scholarly journals Arl4D-EB1 interaction promotes centrosomal recruitment of EB1 and microtubule growth

2020 ◽  
Vol 31 (21) ◽  
pp. 2348-2362
Author(s):  
Shin-Jin Lin ◽  
Chun-Fang Huang ◽  
Tsung-Sheng Wu ◽  
Chun-Chun Li ◽  
Fang-Jen S. Lee
Keyword(s):  
Small Gtpase ◽  
Adp Ribosylation ◽  
Microtubule Growth ◽  
Adp Ribosylation Factor

The GTP-bound form of ADP-ribosylation factor-like 4D (Arl4D) small GTPase localizes to the centrosome and interacts with microtubule (MT) end-binding 1 (EB1) protein. Arl4D-EB1 interaction promotes EB1 centrosomal recruitment and increases the association of EB1 and p150 subunit of dynactin, thereby contributing to the nucleation of MTs at the centrosome.

scholarly journals ADP-ribosylation factor–like 4A interacts with Robo1 to promote cell migration by regulating Cdc42 activation

2019 ◽  
Vol 30 (1) ◽  
pp. 69-81 ◽  
Author(s):  
Tsai-Shin Chiang ◽  
Ming-Chieh Lin ◽  
Meng-Chen Tsai ◽  
Chieh-Hsin Chen ◽  
Li-Ting Jang ◽  
...  
Keyword(s):  
Cell Migration ◽  
Molecular Mechanisms ◽  
Small Gtpase ◽  
Dependent Manner ◽  
Amino Acid Residues ◽  
Adp Ribosylation ◽  
Promote Cell Migration ◽  
Cytoskeleton Remodeling ◽  
Adp Ribosylation Factor

Cell migration is a highly regulated event that is initiated by cell membrane protrusion and actin reorganization. Robo1, a single-pass transmembrane receptor, is crucial for neuronal guidance and cell migration. ADP-ribosylation factor (Arf)–like 4A (Arl4A), an Arf small GTPase, functions in cell morphology, cell migration, and actin cytoskeleton remodeling; however, the molecular mechanisms of Arl4A in cell migration are unclear. Here, we report that the binding of Arl4A to Robo1 modulates cell migration by promoting Cdc42 activation. We found that Arl4A interacts with Robo1 in a GTP-dependent manner and that the Robo1 amino acid residues 1394–1398 are required for this interaction. The Arl4A-Robo1 interaction is essential for Arl4A-induced cell migration and Cdc42 activation but not for the plasma membrane localization of Robo1. In addition, we show that the binding of Arl4A to Robo1 decreases the association of Robo1 with the Cdc42 GTPase-activating protein srGAP1. Furthermore, Slit2/Robo1 binding down-regulates the Arl4A-Robo1 interaction in vivo, thus attenuating Cdc42-mediated cell migration. Therefore, our study reveals a novel mechanism by which Arl4A participates in Slit2/Robo1 signaling to modulate cell motility by regulating Cdc42 activity.

scholarly journals Recombinant protein of Haemonchus contortus small GTPase ADP-ribosylation factor 1 (HcARF1) modulate the cell mediated immune response in vitro

Oncotarget ◽  
2017 ◽  
Vol 8 (68) ◽  
pp. 112211-112221 ◽  
Author(s):  
Javaid Ali Gadahi ◽  
Muhammad Ehsan ◽  
Shuai Wang ◽  
Zhenchao Zhang ◽  
Ruofeng Yan ◽  
...  
Keyword(s):  
Immune Response ◽  
Recombinant Protein ◽  
Haemonchus Contortus ◽  
Small Gtpase ◽  
Adp Ribosylation ◽  
Cell Mediated Immune Response ◽  
Adp Ribosylation Factor ◽  
Immune Response In Vitro

scholarly journals Cross-Kingdom Activation of Vibrio Toxins by ADP-Ribosylation Factor Family GTPases

2020 ◽  
Vol 202 (24) ◽  
Author(s):  
Alfa Herrera ◽  
Karla J. F. Satchell
Keyword(s):  
Vibrio Vulnificus ◽  
Bacterial Species ◽  
Small Gtpases ◽  
Small Gtpase ◽  
Cell Organelle ◽  
Content Type ◽  
Adp Ribosylation ◽  
Cellular Processes ◽  
Adp Ribosyltransferase ◽  
Adp Ribosylation Factor

