Arfaptin 1, an ARF‐binding protein, inhibits phospholipase D and endoplasmic reticulum/Golgi protein transport

Williger, Ben-Tsion; Ostermann, Joachim; Exton, John H.

doi:10.1016/s0014-5793(98)01707-4

Cited by 29 publications

(20 citation statements)

References 22 publications

(39 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…48,49 Several families of proteins, including the FERM (4.1 protein, Ezrin, Radixin, and Moesin) and BAR (Bin/amphiphysin/Rvs) domain proteins, have molecular motifs that are sensitive to membrane curvature. Proteins containing these domains, which include the ARF (adenosine-ribosylation factor) family, 50,51 small GTPases like Rac, 50,52 and guanine exchange factors, 53 can assemble multiprotein complexes and preferentially target these complexes toward a curved membrane, thereby affecting protein localization and signaling. Similarly, membrane tension is a key regulator of endo- and exocytosis.…”

Section: The Cell In 3d: Cell–matrix Interactionsmentioning

confidence: 99%

Deconstructing Signaling in Three Dimensions

Rubashkin

Weaver

2014

Biochemistry

View full text Add to dashboard Cite

Cells in vivo exist within the context of a multicellular tissue, where their behavior is governed by homo- and heterotypic cell–cell interactions, the material properties of the extracellular matrix, and the distribution of various soluble and physical factors. Most methods currently used to study and manipulate cellular behavior in vitro, however, sacrifice physiological relevance for experimental expediency. The fallacy of such approaches has been highlighted by the recent development and application of three-dimensional culture models to cell biology, which has revealed striking phenotypic differences in cell survival, migration, and differentiation in genetically identical cells simply by varying culture conditions. These perplexing findings beg the question of what constitutes a three-dimensional culture and why cells behave so differently in two- and three-dimensional culture formats. In the following review, we dissect the fundamental differences between two- and three-dimensional culture conditions. We begin by establishing a basic definition of what “three dimensions” means at different biological scales and discuss how dimensionality influences cell signaling across different length scales. We identify which three-dimensional features most potently influence intracellular signaling and distinguish between conserved biological principles that are maintained across culture conditions and cellular behaviors that are sensitive to microenvironmental context. Finally, we highlight state-of-the-art molecular tools amenable to the study of signaling in three dimensions under conditions that facilitate deconstruction of signaling in a more physiologically relevant manner.

show abstract

Section: The Cell In 3d: Cell–matrix Interactionsmentioning

confidence: 99%

Deconstructing Signaling in Three Dimensions

Rubashkin

Weaver

2014

Biochemistry

View full text Add to dashboard Cite

show abstract

“…5,2001 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS ments at the plasma membrane (5,8). Our laboratory proposed that arfaptin 2/POR1 is a binding protein for GTP-ARF (especially ARF1) acting in Golgi (2,12). At first glance, arfaptin 2/POR1 seems unlikely to be a common down stream effector for Rac1 and ARF1 because the subcellular localizations and proposed cellular roles of Rac1 and ARF1 are different (6 -9).…”

Section: Figmentioning

confidence: 99%

Differential Binding of Arfaptin 2/POR1 to ADP-Ribosylation Factors and Rac1

Shin

Exton

2001

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

“…Arf1 (and its close relatives Arfs 2-5) are chiefly responsible for regulating vesicle budding by recruiting protein complexes such as COPI, adaptor protein complex-1 and the GGAs to their sites of action [6]–[10]. Arf1 is activated in vivo by exchange factors of the GBF1 and BIG subfamilies [11]–[14].…”

Section: Introductionmentioning

confidence: 99%

Identification of a Guanine Nucleotide Exchange Factor for Arf3, the Yeast Orthologue of Mammalian Arf6

Gillingham

Munro

2007

PLoS ONE

View full text Add to dashboard Cite

Small G proteins of the Arf and Rab families are fundamental to the organisation and activity of intracellular membranes. One of the most well characterised of these G proteins is mammalian Arf6, a protein that participates in many cellular processes including endocytosis, actin remodelling and cell adhesion. Exchange of GDP for GTP on Arf6 is performed by a variety of guanine nucleotide exchange factors (GEFs), principally of the cytohesin (PSCD) and EFA6 (PSD) families. In this paper we describe the characterisation of a GEF for the yeast orthologue of Arf6, Arf3, which we have named Yel1 (yeast EFA6-like-1) using yeast genetics, fluorescence microscopy and in vitro nucleotide exchange assays. Yel1 appears structurally related to the EFA6 family of GEFs, having an N-terminal Sec7 domain and C-terminal PH and coiled-coil domains. We find that Yel1 is constitutively targeted to regions of polarised growth in yeast, where it co-localises with Arf3. Moreover the Sec7 domain of Yel1 is required for its membrane targeting and for that of Arf3. Finally we show that the isolated Yel1 Sec7 domain strongly stimulates nucleotide exchange activity specifically on Arf3 in vitro.

show abstract

Arfaptin 1, an ARF‐binding protein, inhibits phospholipase D and endoplasmic reticulum/Golgi protein transport

Cited by 29 publications

References 22 publications

Deconstructing Signaling in Three Dimensions

Deconstructing Signaling in Three Dimensions

Differential Binding of Arfaptin 2/POR1 to ADP-Ribosylation Factors and Rac1

Identification of a Guanine Nucleotide Exchange Factor for Arf3, the Yeast Orthologue of Mammalian Arf6

Contact Info

Product

Resources

About