Research Topics
Genomes and Genes
| Paul A RandazzoSummaryAffiliation: National Institutes of Health Country: USA Publications
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Detail Information
Publications
Differences between AGAP1, ASAP1 and Arf GAP1 in substrate recognition: interaction with the N-terminus of Arf1Hye-Young Yoon
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Building 37, Room 4118, National Institutes of Health, Bethesda, MD 20892, USA
Cell Signal 16:1033-44. 2004..Taken together, our results indicate that (i) Arf GAPs interact with amino acids 2-17 of Arf1 and (ii) each subgroup of Arf GAPs has a unique interface with Arf1...
Kinetic analysis of Arf GAP1 indicates a regulatory role for coatomerRuiBai Luo
Laboratory of Cellular and Molecular Biology, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 283:21965-77. 2008..We conclude that coatomer is an allosteric regulator of Arf GAP1. The relevance of the results to the two models of Arf GAP1-mediated regulation of Arf1 is discussed...- Consensus nomenclature for the human ArfGAP domain-containing proteinsRichard A Kahn
Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA
J Cell Biol 182:1039-44. 2008..This article describes the resulting consensus nomenclature and provides a brief description of each of the 10 subfamilies of 31 human genes encoding proteins containing the ArfGAP domain... - The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeletonP A Randazzo
Division of Basic Sciences, National Cancer Institute, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 97:4011-6. 2000..These data support a role for an Arf GTPase-activating protein, ASAP1, as a regulator of cytoskeletal remodeling and raise the possibility that the Arf pathway is a target for PDGF signaling... - Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodellingPaul A Randazzo
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Building 37 Room 4118, Bethesda, MD 20892, USA
Cell Signal 16:401-13. 2004..The results discussed illustrate roles for both Arf-dependent and -independent activities in the regulation of cellular architecture... - Functional interaction of ADP-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphateP A Randazzo
Laboratory of Biological Chemistry, Division of Basic Sciences, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 272:7688-92. 1997..These data support the hypothesis that PIP2 binding to Arf1 promotes interaction with Arf GAP. The implications of lipid-directed protein-protein interactions for membrane traffic are discussed... - Molecular aspects of the cellular activities of ADP-ribosylation factorsP A Randazzo
Laboratory of Cellular Oncology, Division of Basic Sciences, National Cancer Institute, Bethesda, MD, USA
Sci STKE 2000:re1. 2000..Understanding Arf's role in complex cellular functions such as protein secretion or cell movement will involve a description of the temporal and spatial coordination of these multiple Arf-dependent events... - Arf GAPs as regulators of the actin cytoskeletonPaul A Randazzo
Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA
Biol Cell 99:583-600. 2007..With multiple functional elements, the Arf GAPs could integrate signals and biochemical activities that result in co-ordinated changes in actin and membranes necessary for a wide range of cellular functions... - A PH domain in the Arf GTPase-activating protein (GAP) ARAP1 binds phosphatidylinositol 3,4,5-trisphosphate and regulates Arf GAP activity independently of recruitment to the plasma membranesFanny Campa
Laboratory of Cellular and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 284:28069-83. 2009..In our model, ARAP1 is recruited to membranes independently of PtdIns(3,4,5)P(3), the subsequent production of which triggers enzymatic activity... - ASAP3 is a focal adhesion-associated Arf GAP that functions in cell migration and invasionVi Luan Ha
Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
J Biol Chem 283:14915-26. 2008..In comparing ASAP1 and ASAP3, we also found that invadopodia are dispensable for the invasive behavior of cells derived from a mammary carcinoma... - Regulation of ASAP1 by phospholipids is dependent on the interface between the PH and Arf GAP domainsMagnus M Che
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, United States
Cell Signal 17:1276-88. 2005.... - Src-dependent phosphorylation of ASAP1 regulates podosomesSanita Bharti
Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA
Mol Cell Biol 27:8271-83. 2007.... - ARAP2 effects on the actin cytoskeleton are dependent on Arf6-specific GTPase-activating-protein activity and binding to RhoA-GTPHye Young Yoon
