Literature DB >> 17868031

Arf GAPs as regulators of the actin cytoskeleton.

Paul A Randazzo1, Hiroki Inoue, Sanita Bharti.   

Abstract

The Arf (ADP-ribosylation factor) GAPs (GTPase-activating proteins) are a family of proteins with a common catalytic domain that induces hydrolysis of GTP bound to Arf GTP-binding proteins. At least three groups of multidomain Arf GAPs affect the actin cytoskeleton and cellular activities, such as migration and movement, that depend on the cytoskeleton. One role of the Arf GAPs is to regulate membrane remodelling that accompanies actin polymerization. Regulation of membrane remodelling is mediated in part by the regulation of Arf proteins. However, Arf GAPs also regulate actin independently of effects on membranes or Arf. These functions include acting as upstream regulators of Rho family proteins and providing a scaffold for Rho effectors and exchange factors. 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.

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Year:  2007        PMID: 17868031     DOI: 10.1042/bc20070034

Source DB:  PubMed          Journal:  Biol Cell        ISSN: 0248-4900            Impact factor:   4.458


  52 in total

1.  ARAP1 association with CIN85 affects epidermal growth factor receptor endocytic trafficking.

Authors:  Hye-Young Yoon; Stephen C Kales; Ruibai Luo; Stanley Lipkowitz; Paul A Randazzo
Journal:  Biol Cell       Date:  2011-04       Impact factor: 4.458

2.  GTP-binding protein-like domain of AGAP1 is protein binding site that allosterically regulates ArfGAP protein catalytic activity.

Authors:  Ruibai Luo; Itoro O Akpan; Ryo Hayashi; Marek Sramko; Valarie Barr; Yoko Shiba; Paul A Randazzo
Journal:  J Biol Chem       Date:  2012-03-27       Impact factor: 5.157

3.  MiR-203 is downregulated in laryngeal squamous cell carcinoma and can suppress proliferation and induce apoptosis of tumours.

Authors:  Linli Tian; Minghua Li; Jingchun Ge; Yan Guo; Yanan Sun; Ming Liu; Hui Xiao
Journal:  Tumour Biol       Date:  2014-04-01

Review 4.  Regulation of actin cytoskeleton dynamics by Arf-family GTPases.

Authors:  Kenneth R Myers; James E Casanova
Journal:  Trends Cell Biol       Date:  2008-03-06       Impact factor: 20.808

Review 5.  Contribution of AZAP-Type Arf GAPs to cancer cell migration and invasion.

Authors:  Vi Luan Ha; Ruibai Luo; Zhongzhen Nie; Paul A Randazzo
Journal:  Adv Cancer Res       Date:  2008       Impact factor: 6.242

6.  Arf GTPase-activating protein ASAP1 interacts with Rab11 effector FIP3 and regulates pericentrosomal localization of transferrin receptor-positive recycling endosome.

Authors:  Hiroki Inoue; Vi Luan Ha; Rytis Prekeris; Paul A Randazzo
Journal:  Mol Biol Cell       Date:  2008-08-06       Impact factor: 4.138

7.  Autoinhibition of Arf GTPase-activating protein activity by the BAR domain in ASAP1.

Authors:  Xiaoying Jian; Patrick Brown; Peter Schuck; James M Gruschus; Andrea Balbo; Jenny E Hinshaw; Paul A Randazzo
Journal:  J Biol Chem       Date:  2008-11-18       Impact factor: 5.157

8.  Kinetic analysis of Arf GAP1 indicates a regulatory role for coatomer.

Authors:  Ruibai Luo; Paul A Randazzo
Journal:  J Biol Chem       Date:  2008-06-09       Impact factor: 5.157

9.  Arf GAP2 is positively regulated by coatomer and cargo.

Authors:  Ruibai Luo; Vi Luan Ha; Ryo Hayashi; Paul A Randazzo
Journal:  Cell Signal       Date:  2009-03-16       Impact factor: 4.315

10.  ARAP2 inhibits Akt independently of its effects on focal adhesions.

Authors:  Ruibai Luo; Pei-Wen Chen; Jean-Cheng Kuo; Lisa Jenkins; Xiaoying Jian; Clare M Waterman; Paul A Randazzo
Journal:  Biol Cell       Date:  2018-09-10       Impact factor: 4.458

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