cell Logist 2015; 5(3): e1090523 [6 p].