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Department of Health and Human Services, Building 37, Bethesda, MD 20892, USA
J Cell Sci 119:4650-66. 2006..We conclude that ARAP2 is an Arf6GAP that functions downstream of RhoA to regulate focal adhesion dynamics... - Arf GAPs and their interacting proteinsHiroki Inoue
Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA
Traffic 8:1465-75. 2007..Here we describe the Arf GAP family and summarize the currently identified protein interactors in the context of known Arf GAP functions... - Phosphatidylinositol-4-phosphate 5-kinase and GEP100/Brag2 protein mediate antiangiogenic signaling by semaphorin 3E-plexin-D1 through Arf6 proteinAtsuko Sakurai
Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 286:34335-45. 2011.... - Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and regulates pericentrosomal localization of transferrin receptor-positive recycling endosomeHiroki Inoue
Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
Mol Biol Cell 19:4224-37. 2008..The depletion also altered the trafficking of endocytosed transferrin. These results support the conclusion that ASAP1, like FIP3, functions as a component of the endocytic recycling compartment... - Mutational analysis of the Arf1*GTP/Arf GAP interface reveals an Arf1 mutant that selectively affects the Arf GAP ASAP1RuiBai Luo
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Curr Biol 15:2164-9. 2005..Based on our results, we conclude that the contribution of specific residues within switch 1 of Arf to binding and achieving a transition state toward GTP hydrolysis differs among Arf GAPs... - Modifications to the C-terminus of Arf1 alter cell functions and protein interactionsXiaoying Jian
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bldg 37 Room 2042, Bethesda, MD 20892, USA
Traffic 11:732-42. 2010.... - Kinetic analysis of GTP hydrolysis catalysed by the Arf1-GTP-ASAP1 complexRuiBai Luo
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA
Biochem J 402:439-47. 2007..The ramifications for the putative effector function of ASAP1 are discussed... - A BAR domain in the N terminus of the Arf GAP ASAP1 affects membrane structure and trafficking of epidermal growth factor receptorZhongzhen Nie
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Bethesda, Maryland 20892, USA
Curr Biol 16:130-9. 2006..We have examined the role of a putative BAR domain in the function of the Arf GAP ASAP1... - The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3Zhongzhen Nie
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
J Cell Sci 118:3555-66. 2005..Based on these results, we concluded that the closely related Arf GAPs, AGAP1 and AGAP2, distinguish between these related heterotetrameric adaptor protein complexes to specifically regulate AP-3 endosomes and AP-1 recycling endosomes... - ARAP1 association with CIN85 affects epidermal growth factor receptor endocytic traffickingHye Young Yoon
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892, U S A
Biol Cell 103:171-84. 2011..To further understand the function of ARAP1, we sought to identify proteins that interact with ARAP1... - Arf GAP2 is positively regulated by coatomer and cargoRuiBai Luo
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892, USA
Cell Signal 21:1169-79. 2009..Based on the common regulatory features of Arf GAP1 and 2, we propose a mechanism for cargo selection in which GTP hydrolysis triggered by cargo binding to the coat protein is coupled to coat polymerization... 
Contribution of AZAP-Type Arf GAPs to cancer cell migration and invasionVi Luan Ha
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, Maryland, USA
Adv Cancer Res 101:1-28. 2008..We also discuss the enzymology of the Arf GAPs related to possible targeted inhibition of specific subtypes of Arf GAPs...- Autoinhibition of Arf GTPase-activating protein activity by the BAR domain in ASAP1Xiaoying Jian
Laboratory of Cellular and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 284:1652-63. 2009..Analysis of single turnover kinetics revealed a transition state intermediate that was affected by the BAR domain. We conclude that BAR domains can affect enzymatic activity through intraprotein interactions... - ARAP1 regulates endocytosis of EGFRHye Young Yoon
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892, USA
Traffic 9:2236-52. 2008..Based on these findings, we propose that ARAP1 regulates the endocytic traffic of EGFR and, consequently, the rate of EGFR signal attenuation... - Dynamic interaction between Arf GAP and PH domains of ASAP1 in the regulation of GAP activityRuiBai Luo