ABSTRACT Pathogenic Vibrio species use many different approaches to subvert, attack, and undermine the host response. The toxins they produce are often responsible for the devastating effects associated with their diseases. These toxins target a variety of host proteins, which leads to deleterious effects, including dissolution of cell organelle integrity and inhibition of protein secretion. Becoming increasingly prevalent as cofactors for Vibrio toxins are proteins of the small GTPase families. ADP-ribosylation factor small GTPases (ARFs) in particular are emerging as a common host cofactor necessary for full activation of Vibrio toxins. While ARFs are not the direct target of Vibrio cholerae cholera toxin (CT), ARF binding is required for its optimal activity as an ADP-ribosyltransferase. The makes caterpillars floppy (MCF)-like and the domain X (DmX) effectors of the Vibrio vulnificus multifunctional autoprocessing repeats-in-toxin (MARTX) toxin also both require ARFs to initiate autoprocessing and activation as independent effectors. ARFs are ubiquitously expressed in eukaryotes and are key regulators of many cellular processes, and as such they are ideal cofactors for Vibrio pathogens that infect many host species. In this review, we cover in detail the known Vibrio toxins that use ARFs as cross-kingdom activators to both stimulate and optimize their activity. We further discuss how these contrast to toxins and effectors from other bacterial species that coactivate, stimulate, or directly modify host ARFs as their mechanisms of action.

scholarly journals ADP-ribosylation factor 6 modulates adrenergic stimulated lipolysis in adipocytes

2010 ◽  
Vol 298 (4) ◽  
pp. C921-C928 ◽  
Author(s):  
Yingqiu Liu ◽  
Dequan Zhou ◽  
Nada A. Abumrad ◽  
Xiong Su
Keyword(s):  
Glucose Transporter ◽  
Specific Inhibitor ◽  
Small Gtpase ◽  
Receptor Trafficking ◽  
Endocytic Pathway ◽  
Mrna Levels ◽  
Adrenergic Stimulation ◽  
Adp Ribosylation ◽  
Adp Ribosylation Factor

ADP-ribosylation factor 6 (Arf6) is a small GTPase that influences membrane receptor trafficking and the actin cytoskeleton. In adipocytes, Arf6 regulates the trafficking of the glucose transporter type 4 (GLUT4) and consequently insulin-stimulated glucose transport. Previous studies also indicated a role of Arf6 in adrenergic receptor trafficking, but whether this contributes to the control of lipolysis in adipocytes remains unknown. This was examined in the present study by using RNA interference (RNAi) and pharmaceutical inhibition in murine cultured 3T3-L1 adipocytes. Downregulation of Arf6 by RNAi impairs isoproterenol-stimulated lipolysis specifically but does not alter triacylglycerol (TAG) synthesis or the insulin signaling pathway. Neither total TAG amounts nor TAG fatty acid compositions are altered. The inhibitory effect on lipolysis is mimicked by dynasore, a specific inhibitor for dynamin, which is required for endocytosis. In contrast, lipolysis triggered by reagents that bypass events at the plasma membrane (e.g., forskolin, isobutylmethylxanthine or 8-bromo-cAMP) is not affected. Moreover, Arf6 protein levels in white adipose tissues are markedly increased in ob/ob mice, whereas they are decreased in obesity-resistant CD36 null mice. These changes reflect at least in part alterations in Arf6 mRNA levels. Collectively, these results suggest a role of the endocytic pathway and its regulation by Arf6 in adrenergic stimulation of lipolysis in adipocytes and potentially in the development of obesity.

scholarly journals ADP-ribosylation factor–like 4C binding to filamin-A modulates filopodium formation and cell migration

2017 ◽  
Vol 28 (22) ◽  
pp. 3013-3028 ◽  
Author(s):  
Tsai-Shin Chiang ◽  
Hsu-Feng Wu ◽  
Fang-Jen S. Lee
Keyword(s):  
Cell Migration ◽  
Morphological Changes ◽  
Small Gtpase ◽  
Dependent Manner ◽  
Filamin A ◽  
Filamentous Actin ◽  
Adp Ribosylation ◽  
Gtpase Activation ◽  
Adp Ribosylation Factor ◽  
Filopodium Formation

Changes in cell morphology and the physical forces that occur during migration are generated by a dynamic filamentous actin cytoskeleton. The ADP-ribosylation factor–like 4C (Arl4C) small GTPase acts as a molecular switch to regulate morphological changes and cell migration, although the mechanism by which this occurs remains unclear. Here we report that Arl4C functions with the actin regulator filamin-A (FLNa) to modulate filopodium formation and cell migration. We found that Arl4C interacted with FLNa in a GTP-dependent manner and that FLNa IgG repeat 22 is both required and sufficient for this interaction. We also show that interaction between FLNa and Arl4C is essential for Arl4C-induced filopodium formation and increases the association of FLNa with Cdc42-GEF FGD6, promoting cell division cycle 42 (Cdc42) GTPase activation. Thus our study revealed a novel mechanism, whereby filopodium formation and cell migration are regulated through the Arl4C-FLNa–mediated activation of Cdc42.

