Acaps Are Arf6 Gtpase-Activating Proteins That Function in the Cell Periphery

Jackson, Trevor; Brown, Fraser D.; Nie, Zhongzhen; Miura, Koichi; Foroni, Letizia; Sun, Jianlan; Hsu, Victor; Donaldson, Julie G.; Randazzo, Paul A.

doi:10.1083/jcb.151.3.627

Cited by 177 publications

(181 citation statements)

References 57 publications

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“…8C; Koizumi et al, 2005). The partial localization of AGD1 to FM4-64-labeled bodies that we observed here is consistent with the endosomal localization of the closely related animal AZAPs (Jackson et al, 2000;Nie et al, 2002). The differences in localization, domain organization, and possibly ARF substrate preference between AGD1 and AGD10 could likely explain the different nature of tip growth defects caused by their respective mutants.…”

Section: Discussionsupporting

confidence: 73%

“…For instance, the PH domain of class I ARF-GAPs, as demonstrated in the closely related AGD3, binds to phosphatidylinositol-4,5-bisphosphate (Koizumi et al, 2005). In mammalian systems, GAP activity of the AZAP-type ARF-GAPs is stimulated by phosphoinositide binding to the PH domain (Jackson et al, 2000). In this regard, overexpression or down-regulation of a type B phosphatidylinositol-4-phosphate 5-kinase 3, which regulates endogenous phosphatidylinositol-4,5-bisphosphate levels, leads to deformed root hairs (Kusano et al, 2008;Stenzel et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

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A Class I ADP-Ribosylation Factor GTPase-Activating Protein Is Critical for Maintaining Directional Root Hair Growth in Arabidopsis

et al. 2008

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Membrane trafficking and cytoskeletal dynamics are important cellular processes that drive tip growth in root hairs. These processes interact with a multitude of signaling pathways that allow for the efficient transfer of information to specify the direction in which tip growth occurs. Here, we show that AGD1, a class I ADP ribosylation factor GTPase-activating protein, is important for maintaining straight growth in Arabidopsis (Arabidopsis thaliana) root hairs, since mutations in the AGD1 gene resulted in wavy root hair growth. Live cell imaging of growing agd1 root hairs revealed bundles of endoplasmic microtubules and actin filaments extending into the extreme tip. The wavy phenotype and pattern of cytoskeletal distribution in root hairs of agd1 partially resembled that of mutants in an armadillo repeat-containing kinesin (ARK1). Root hairs of double agd1 ark1 mutants were more severely deformed compared with single mutants. Organelle trafficking as revealed by a fluorescent Golgi marker was slightly inhibited, and Golgi stacks frequently protruded into the extreme root hair apex of agd1 mutants. Transient expression of green fluorescent protein-AGD1 in tobacco (Nicotiana tabacum) epidermal cells labeled punctate bodies that partially colocalized with the endocytic marker FM4-64, while ARK1-yellow fluorescent protein associated with microtubules. Brefeldin A rescued the phenotype of agd1, indicating that the altered activity of an AGD1-dependent ADP ribosylation factor contributes to the defective growth, organelle trafficking, and cytoskeletal organization of agd1 root hairs. We propose that AGD1, a regulator of membrane trafficking, and ARK1, a microtubule motor, are components of converging signaling pathways that affect cytoskeletal organization to specify growth orientation in Arabidopsis root hairs.

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Section: Discussionsupporting

confidence: 73%

Section: Discussionmentioning

confidence: 99%

A Class I ADP-Ribosylation Factor GTPase-Activating Protein Is Critical for Maintaining Directional Root Hair Growth in Arabidopsis

et al. 2008

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“…ASAP and ACAP constructs are described in Brown et al (1998) and Jackson et al (2000). FIP constructs are described in Prekeris et al (2001) and were kindly provided by Dr. G. W. Gould (University of Glasgow, Glasgow, United Kingdom).…”