Laboratory of Cellular and Molecular Biology, National Institutes of Health, Bethesda, MD 20892, United Sates
Cell Signal 20:1968-77. 2008..We propose that the PH domain contributes to Arf GAP activity by either binding to or positioning Arf1 GTP that is simultaneously bound to the Arf GAP domain... - AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeletonZhongzhen Nie
Laboratories of Cellular Oncology and Biochemistry, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 277:48965-75. 2002..However, distinct from other ASAP family members, AGAP1 also induced the loss of actin stress fibers. Thus, AGAP1 is a phosphoinositide-dependent Arf GAP that impacts both the endocytic compartment and actin... - Arf regulates interaction of GGA with mannose-6-phosphate receptorDianne Snow Hirsch
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Bldg 37 Room 6032 and Cell Biology and Metabolism Branch, National Institute of Child Health and Development, National Institutes of Health, Bethesda. MD 20892, USA
Traffic 4:26-35. 2003..GGA and mannose-6-phosphate receptor are then incorporated into a transport intermediate that excludes Arf... - In vitro and in vivo analysis of neurotrophin-3 activation of Arf6 and Rac-1Pedro F Esteban
Neural Development Group, Mouse Cancer Genetics Program, National Cancer Institute, Frederick, Maryland, USA
Methods Enzymol 438:171-83. 2008..Here we describe the rationale and protocols used for the dissection of an NT3 activated pathway that leads to the specific activation of Arf6 and Rac1... - Arf1 dissociates from the clathrin adaptor GGA prior to being inactivated by Arf GTPase-activating proteinsKerry M Jacques
Laboratory of Cellular Oncology, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 277:47235-41. 2002..Instead, termination of Arf1 signals mediated through GGA require that Arf1.GTP dissociates from GGA prior to interaction with GAP and consequent hydrolysis of GTP... - Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1Zhongzhen Nie
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Building 37, Room 4118, Bethesda, MD 20892, USA
Dev Cell 5:513-21. 2003..Cells overexpressing AGAP1 also exhibit increased LAMP1 trafficking via the plasma membrane. Taken together, these results support the hypothesis that AGAP1 directly and specifically regulates AP-3-dependent trafficking... - In vitro assays of Arf1 interaction with GGA proteinsHye-Young Yoon
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USA
Methods Enzymol 404:316-32. 2005..In this chapter, we describe in vitro assays for analysis of GGA interaction with Arf1 x GTP and for determining intracellular Arf1 x GTP levels... - Semaphorin 3E initiates antiangiogenic signaling through plexin D1 by regulating Arf6 and R-RasAtsuko Sakurai
Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, 30 Convent Drive, Rm 211, MSC 4340, Bethesda, MD 20892, USA
Mol Cell Biol 30:3086-98. 2010..Ultimately, our present study provides a molecular framework for antiangiogenesis signaling, thus impinging on a myriad of pathological conditions that are characterized by aberrant increase in neovessel formation, including cancer... - GTP-binding protein-like domain of AGAP1 is protein binding site that allosterically regulates ArfGAP protein catalytic activityRuiBai Luo
From the Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, Maryland 20892, USA
J Biol Chem 287:17176-85. 2012..In contrast, a C-terminal peptide from Cdc42 neither bound nor activated AGAP1. Based on these results, we propose that AGAPs are allosterically regulated through protein binding to the GLD domain... - RhoD, Src, and hDia2C in endosome motilityPaul A Randazzo
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA
Dev Cell 4:287-8. 2003..A recent report from Marino Zerial and colleagues examining RhoD identifies mDia2C, a novel splice variant of mDia2, and Src as components of the regulatory machinery influencing actin-dependent endosome movement... - Arf and its many interactorsZhongzhen Nie
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Building 37, Room 4118, Bethesda, MD 20892, USA
Curr Opin Cell Biol 15:396-404. 2003..Recent work examining the functional relationships among the diverse Arf interactors has led to reconsideration of the prevailing paradigms for Arf action... - Assays and properties of the Arf GAPs AGAP1, ASAP1, and Arf GAP1Magnus Mutah Che
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USA
