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Dive into the research topics where Cathal Wilson is active.

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Featured researches published by Cathal Wilson.


Science | 2012

Sedlin Controls the ER Export of Procollagen by Regulating the Sar1 Cycle

Rossella Venditti; Tiziana Scanu; Michele Santoro; Giuseppe Di Tullio; Alexander Spaar; Renato Gaibisso; Galina V. Beznoussenko; Alexander A. Mironov; A. S. Mironov; Leopoldo Zelante; Maria Rosaria Piemontese; Angelo Notarangelo; Vivek Malhotra; Barbara M. Vertel; Cathal Wilson; Maria Antonietta De Matteis

A Tight Squeeze During intracellular transport, the export of procollagen from the endoplasmic reticulum is intriguing because procollagen is too large to fit into conventional coat protein complex II (COPII)–coated transport vesicles. Recent work has implicated the receptor TANGO1 in procollagen export. Now, Venditti et al. (p. 1668) report that TANGO1 recruits Sedlin—also known as TRAPPC2, a homolog of the yeast TRAPP subunit Trs20—and helps to allow COPII-coated carriers to grow large enough to incorporate procollagen. Sedlin, the product of the gene mutated in spondyloepiphyseal dyplasia tarda, acts to expand cargo containers to fit bulky procollagen. Newly synthesized proteins exit the endoplasmic reticulum (ER) via coat protein complex II (COPII) vesicles. Procollagen (PC), however, forms prefibrils that are too large to fit into typical COPII vesicles; PC thus needs large transport carriers, which we term megacarriers. TANGO1 assists PC packing, but its role in promoting the growth of megacarriers is not known. We found that TANGO1 recruited Sedlin, a TRAPP component that is defective in spondyloepiphyseal dysplasia tarda (SEDT), and that Sedlin was required for the ER export of PC. Sedlin bound and promoted efficient cycling of Sar1, a guanosine triphosphatase that can constrict membranes, and thus allowed nascent carriers to grow and incorporate PC prefibrils. This joint action of TANGO1 and Sedlin sustained the ER export of PC, and its derangement may explain the defective chondrogenesis underlying SEDT.


BioEssays | 2013

Phosphatidylinositol‐4‐phosphate: The Golgi and beyond

Maria Antonietta De Matteis; Cathal Wilson; Giovanni D'Angelo

Initially identified as a key phosphoinositide that controls membrane trafficking at the Golgi complex, phosphatidylinositol-4-phosphate (PI4P) has emerged as a key molecule in the regulation of a diverse array of cellular functions. In this review we will discuss selected examples of the findings that in the last few years have significantly increased our awareness of the regulation and roles of PI4P in the Golgi complex and beyond. We will also highlight the role of PI4P in infection and cancer. We believe that, with the increasing number of regulators and effectors of PI4P identified, the time is ripe for a more integrated approach of study. A first step in this direction is the delineation of PI4P-centered molecular networks that we provide using data from low and high throughput studies in yeast and mammals.


Trends in Cell Biology | 2014

Exiting the ER: what we know and what we don’t

Rossella Venditti; Cathal Wilson; Maria Antonietta De Matteis

The vast majority of proteins that are transported to different cellular compartments and secreted from the cell require coat protein complex II (COPII) for export from the endoplasmic reticulum (ER). Many of the molecular mechanisms underlying COPII assembly are understood in great detail, but it is becoming increasingly evident that this basic machinery is insufficient to account for diverse aspects of protein export from the ER that are observed in vivo. Here we review recent data that have furthered our mechanistic understanding of COPII assembly and, in particular, how genetic diseases associated with the early secretory pathway have added fundamental insights into the regulation of ER-derived carrier formation. We also highlight some unresolved issues that future work should address to better understand the physiology of COPII-mediated transport.


Sub-cellular biochemistry | 2012

Phosphoinositides in Golgi Complex Function

Giovanni D’Angelo; Mariella Vicinanza; Cathal Wilson; Maria Antonietta De Matteis

The Golgi complex is a ribbon-like organelle composed of stacks of flat cisternae interconnected by tubular junctions. It occupies a central position in the endomembrane system as proteins and lipids that are synthesized in the endoplasmic reticulum (ER) pass through the Golgi complex to undergo biosynthetic modification (mainly glycosylation) and to be sorted to their final destinations. In addition the Golgi complex possesses a number of activities, apparently not directly connected with its main role in trafficking and sorting, which have been recently reviewed in Wilson et al. 2011. In spite of the constant massive flux of material the Golgi complex maintains its identity and phosphoinositides (PIs), among other factors, play a central role in this process. The active metabolism of PIs at the Golgi is necessary for the proper functioning of the organelle both in terms of membrane trafficking/sorting and its manifold metabolic and signalling activities. Phosphatidylinositol 4-phosphate (PtdIns4P), in particular, is responsible for the recruitment of numerous cytosolic proteins that recognise and bind PtdIns4P via specific lipid-binding domains. In this chapter we will summarize the findings that have contributed to our current understanding of the role of PIs in the biology of the Golgi complex in terms of the regulation of PI metabolism and the functional roles and regulation of PtdIns4P effectors.