Section: Plasmids and Antibodiesmentioning

confidence: 99%

Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Inoue

Prekeris

et al. 2008

MBoC

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ADP-ribosylation factors (Arfs) and Arf GTPase-activating proteins (GAPs) are key regulators of membrane trafficking and the actin cytoskeleton. The Arf GAP ASAP1 contains an N-terminal BAR domain, which can induce membrane tubulation. Here, we report that the BAR domain of ASAP1 can also function as a protein binding site. Two-hybrid screening identified FIP3, which is a putative Arf6-and Rab11-effector, as a candidate ASAP1 BAR domain-binding protein. Both coimmunoprecipitation and in vitro pulldown assays confirmed that ASAP1 directly binds to FIP3 through its BAR domain. ASAP1 formed a ternary complex with Rab11 through FIP3. FIP3 binding to the BAR domain stimulated ASAP1 GAP activity against Arf1, but not Arf6. ASAP1 colocalized with FIP3 in the pericentrosomal endocytic recycling compartment. Depletion of ASAP1 or FIP3 by small interfering RNA changed the localization of transferrin receptor, which is a marker of the recycling endosome, in HeLa cells. 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. INTRODUCTIONArf family GTP-binding proteins and their GTPase-activating proteins (Arf GAPs) play crucial roles for membrane traffic and actin remodeling (D'Souza-Schorey and Chavrier, 2006;Gillingham and Munro, 2007). Arf GAPs share the same catalytic domain, the Arf GAP domain, which is responsible for GTP hydrolysis. In humans, 31 genes encoding proteins with Arf GAP domains have been found. They are classified into several subfamilies based on their domain structures Inoue and Randazzo, 2007). Three subfamilies, ArfGAPs, SMAPs, and GITs, have an Arf GAP domain at the N-terminus of the molecules. In contrast, the others, which are called AZAP-family Arf GAPs, contain an Arf GAP domain following a pleckstrin homology (PH) domain in the middle of the protein. They are subdivided into four subfamilies, ASAPs, ACAPs, ARAPs, and AGAPs.ASAP1 is one of the best-characterized Arf GAPs. In addition to PH and Arf GAP domains, ASAP1 contains an N-terminal Bin, Amphiphysin, and Rvs167/Rvs161 (BAR) domain and, in the C-terminal half of the protein, a proline (Pro)-rich domain and Src homology 3 (SH3) domain. Other ASAP isoforms, ASAP2 and ASAP3, have similar domain structures and high homology, especially in the Arf GAP domains, although ASAP3 lacks C-terminal SH3 domain (Ha et al., 2008). Through its Pro-rich and SH3 domains, ASAP1 interacts with a number of proteins, which are mainly adhesion-and actin cytoskeleton-related proteins including Src, focal adhesion kinase (FAK), Crk/CrkL, and cortactin (Brown et al., 1998;Liu et al., 2002;Oda et al., 2003;Onodera et al., 2005;Bharti et al., 2007). ASAP1 is a component of three integrated membrane/actin cytoskeleton structures: focal adhesions, circular dorsal ruffles (CDRs) and invadopodia/podosomes. ASAP1 associates with focal adhesions in fibroblasts . The focal adhesion localization depends on the interaction of ASAP1 with FA...

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“…In further support of the regulation of actin reorganization and cell migration by ARF GTPases, ARF guanine nucleotide exchange factors and ARF-GTPase activating proteins (ARF-GAP) regulate these processes as well (Franco et al, 1999;Turner et al, 1999;Di Cesare et al, 2000;Jackson et al, 2000;Kondo et al, 2000;Randazzo et al, 2000;Mazaki et al, 2001;Santy and Casanova, 2001;Uchida et al, 2001;West et al, 2001;Brown et al, 2002;Liu et al, 2002a;Manabe Ri et al, 2002). For example, the overexpression of various ARF-GAP proteins modulates the formation and/or turnover of focal adhesions (Di Cesare et al, 2000;Jackson et al, 2000;Kondo et al, 2000;Randazzo et al, 2000;Mazaki et al, 2001;Liu et al, 2002a) and the overexpression of an ARF guanine nucleotide exchange factor, ARNO, enhances the spreading and dispersal of epithelial cells (Santy and Casanova, 2001). In addition to their role as GAPs, ARF-GAP proteins may also influence signaling pathways through additional proteinprotein interactions.…”

Section: Introductionmentioning

confidence: 99%

Crk Associates with a Multimolecular Paxillin/GIT2/β-PIX Complex and Promotes Rac-dependent Relocalization of Paxillin to Focal Contacts

Lamorte

Rodrigues²,

Sangwan³

et al. 2003

MBoC

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We have previously demonstrated that the CrkII and CrkL adapter proteins are required for the spreading of epithelial colonies and the breakdown of adherens junctions in response to hepatocyte growth factor. When overexpressed, CrkII and CrkL promote lamellipodia formation, cell spreading, and the loss of epithelial adherens junctions in the absence of hepatocyte growth factor. The exact mechanism by which Crk proteins elicit these changes is unclear. We show that the overexpression of CrkII or CrkL, but not Src homology 2 or amino-terminal Src homology 3 domain mutant Crk proteins, promotes the relocalization of Paxillin to focal contacts throughout the cell and within lamellipodia in a Rac-dependent manner. In stable cell lines overexpressing CrkII, enhanced lamellipodia formation and cell spreading correlate with an increased association of CrkII with Paxillin, GIT2 (an ARF-GAP) and β-PIX (a Rac1 exchange factor). Mutants of Paxillin that fail to associate with Crk or GIT2, or do not target to focal adhesions inhibit Crk-dependent cell spreading and lamellipodia formation. We conclude from these studies that the association of Crk with Paxillin is important for the spreading of epithelial colonies, by influencing the recruitment of Paxillin to focal complexes and promoting the enhanced assembly of Paxillin/GIT2/β-PIX complexes.

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Acaps Are Arf6 Gtpase-Activating Proteins That Function in the Cell Periphery

Cited by 177 publications

References 57 publications

A Class I ADP-Ribosylation Factor GTPase-Activating Protein Is Critical for Maintaining Directional Root Hair Growth in Arabidopsis

A Class I ADP-Ribosylation Factor GTPase-Activating Protein Is Critical for Maintaining Directional Root Hair Growth in Arabidopsis

Arf GTPase-activating Protein ASAP1 Interacts with Rab11 Effector FIP3 and Regulates Pericentrosomal Localization of Transferrin Receptor–positive Recycling Endosome

Crk Associates with a Multimolecular Paxillin/GIT2/β-PIX Complex and Promotes Rac-dependent Relocalization of Paxillin to Focal Contacts

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