Methods Enzymol 404:147-63. 2005..Conditions that optimize activity for each GAP are discussed. These methods can be used for the further characterization of Arf-Arf GAP interaction that is necessary for understanding the function of Arf in cellular physiology... - The pleckstrin homology (PH) domain of the Arf exchange factor Brag2 is an allosteric binding siteXiaoying Jian
Laboratory of Cellular and Molecular Biology, Center for Cancer Research, NCI, NHLBI, National Institutes of Health Bethesda, Maryland 20892, USA
J Biol Chem 287:24273-83. 2012..Thus, the PH domain and the interdomain linker of Brag2 may be targets for selectively regulating the activity of Brag2... - Arf GAPs and membrane trafficZhongzhen Nie
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Department of Health and Human Services, Bethesda, MD 20892, USA
J Cell Sci 119:1203-11. 2006..These results are the primary basis for modifications to the classical model for the function of Arf in transport vesicle formation, including a recent proposal that Arf has a proofreading, rather than a structural, role... - Arf GTPase-activating proteins and their potential role in cell migration and invasionFanny Campa
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892 4256, USA
Cell Adh Migr 2:258-62. 2008..In this commentary, we discuss examples of Arf GAPs that function either as regulators of Arfs or independently of the GTPase activity to regulate membrane structures that mediate cell adhesion and movement... - Preparation of myristoylated Arf1 and Arf6Vi Luan Ha
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USA
Methods Enzymol 404:164-74. 2005..Here, we describe methods that yield homogeneous preparations of myristoylated Arf1 and Arf6... - ACAPs are arf6 GTPase-activating proteins that function in the cell peripheryT R Jackson
Laboratory of Cellular Oncology, Division of Basic Sciences, National Cancer Institute, Bethesda, Maryland 20892 4255, USA
J Cell Biol 151:627-38. 2000..The additional effects of ASAP1 on PDGF-induced ruffling in fibroblasts suggest that multiple Arf GAPs function coordinately in the cell periphery... - Approaches to studying Arf GAPs in cells: in vitro assay with isolated focal adhesionsPei wen Chen
Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA
Curr Protoc Cell Biol . 2012..Detailed protocols for examining the activity of Arf GAPs in whole cell lysates and in association with isolated focal adhesions are provided... - A kinase-deficient TrkC receptor isoform activates Arf6-Rac1 signaling through the scaffold protein tamalinPedro F Esteban
Neural Development Group, Mouse Cancer Genetics Program, National Cancer Institute, Frederick, MD 21702, USA
J Cell Biol 173:291-9. 2006..Thus, our data identify a new signaling pathway elicited by the kinase-deficient TrkCT1 receptor. Moreover, we establish NT3 as an upstream regulator of Arf6... - GEFH1 binds ASAP1 and regulates podosome formationYoko Shiba
Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bldg 37 Room 2042, Bethesda, MD 20892, United States
Biochem Biophys Res Commun 406:574-9. 2011..Reduced expression of GEFH1, achieved with siRNA treatment, did not affect matrix degradation by podosomes but increased the rate of podosome assembly. Based on these results, we conclude that GEFH1 is a negative regulator of podosomes... - ARAP1: a point of convergence for Arf and Rho signalingKoichi Miura
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA
Mol Cell 9:109-19. 2002..The Arf GAP and Rho GAP activities both contributed to inhibiting cell spreading. Thus, ARAP1 is a PIP3-dependent Arf GAP that regulates Arf-, Rho-, and Cdc42-dependent cell activities... - Effects of acid phospholipids on ARF activities: potential roles in membrane trafficR A Kahn
Laboratory of Biological Chemistry, DTP, DCT, National Cancer Institute, NIH, Bethesda MD 20892, USA
J Lipid Mediat Cell Signal 14:209-14. 1996..There are potentially two distinct phospholipid binding sites each of which are coupled to the nucleotide binding site of ARFs... - ARAP2 signals through Arf6 and Rac1 to control focal adhesion morphologyPei wen Chen
Laboratory of Cellular and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 288:5849-60. 2013..We conclude that changes in Arf6 and Rac1 activities are necessary but not sufficient for ARAP2 to promote the growth of FAs and we speculate that ARAP2 has additional functions that are effector in nature to promote or stabilize FAs... - ArfGAP1 function in COPI mediated membrane traffic: currently debated models and comparison to other coat-binding ArfGAPsYoko Shiba
National Cancer Institute, Laboratory of Cellular and Molecular Biology, Bethesda, MD 20892, USA