Advances in biological regulation | 2016

PI(4)P homeostasis: Who controls the controllers?

Rossella Venditti; Maria Chiara Masone; Cathal Wilson; Maria Antonietta De Matteis

During recent decades, PI(4)P (phosphoinositol-4-phosphate) has been described as a key regulator of a wide range of cellular functions such as organelle biogenesis, lipid metabolism and distribution, membrane trafficking, ion channels, pumps, and transporter activities. In this review we will focus on the multiple mechanisms that regulate PI(4)P homeostasis ranging from those responsible for the spatial distribution of the PI4 kinases and PI(4)P phosphatase to those controlling their enzymatic activity or the delivery/presentation of the substrate, i.e. PI or PI(4)P, to the PI4Ks or PI(4)P phosphatase, respectively. We will also highlight the open questions in the field mainly dealing with the existence and mode of action of PI(4)P sensors that monitor its amount and can act as a rheostat tuning PI(4)P levels in different compartments and adapting them to the different needs of the cell.


Annual Review of Genomics and Human Genetics | 2013

Cellular Assays for Drug Discovery in Genetic Disorders of Intracellular Trafficking

Maria Antonietta De Matteis; Mariella Vicinanza; Rossella Venditti; Cathal Wilson

Intracellular membrane trafficking is essential for organelle biogenesis, structure, and function; the exchange of material between organelles; and communication between the cell and its external environment. Genetic disorders affecting intracellular trafficking can lead to a variety of human diseases, but specific therapies for these diseases are notably lacking. In this article, we focus on how current knowledge about genetic disorders that affect intracellular trafficking can be used to develop strategies for cell-based assays in order to identify drugs using high-content screening approaches.


Archive | 2008

The TRAPP complex

Tiziana Scanu; Cathal Wilson

Intracellular transport of biosynthetic cargo from the endoplasmic reticulum to the plasma membrane occurs by membrane-bound vesicular or tubulove-sicular carriers that dissociate from a donor compartment and fuse with an acceptor compartment. The arrival of a transport carrier to the correct destination along the exocytic pathway is important for the appropriate spatio-temporal processing and delivery of the cargo molecules. Membrane fusion requires the formation of a trans SNARE complex (SNAREpin) of SNARE proteins contributed by the donor and acceptor membranes that is thought to overcome the energy barrier that would prevent two membranes from fusing. Prior to this event, however, proteins called tethering factors appear to act as physical links between membrane compartments (Whyte and Munro 2002). In addition to acting as physical links the tethering factors may contribute to the specificity of compartmental fusion by their interaction with various molecules on the donor and acceptor membranes. Two broad classes of tethering factors are represented by proteins containing extensive coiled-coil domains (such as p115/Uso1 in mammals/yeast) or by a number of large multiprotein complexes that mediate membrane traffic between various compartments within the cell (Whyte and Munro 2002). A common feature of the tethering factors seems to be their interaction with small GTPases of the Rab/Ypt family and with SNAREs that appears to contribute to the specificity of membrane fusion.


PLOS ONE | 2012

Mutational Analysis of the Yeast TRAPP Subunit Trs20p Identifies Roles in Endocytic Recycling and Sporulation

Hichem Mahfouz; Antonella Ragnini-Wilson; Rossella Venditti; Maria Antonietta De Matteis; Cathal Wilson

Trs20p is a subunit of the evolutionarily conserved TRAPP (TRAnsport Protein Particle) complex that mediates various aspects of membrane trafficking. Three TRAPP complexes have been identified in yeast with roles in ER-to-Golgi trafficking, post-Golgi and endosomal-to-Golgi transport and in autophagy. The role of Trs20p, which is essential for viability and a component of all three complexes, and how it might function within each TRAPP complex, has not been clarified to date. To begin to address the role of Trs20p we generated different mutants by random mutagenesis but, surprisingly, no defects were observed in diverse anterograde transport pathways or general secretion in Trs20 temperature-sensitive mutants. Instead, mutation of Trs20 led to defects in endocytic recycling and a block in sporulation/meiosis. The phenotypes of different mutants appear to be separable suggesting that the mutations affect the function of Trs20 in different TRAPP complexes.


Biochemical Journal | 2011

The Golgi apparatus: an organelle with multiple complex functions

Cathal Wilson; Rossella Venditti; Laura Rita Rega; Antonino Colanzi; Giovanni D'Angelo; M. Antonietta De Matteis


Histochemistry and Cell Biology | 2016

Three-dimensional and immune electron microscopic analysis of the secretory pathway in Saccharomyces cerevisiae

Galina V. Beznoussenko; Antonella Ragnini-Wilson; Cathal Wilson; Alexander A. Mironov

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Maria Antonietta De Matteis

Seconda Università degli Studi di Napoli

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Angelo Notarangelo

Casa Sollievo della Sofferenza

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Giampiero Porcu

University of Rome Tor Vergata

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Leopoldo Zelante

Casa Sollievo della Sofferenza

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