The ADP-ribosylation factor-like small GTPase FgArl1 participates in growth, pathogenicity and DON production in Fusarium graminearum

2020 ◽  
Vol 124 (11) ◽  
pp. 969-980
Author(s):  
Chenyu Wang ◽  
Yixiao Wang ◽  
Yao Wang ◽  
Zuodong Wang ◽  
Liyuan Zhang ◽  
...  
Keyword(s):  
Fusarium Graminearum ◽  
Small Gtpase ◽  
Adp Ribosylation ◽  
Adp Ribosylation Factor

scholarly journals ADP-ribosylation Factor 1-independent Protein Sorting and Export from thetrans-Golgi Network

2004 ◽  
Vol 279 (50) ◽  
pp. 52735-52743 ◽  
Author(s):  
Mark A. Ellis ◽  
Mark T. Miedel ◽  
Christopher J. Guerriero ◽  
Ora A. Weisz
Keyword(s):  
Small Gtpase ◽  
Proton Channel ◽  
Coat Proteins ◽  
Adp Ribosylation ◽  
Influenza Hemagglutinin ◽  
Intact Membrane ◽  
Golgi Network ◽  
Adp Ribosylation Factor

Polarized epithelial cells efficiently sort newly synthesized apical and basolateral proteins into distinct transport carriers that emerge from thetrans-Golgi network (TGN), and this sorting is recapitulated in nonpolarized cells. While the targeting signals of basolaterally destined proteins are generally cytoplasmically disposed, apical sorting signals are not typically accessible to the cytosol, and the transport machinery required for segregation and export of apical cargo remains largely unknown. Here we investigated the molecular requirements for TGN export of the apical marker influenza hemagglutinin (HA) in HeLa cells using anin vitroreconstitution assay. HA was released from the TGN in intact membrane-bound compartments, and export was dependent on addition of an ATP-regenerating system and exogenous cytosol. HA release was inhibited by guanosine 5′-O-(3-thiotriphosphate) (GTPγS) as well as under conditions known to negatively regulate apical transportin vivo, including expression of the acid-activated proton channel influenza M2. Interestingly, release of HA was unaffected by depletion of ADP-ribosylation factor 1, a small GTPase that has been implicated in the recruitment of all known adaptors and coat proteins to the Golgi complex. Furthermore, regulation of HA release by GTPγS or M2 expression was unaffected by cytosolic depletion of ADP-ribosylation factor 1, suggesting that HA sorting remains functionally intact in the absence of the small GTPase. These data suggest that TGN sorting and export of influenza HA does not require classical adaptors involved in the formation of other classes of exocytic carriers and thus appears to proceed via a novel mechanism.

scholarly journals Role of the Second Cysteine-rich Domain and Pro275 in Protein Kinase D2 Interaction with ADP-Ribosylation Factor 1, Trans-Golgi Network Recruitment, and Protein Transport

2010 ◽  
Vol 21 (6) ◽  
pp. 1011-1022 ◽  
Author(s):  
Ganesh Varma Pusapati ◽  
Denis Krndija ◽  
Milena Armacki ◽  
Götz von Wichert ◽  
Julia von Blume ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Protein Transport ◽  
Small Gtpase ◽  
Adp Ribosylation ◽  
Trans Golgi Network ◽  
Rich Domain ◽  
Golgi Network ◽  
Adp Ribosylation Factor ◽  
Cysteine Rich Domain

Protein kinase D (PKD) isoenzymes regulate the formation of transport carriers from the trans-Golgi network (TGN) that are en route to the plasma membrane. The PKD C1a domain is required for the localization of PKDs at the TGN. However, the precise mechanism of how PKDs are recruited to the TGN is still elusive. Here, we report that ADP-ribosylation factor (ARF1), a small GTPase of the Ras superfamily and a key regulator of secretory traffic, specifically interacts with PKD isoenzymes. ARF1, but not ARF6, binds directly to the second cysteine-rich domain (C1b) of PKD2, and precisely to Pro275 within this domain. Pro275 in PKD2 is not only crucial for the PKD2-ARF1 interaction but also for PKD2 recruitment to and PKD2 function at the TGN, namely, protein transport to the plasma membrane. Our data suggest a novel model in which ARF1 recruits PKD2 to the TGN by binding to Pro275 in its C1b domain followed by anchoring of PKD2 in the TGN membranes via binding of its C1a domain to diacylglycerol. Both processes are critical for PKD2-mediated protein transport.

scholarly journals The small GTPase ADP-ribosylation factor 6 negatively regulates dendritic spine formation

FEBS Letters ◽  
2005 ◽  
Vol 579 (30) ◽  
pp. 6834-6838 ◽  
Author(s):  
Hideyuki Miyazaki ◽  
Masakazu Yamazaki ◽  
Hiroshi Watanabe ◽  
Tomohiko Maehama ◽  
Takeaki Yokozeki ◽  
...  
Keyword(s):  
Dendritic Spine ◽  
Small Gtpase ◽  
Spine Formation ◽  
Adp Ribosylation ◽  
Adp Ribosylation Factor
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