Histol Histopathol 27:1143-53. 2012..We briefly discuss other ArfGAPs that may have similar function in Arf-dependent membrane traffic outside the ER-Golgi... - ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by SrcM T Brown
Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA
Mol Cell Biol 18:7038-51. 1998..By directly interacting with both Arfs and tyrosine kinases involved in regulating cell growth and cytoskeletal organization, ASAP1 could coordinate membrane remodeling events with these processes... - Preparation of myristoylated Arf1 and Arf6 proteinsPaul A Randazzo
Laboratory of Cellular Oncology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA
Methods Mol Biol 189:169-79. 2002 - Resolution of two ADP-ribosylation factor 1 GTPase-activating proteins from rat liverP A Randazzo
Laboratory of Biological Chemistry, Division of Basic Sciences, National Cancer Institute, Bldg 37, Rm 5D 02, 37 Convent Dr MSC 4255, Bethesda, MD 20892 4255, USA
Biochem J 324:413-9. 1997..Both GAP1 and GAP2 used ARF1 and ARF5 as substrates but not ARF6 or ARF-like protein-2. The potential role of multiple ARF GAPs in the independent regulation of ARF at specific steps in membrane traffic is discussed... - Mutational analysis of Saccharomyces cerevisiae ARF1R A Kahn
Laboratory of Biological Chemistry, NCI, National Institutes of Health, Bethesda, Maryland 20892
J Biol Chem 270:143-50. 1995..Two high-copy suppressors of this conditional phenotype were cloned and sequenced. One of these suppressors, SFS4, was found to be identical to PBS2/HOG4, recently shown to encode a microtubule-associated protein kinase kinase in yeast... - The GGAs promote ARF-dependent recruitment of clathrin to the TGNR Puertollano
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA
Cell 105:93-102. 2001..These observations suggest that the GGAs could function to link clathrin to membrane-bound ARF.GTP... - ADP-ribosylation factor (ARF)-like 3, a new member of the ARF family of GTP-binding proteins cloned from human and rat tissuesM M Cavenagh
Laboratory of Biological Chemistry, NCI, National Institutes of Health, Bethesda, Maryland 20892
J Biol Chem 269:18937-42. 1994..Thus, Arl3 is a ubiquitously expressed GTP-binding protein in the ARF family with distinctive biochemical properties consistent with its having unique, but unknown, role(s) in cell physiology... - Rac inhibits thrombin-induced Rho activation: evidence of a Pak-dependent GTPase crosstalkHans Rosenfeldt
Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, DHHS, Bethesda, Maryland 20892 4330, USA
J Mol Signal 1:8. 2006..These findings indicate that Rac interferes with receptor-dependent Rho stimulation through Pak1, thus providing a mechanism for cross-talk between these two small-GTPases... - ACAP-A/B are ArfGAP homologs in dictyostelium involved in sporulation but not in chemotaxisPei wen Chen
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, Maryland, United States of America
PLoS ONE 5:e8624. 2010..The absence of an effect on Dictyostelium migration may be due to a specific requirement for ACAPs in mesenchymal migration, which is observed in epithelial cancer cells where most studies of mammalian ArfGAPs were performed... - Activity of specific lipid-regulated ADP ribosylation factor-GTPase-activating proteins is required for Sec14p-dependent Golgi secretory function in yeastLora L Yanagisawa
Department of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294 0005, USA
Mol Biol Cell 13:2193-206. 2002.... - ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent mannerStacey T T I
Department of Surgery, University of Melbourne, Level 5 Clinical Sciences Building, Royal Melbourne Hospital, VIC 3050, Australia
J Cell Sci 117:6071-84. 2004..These results implicate ARAP3 in integrin-mediated tyrosine kinase signalling pathways controlling Rho GTPases and cell spreading... - ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coatJia Shu Yang
Division of Rheumatology, Immunology, and Allergy, Brigham and Women s Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115, USA
J Cell Biol 159:69-78. 2002..Collectively, these findings suggest that ARFGAP1 promotes vesicle formation by functioning as a component of the COPI coat... - CIN85 associates with multiple effectors controlling intracellular trafficking of epidermal growth factor receptorsKatarzyna Kowanetz
Institute of Biochemistry II, Goethe University Medical School, 60590 Frankfurt, Germany
Mol Biol Cell 15:3155-66. 2004..We propose that CIN85 functions as a scaffold molecule that binds to numerous endocytic accessory proteins, thus controlling distinct steps in trafficking of EGF receptors along the endocytic and recycling pathways...